Structured Review

Difco brain heart infusion bhi broth
Protease activation in the extracellular protein fraction from P. <t>gingivalis</t> FLL93. P. gingivalis was grown to stationary phase (OD 600 of 1.3) in 1 liter of <t>BHI</t> broth supplemented with hemin and vitamin K. Acetone (37.5%)-precipitated proteins were mixed with 8 M urea and were incubated at 4°C for 1 h. The urea was slowly removed from the mixture by centrifugation (10,000 × g ) in a Millipore filtration unit with the addition of increasing volumes of 100 mM Tris-HCl buffer (pH 7.4). Activities for Rgp and Kgp were tested. Error bars indicate the standard errors of the means of three independent trials.
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1) Product Images from "The vimE Gene Downstream of vimA Is Independently Expressed and Is Involved in Modulating Proteolytic Activity in Porphyromonas gingivalis W83 "

Article Title: The vimE Gene Downstream of vimA Is Independently Expressed and Is Involved in Modulating Proteolytic Activity in Porphyromonas gingivalis W83

Journal: Infection and Immunity

doi: 10.1128/IAI.72.10.5555-5564.2004

Protease activation in the extracellular protein fraction from P. gingivalis FLL93. P. gingivalis was grown to stationary phase (OD 600 of 1.3) in 1 liter of BHI broth supplemented with hemin and vitamin K. Acetone (37.5%)-precipitated proteins were mixed with 8 M urea and were incubated at 4°C for 1 h. The urea was slowly removed from the mixture by centrifugation (10,000 × g ) in a Millipore filtration unit with the addition of increasing volumes of 100 mM Tris-HCl buffer (pH 7.4). Activities for Rgp and Kgp were tested. Error bars indicate the standard errors of the means of three independent trials.
Figure Legend Snippet: Protease activation in the extracellular protein fraction from P. gingivalis FLL93. P. gingivalis was grown to stationary phase (OD 600 of 1.3) in 1 liter of BHI broth supplemented with hemin and vitamin K. Acetone (37.5%)-precipitated proteins were mixed with 8 M urea and were incubated at 4°C for 1 h. The urea was slowly removed from the mixture by centrifugation (10,000 × g ) in a Millipore filtration unit with the addition of increasing volumes of 100 mM Tris-HCl buffer (pH 7.4). Activities for Rgp and Kgp were tested. Error bars indicate the standard errors of the means of three independent trials.

Techniques Used: Activation Assay, Incubation, Centrifugation, Filtration

Inactivation of vimE resulted in decreased proteolytic activity of P. gingivalis. P. gingivalis was grown to late log phase (OD 600 of 0.7 to 0.8) or stationary phase (OD 600 of 1.4 to 1.5) in BHI broth supplemented with yeast extract, hemin, and vitamin K. Activities against Rgp (A) and Kgp (B) were tested in whole-cell culture. The results shown are representative of three independent experiments in triplicate. E, exponential phase; L, stationary phase. Error bars indicate the standard errors of the means of three independent trials.
Figure Legend Snippet: Inactivation of vimE resulted in decreased proteolytic activity of P. gingivalis. P. gingivalis was grown to late log phase (OD 600 of 0.7 to 0.8) or stationary phase (OD 600 of 1.4 to 1.5) in BHI broth supplemented with yeast extract, hemin, and vitamin K. Activities against Rgp (A) and Kgp (B) were tested in whole-cell culture. The results shown are representative of three independent experiments in triplicate. E, exponential phase; L, stationary phase. Error bars indicate the standard errors of the means of three independent trials.

Techniques Used: Activity Assay, Cell Culture

Immunoreactivity of the RgpB proenzyme in P. gingivalis FLL93. Western blot analysis using specific RgpB proenzyme antibodies as probes was done on the extracellular fractions from P. gingivalis W83 (lane 1), FLL92 (lane 2), and FLL93 (lane 3). All lanes contained 20 μg of acetone (37.5%)-precipitated proteins from the supernatant fractions of cultures in BHI medium at exponential growth phase.
Figure Legend Snippet: Immunoreactivity of the RgpB proenzyme in P. gingivalis FLL93. Western blot analysis using specific RgpB proenzyme antibodies as probes was done on the extracellular fractions from P. gingivalis W83 (lane 1), FLL92 (lane 2), and FLL93 (lane 3). All lanes contained 20 μg of acetone (37.5%)-precipitated proteins from the supernatant fractions of cultures in BHI medium at exponential growth phase.

Techniques Used: Western Blot

2) Product Images from "LipA, a Tyrosine and Lipid Phosphatase Involved in the Virulence of Listeria monocytogenes ▿ ▿ †"

Article Title: LipA, a Tyrosine and Lipid Phosphatase Involved in the Virulence of Listeria monocytogenes ▿ ▿ †

Journal: Infection and Immunity

doi: 10.1128/IAI.05073-11

Expression of L. monocytogenes lipA in human blood. Transcriptional tiling maps of L. monocytogenes EGDe grown in BHI to exponential phase at 37°C (black dots) or in human blood at 37°C for 60 min (red dots) show normalized hybridization
Figure Legend Snippet: Expression of L. monocytogenes lipA in human blood. Transcriptional tiling maps of L. monocytogenes EGDe grown in BHI to exponential phase at 37°C (black dots) or in human blood at 37°C for 60 min (red dots) show normalized hybridization

Techniques Used: Expressing, Hybridization

3) Product Images from "Identification and Characterization of Di- and Tripeptide Transporter DtpT of Listeria monocytogenes EGD-e"

Article Title: Identification and Characterization of Di- and Tripeptide Transporter DtpT of Listeria monocytogenes EGD-e

Journal: Applied and Environmental Microbiology

doi: 10.1128/AEM.71.10.5771-5778.2005

Uptake of the Pro-[ 14 C]Ala peptide in L. monocytogenes EGD-e and L. monocytogenes Δ dtpT . Cells were grown in BHI to mid-exponential phase (OD 600 , 0.5) and washed twice in 240 mM sodium PIPES buffer (pH 6.0) containing 5 mM MgSO 4 . Assays of Pro-[
Figure Legend Snippet: Uptake of the Pro-[ 14 C]Ala peptide in L. monocytogenes EGD-e and L. monocytogenes Δ dtpT . Cells were grown in BHI to mid-exponential phase (OD 600 , 0.5) and washed twice in 240 mM sodium PIPES buffer (pH 6.0) containing 5 mM MgSO 4 . Assays of Pro-[

Techniques Used:

4) Product Images from "A GntR Family Transcription Factor in Streptococcus mutans Regulates Biofilm Formation and Expression of Multiple Sugar Transporter Genes"

Article Title: A GntR Family Transcription Factor in Streptococcus mutans Regulates Biofilm Formation and Expression of Multiple Sugar Transporter Genes

Journal: Frontiers in Microbiology

doi: 10.3389/fmicb.2018.03224

Determination of growth curves of S. mutans UA159, S. mutans Δ stsR , and Δ stsR/pDL278-stsR . S. mutans UA159, S. mutans Δ stsR , and Δ stsR/pDL278-stsR strains were cultivated in BHI to mid-exponential phase and then diluted into (A) fresh BHI broth or (B) TV base medium supplemented with either 10 mM (limiting) or 100 mM (excess) sucrose, glucose, or lactose. Growth curves were monitored with a Multiskan Spectrum (Thermo, Multiskan Go, United States), and the OD 600 was measured in 1 h intervals. (A) For CFU counts, after diluted, the bacteria were cultured at 37°C for 1, 4, 8, and 12 h. Then bacterial suspension was serially diluted in BHI and plated on BHI agar plates. CFU values were calculated after the plates were incubated anaerobically at 37°C for 48 h. Error bars represent standard deviations based on results from at least three biological replicates.
Figure Legend Snippet: Determination of growth curves of S. mutans UA159, S. mutans Δ stsR , and Δ stsR/pDL278-stsR . S. mutans UA159, S. mutans Δ stsR , and Δ stsR/pDL278-stsR strains were cultivated in BHI to mid-exponential phase and then diluted into (A) fresh BHI broth or (B) TV base medium supplemented with either 10 mM (limiting) or 100 mM (excess) sucrose, glucose, or lactose. Growth curves were monitored with a Multiskan Spectrum (Thermo, Multiskan Go, United States), and the OD 600 was measured in 1 h intervals. (A) For CFU counts, after diluted, the bacteria were cultured at 37°C for 1, 4, 8, and 12 h. Then bacterial suspension was serially diluted in BHI and plated on BHI agar plates. CFU values were calculated after the plates were incubated anaerobically at 37°C for 48 h. Error bars represent standard deviations based on results from at least three biological replicates.

Techniques Used: Cell Culture, Incubation

5) Product Images from "The TIR Domain Containing Locus of Enterococcus faecalis Is Predominant among Urinary Tract Infection Isolates and Downregulates Host Inflammatory Response"

Article Title: The TIR Domain Containing Locus of Enterococcus faecalis Is Predominant among Urinary Tract Infection Isolates and Downregulates Host Inflammatory Response

Journal: International Journal of Microbiology

doi: 10.1155/2014/918143

TcpF is constitutively transcribed in E . faecalis Symbioflor 1. (a) Full length mRNA transcript of tcpF in E . faecalis Symbioflor 1. Reverse transcription was performed with primer E.f.seq.2. PCR primers E.f.seq. 8/15: 457 bp, primers E.f.seq. 8/14: 640 bp, primers E.f.seq. 8/17a: 671 bp, and primers E.f.seq. 8/1: 680 bp. (b) TcpF mRNA is transcribed upon growth in BHI medium and upon infection on CaCo cells. PCR primers E.f.seq. 7/6: 300 bp. Reverse transcriptase minus (RT-) reactions served as negative control.
Figure Legend Snippet: TcpF is constitutively transcribed in E . faecalis Symbioflor 1. (a) Full length mRNA transcript of tcpF in E . faecalis Symbioflor 1. Reverse transcription was performed with primer E.f.seq.2. PCR primers E.f.seq. 8/15: 457 bp, primers E.f.seq. 8/14: 640 bp, primers E.f.seq. 8/17a: 671 bp, and primers E.f.seq. 8/1: 680 bp. (b) TcpF mRNA is transcribed upon growth in BHI medium and upon infection on CaCo cells. PCR primers E.f.seq. 7/6: 300 bp. Reverse transcriptase minus (RT-) reactions served as negative control.

Techniques Used: Polymerase Chain Reaction, Infection, Negative Control

TcpF suppresses TNF- α induction. (a) E. faecalis Symbioflor 1 and its isogenic tcpF deletion mutant Symbioflor 1 Δ tcpF show identical growth rate. Fresh culture was started from overnight culture 1 : 25 in BHI at 37°C and 100 rpm. Optical density at 600 nm (OD 600 ) at indicated time points. (b) RAW264.7 macrophages were infected for 6 h with E. faecalis Symbioflor 1 and E . faecalis Symbioflor 1 Δ tcpF at indicated moi. NC: negative control—uninfected macrophages. Error bars represent s.d. ( n = 4). Student's t -test: ∗∗∗ P
Figure Legend Snippet: TcpF suppresses TNF- α induction. (a) E. faecalis Symbioflor 1 and its isogenic tcpF deletion mutant Symbioflor 1 Δ tcpF show identical growth rate. Fresh culture was started from overnight culture 1 : 25 in BHI at 37°C and 100 rpm. Optical density at 600 nm (OD 600 ) at indicated time points. (b) RAW264.7 macrophages were infected for 6 h with E. faecalis Symbioflor 1 and E . faecalis Symbioflor 1 Δ tcpF at indicated moi. NC: negative control—uninfected macrophages. Error bars represent s.d. ( n = 4). Student's t -test: ∗∗∗ P

Techniques Used: Mutagenesis, Infection, Negative Control

6) Product Images from "The Streptococcus mutans Cid and Lrg systems modulate virulence traits in response to multiple environmental signals"

Article Title: The Streptococcus mutans Cid and Lrg systems modulate virulence traits in response to multiple environmental signals

Journal: Microbiology

doi: 10.1099/mic.0.039586-0

Growth curves of S. mutans wild-type and its lrg (a) and cid (b) derivatives under oxidative stress. Strains were grown in BHI medium containing 10 mM paraquat under anaerobic conditions. Growth was monitored in a Bioscreen C system that was set to shake for 15 s every 30 min. For anaerobic growth, sterile mineral oil (50 μl) was placed on top of the broth cultures. The results are representative of two independent experiments.
Figure Legend Snippet: Growth curves of S. mutans wild-type and its lrg (a) and cid (b) derivatives under oxidative stress. Strains were grown in BHI medium containing 10 mM paraquat under anaerobic conditions. Growth was monitored in a Bioscreen C system that was set to shake for 15 s every 30 min. For anaerobic growth, sterile mineral oil (50 μl) was placed on top of the broth cultures. The results are representative of two independent experiments.

Techniques Used:

7) Product Images from "Gingipain RgpB Is Excreted as a Proenzyme in the vimA-Defective Mutant Porphyromonas gingivalis FLL92 "

Article Title: Gingipain RgpB Is Excreted as a Proenzyme in the vimA-Defective Mutant Porphyromonas gingivalis FLL92

Journal: Infection and Immunity

doi: 10.1128/IAI.71.7.3740-3747.2003

Western blot analysis of the urea-activated fraction using antibodies against RgpB. All lanes contained 20 μg of acetone (37.5%)-precipitated proteins from the supernatant fractions of P. gingivalis FLL92 cultures grown in BHI medium at exponential growth phases. The membrane was reacted with antiserum raised in rabbits against RgpB. Lanes: 1, FLL92 exponential-growth-phase extracellular proteins; 2, FLL92 exponential-growth-phase extracellular proteins treated with urea (see the text).
Figure Legend Snippet: Western blot analysis of the urea-activated fraction using antibodies against RgpB. All lanes contained 20 μg of acetone (37.5%)-precipitated proteins from the supernatant fractions of P. gingivalis FLL92 cultures grown in BHI medium at exponential growth phases. The membrane was reacted with antiserum raised in rabbits against RgpB. Lanes: 1, FLL92 exponential-growth-phase extracellular proteins; 2, FLL92 exponential-growth-phase extracellular proteins treated with urea (see the text).

Techniques Used: Western Blot

Protease activation in the extracellular protein fraction from P. gingivalis FLL92. P. gingivalis was grown to late log phase (OD 660 of 0.8) in 1 liter of BHI broth supplemented with hemin and vitamin K. Acetone (37.5%)-precipitated proteins were mixed with 8 M urea and incubated at 4°C for 1 h. The urea was slowly removed from the mixture by centrifugation (10,000 × g ). The results shown are representative of four independent experiments.
Figure Legend Snippet: Protease activation in the extracellular protein fraction from P. gingivalis FLL92. P. gingivalis was grown to late log phase (OD 660 of 0.8) in 1 liter of BHI broth supplemented with hemin and vitamin K. Acetone (37.5%)-precipitated proteins were mixed with 8 M urea and incubated at 4°C for 1 h. The urea was slowly removed from the mixture by centrifugation (10,000 × g ). The results shown are representative of four independent experiments.

Techniques Used: Activation Assay, Incubation, Centrifugation

Detection of proteolytic activity in casein-conjugated polyacrylamide gel. All lanes contained 20 μg of acetone (37.5%)-precipitated proteins from the supernatant fractions of cultures in BHI medium at exponential growth phases. Samples were solubilized at room temperature for 10 min in a Tris-glycine SDS sample buffer (Invitrogen) prior to electrophoresis. Lanes: 1, W83; 2, FLL92. The arrow indicates a 48-kDa proteolytic band present in the FLL92 exponential-growth-phase extracellular proteins.
Figure Legend Snippet: Detection of proteolytic activity in casein-conjugated polyacrylamide gel. All lanes contained 20 μg of acetone (37.5%)-precipitated proteins from the supernatant fractions of cultures in BHI medium at exponential growth phases. Samples were solubilized at room temperature for 10 min in a Tris-glycine SDS sample buffer (Invitrogen) prior to electrophoresis. Lanes: 1, W83; 2, FLL92. The arrow indicates a 48-kDa proteolytic band present in the FLL92 exponential-growth-phase extracellular proteins.

Techniques Used: Activity Assay, Electrophoresis

SDS-PAGE of acetone-precipitated P. gingivalis extracellular proteins. Proteins in the supernatant fractions of cultures at different growth phases in BHI medium were precipitated with 37.5% (A) or 60% (B) acetone. The fractions were solubilized at 72°C in reducing buffer. NuPAGE bis-Tris gels (4 to 12%) were stained with Simply Blue Safe stain. Lanes: 1, W83 at exponential phase; 2, FLL92 at exponential phase; 3, W83 at stationary phase; and 4, FLL92 at stationary phase. The molecular mass markers (in kilodaltons) are indicated on the left. Each lane contains 20 μg of protein. It is noteworthy that the 64-kDa band was observed in abundance when 37.5% acetone instead of 60% acetone was used for the precipitation.
Figure Legend Snippet: SDS-PAGE of acetone-precipitated P. gingivalis extracellular proteins. Proteins in the supernatant fractions of cultures at different growth phases in BHI medium were precipitated with 37.5% (A) or 60% (B) acetone. The fractions were solubilized at 72°C in reducing buffer. NuPAGE bis-Tris gels (4 to 12%) were stained with Simply Blue Safe stain. Lanes: 1, W83 at exponential phase; 2, FLL92 at exponential phase; 3, W83 at stationary phase; and 4, FLL92 at stationary phase. The molecular mass markers (in kilodaltons) are indicated on the left. Each lane contains 20 μg of protein. It is noteworthy that the 64-kDa band was observed in abundance when 37.5% acetone instead of 60% acetone was used for the precipitation.

Techniques Used: SDS Page, Staining

Western immunoblot analysis of the extracellular proteins from P. gingivalis by using specific anti-Rgp and anti-Kgp antibodies as probes. All lanes contained 20 μg of acetone (37.5%)-precipitated proteins from the supernatant fractions of cultures in BHI medium at different growth phases. The membrane was reacted with antiserum raised in rabbits or chickens against the Arg-X- and Lys-X-specific protease from P. gingivalis . The secondary antibody was goat anti-rabbit or anti-chicken immunoglobulin G-horseradish peroxidase conjugate.(Zymed Laboratories Inc.). Reactions were done with rabbit anti-RgpB (A), rabbit anti-RgpA (B), and chicken anti-Kgp (C). Lanes: 1, W83 at exponential phase; 2, FLL92 at exponential phase; 3, W83 at stationary phase; 4, FLL92 at stationary phase. It is noteworthy that the 64-kDa band was identified as the RgpB proenzyme by mass spectrometry (see the text).
Figure Legend Snippet: Western immunoblot analysis of the extracellular proteins from P. gingivalis by using specific anti-Rgp and anti-Kgp antibodies as probes. All lanes contained 20 μg of acetone (37.5%)-precipitated proteins from the supernatant fractions of cultures in BHI medium at different growth phases. The membrane was reacted with antiserum raised in rabbits or chickens against the Arg-X- and Lys-X-specific protease from P. gingivalis . The secondary antibody was goat anti-rabbit or anti-chicken immunoglobulin G-horseradish peroxidase conjugate.(Zymed Laboratories Inc.). Reactions were done with rabbit anti-RgpB (A), rabbit anti-RgpA (B), and chicken anti-Kgp (C). Lanes: 1, W83 at exponential phase; 2, FLL92 at exponential phase; 3, W83 at stationary phase; 4, FLL92 at stationary phase. It is noteworthy that the 64-kDa band was identified as the RgpB proenzyme by mass spectrometry (see the text).

Techniques Used: Western Blot, Mass Spectrometry

8) Product Images from "Moraxella catarrhalis AcrAB-OprM Efflux Pump Contributes to Antimicrobial Resistance and Is Enhanced during Cold Shock Response"

Article Title: Moraxella catarrhalis AcrAB-OprM Efflux Pump Contributes to Antimicrobial Resistance and Is Enhanced during Cold Shock Response

Journal: Antimicrobial Agents and Chemotherapy

doi: 10.1128/AAC.03727-14

(A) Growth curves for wild-type O35E M. catarrhalis strain and its isogenic knockout strains in BHI medium at 37°C. (B) Expression of the mutated gene in each strain was determined by RT-PCR. For each strain, the product of RT-PCR using primers specific for acrA , acrB , oprM , or 16S rRNA, as a control gene, is shown. Ctrl indicates control reactions with no cDNA templates.
Figure Legend Snippet: (A) Growth curves for wild-type O35E M. catarrhalis strain and its isogenic knockout strains in BHI medium at 37°C. (B) Expression of the mutated gene in each strain was determined by RT-PCR. For each strain, the product of RT-PCR using primers specific for acrA , acrB , oprM , or 16S rRNA, as a control gene, is shown. Ctrl indicates control reactions with no cDNA templates.

Techniques Used: Knock-Out, Expressing, Reverse Transcription Polymerase Chain Reaction

9) Product Images from "Identification of a bacteriocin and its cognate immunity factor expressed by Moraxella catarrhalis"

Article Title: Identification of a bacteriocin and its cognate immunity factor expressed by Moraxella catarrhalis

Journal: BMC Microbiology

doi: 10.1186/1471-2180-9-207

Killing of M. catarrhalis O35E by M. catarrhalis E22 carrying pLQ510 . Test strains and indicator strains were grown on BHI agar plates as described in Materials and Methods. Panels: A, O35E test strain on O35E indicator; B, O35E test strain on E22 indicator; C, E22 test strain on O35E indicator; D, E22 test strain on E22 indicator. The white arrow in panel C indicates the zone of killing of the indicator strain by the test strain. Panel E, schematic of pLQ510 indicating the four ORFs located in the mcb locus. The nucleotide sequence of pLQ510 is available at GenBank under accession no. AF129811 . The positions of the restriction sites used to insert kanamycin resistance cassettes in the mcbB and mcbC genes are indicated.
Figure Legend Snippet: Killing of M. catarrhalis O35E by M. catarrhalis E22 carrying pLQ510 . Test strains and indicator strains were grown on BHI agar plates as described in Materials and Methods. Panels: A, O35E test strain on O35E indicator; B, O35E test strain on E22 indicator; C, E22 test strain on O35E indicator; D, E22 test strain on E22 indicator. The white arrow in panel C indicates the zone of killing of the indicator strain by the test strain. Panel E, schematic of pLQ510 indicating the four ORFs located in the mcb locus. The nucleotide sequence of pLQ510 is available at GenBank under accession no. AF129811 . The positions of the restriction sites used to insert kanamycin resistance cassettes in the mcbB and mcbC genes are indicated.

Techniques Used: Sequencing

10) Product Images from "Contribution of a Thickened Cell Wall and Its Glutamine Nonamidated Component to the Vancomycin Resistance Expressed by Staphylococcus aureus Mu50"

Article Title: Contribution of a Thickened Cell Wall and Its Glutamine Nonamidated Component to the Vancomycin Resistance Expressed by Staphylococcus aureus Mu50

Journal: Antimicrobial Agents and Chemotherapy

doi:

Comparison of cell-wall thickness and TRG in the presence of vancomycin among the test strains after cultivation (or incubation) in BHI medium and RM. (A and B) Comparison of cell-wall thicknesses of the test strains cultivated in BHI medium (A) and after further incubation in RM (B). The values under each panel are mean ± SD thicknesses (in nanometers). The bacterial cultures at an OD 600 of 0.7 in BHI medium were divided into two portions. One of them was directly subjected to electron microscopy (A). The other portion was washed twice with RMg−, further incubated in RM at 37°C for 2 h, and then subjected to electron microscopic examination (B). (C and D) TRG was compared among the cell preparations shown in panels A (C) and B (D). (C) Vancomycin was added to a final concentration of 30 mg/liter when the culture (inoculated with the cells shown in p1anel A at an initial concentration of 10 6 cells/ml) reached an OD 600 of 0.4. (D) Cells incubated in RM were spun down and resuspended in BHI medium containing vancomycin at 30 mg/liter.
Figure Legend Snippet: Comparison of cell-wall thickness and TRG in the presence of vancomycin among the test strains after cultivation (or incubation) in BHI medium and RM. (A and B) Comparison of cell-wall thicknesses of the test strains cultivated in BHI medium (A) and after further incubation in RM (B). The values under each panel are mean ± SD thicknesses (in nanometers). The bacterial cultures at an OD 600 of 0.7 in BHI medium were divided into two portions. One of them was directly subjected to electron microscopy (A). The other portion was washed twice with RMg−, further incubated in RM at 37°C for 2 h, and then subjected to electron microscopic examination (B). (C and D) TRG was compared among the cell preparations shown in panels A (C) and B (D). (C) Vancomycin was added to a final concentration of 30 mg/liter when the culture (inoculated with the cells shown in p1anel A at an initial concentration of 10 6 cells/ml) reached an OD 600 of 0.4. (D) Cells incubated in RM were spun down and resuspended in BHI medium containing vancomycin at 30 mg/liter.

Techniques Used: Incubation, Electron Microscopy, Concentration Assay

11) Product Images from "LuxS Is Required for Persistent Pneumococcal Carriage and Expression of Virulence and Biosynthesis Genes "

Article Title: LuxS Is Required for Persistent Pneumococcal Carriage and Expression of Virulence and Biosynthesis Genes

Journal: Infection and Immunity

doi: 10.1128/IAI.72.5.2964-2975.2004

Cell-free supernatants harvested from the luxS mutant or D39 are unable to complement the transcriptional defect in the Δ luxS mutant. RNA was isolated at time zero from D39 or the Δ luxS mutant after incubation with either BHI medium or various cell-free supernatants (in parentheses) isolated from mutant and parent cultures at two different growth phases. RNA was prepared from three independently collected sets of supernatants, and the real-time assays were carried out in triplicate. The relative quantity of accD transcript from each strain under each condition was determined, and the values were normalized to the quantity of rpoB transcript. The average relative value under each condition is shown.
Figure Legend Snippet: Cell-free supernatants harvested from the luxS mutant or D39 are unable to complement the transcriptional defect in the Δ luxS mutant. RNA was isolated at time zero from D39 or the Δ luxS mutant after incubation with either BHI medium or various cell-free supernatants (in parentheses) isolated from mutant and parent cultures at two different growth phases. RNA was prepared from three independently collected sets of supernatants, and the real-time assays were carried out in triplicate. The relative quantity of accD transcript from each strain under each condition was determined, and the values were normalized to the quantity of rpoB transcript. The average relative value under each condition is shown.

Techniques Used: Mutagenesis, Isolation, Incubation

12) Product Images from "Protective Role of the PG1036-PG1037-PG1038 Operon in Oxidative Stress in Porphyromonas gingivalis W83"

Article Title: Protective Role of the PG1036-PG1037-PG1038 Operon in Oxidative Stress in Porphyromonas gingivalis W83

Journal: PLoS ONE

doi: 10.1371/journal.pone.0069645

UV sensitivity of P. gingivalis mutants. P. gingivalis strains W83, FLL144, FLL145 and FLL146 were grown to mid log phase (OD 600 of 0.6) spread on BHI plates then subjected to irradiation at increasing doses (0 µJ, 500 µJ and 1000 µJ) of UV in a Stratalinker 2400 (Stratagene, La Jolla, CA). **P≤0.01, *P≤0.05.
Figure Legend Snippet: UV sensitivity of P. gingivalis mutants. P. gingivalis strains W83, FLL144, FLL145 and FLL146 were grown to mid log phase (OD 600 of 0.6) spread on BHI plates then subjected to irradiation at increasing doses (0 µJ, 500 µJ and 1000 µJ) of UV in a Stratalinker 2400 (Stratagene, La Jolla, CA). **P≤0.01, *P≤0.05.

Techniques Used: Irradiation

Proteolytic activity of P. gingivalis mutants. P. gingivalis strains were grown to late log phase OD 600 of 1.2 in 50 ml of BHI broth supplemented with hemin and vitamin K. Panel A ; whole cell culture was analyzed for Rgp (BAPNA) activity (**P≤0.01). Panel B ; whole cell culture was analyzed for Kgp (ALNA) activity. The results shown are representative of 3 independent experiments performed in triplicate (*P≤0.01).
Figure Legend Snippet: Proteolytic activity of P. gingivalis mutants. P. gingivalis strains were grown to late log phase OD 600 of 1.2 in 50 ml of BHI broth supplemented with hemin and vitamin K. Panel A ; whole cell culture was analyzed for Rgp (BAPNA) activity (**P≤0.01). Panel B ; whole cell culture was analyzed for Kgp (ALNA) activity. The results shown are representative of 3 independent experiments performed in triplicate (*P≤0.01).

Techniques Used: Activity Assay, Cell Culture

Sensitivity of P. gingivalis mutants to hydrogen peroxide. P. gingivalis was grown to early log phase (OD 600 of 0.2) in BHI broth. 0.25 mM H 2 O 2 was then added to the cell cultures and further incubated over 30 h. Cell cultures without H 2 O 2 were used as controls. The greatest observable difference in growth rate and response to H 2 O 2 was seen at 21 h (exponential phase of the growth curve). The results shown are representative of 3 independent experiments each in triplicate. Error bars represent standard error of the mean. **P≤0.01. Asterisks without brackets represent comparisons to treated controls.
Figure Legend Snippet: Sensitivity of P. gingivalis mutants to hydrogen peroxide. P. gingivalis was grown to early log phase (OD 600 of 0.2) in BHI broth. 0.25 mM H 2 O 2 was then added to the cell cultures and further incubated over 30 h. Cell cultures without H 2 O 2 were used as controls. The greatest observable difference in growth rate and response to H 2 O 2 was seen at 21 h (exponential phase of the growth curve). The results shown are representative of 3 independent experiments each in triplicate. Error bars represent standard error of the mean. **P≤0.01. Asterisks without brackets represent comparisons to treated controls.

Techniques Used: Incubation

13) Product Images from "A hag Mutant of Moraxella catarrhalis Strain O35E Is Deficient in Hemagglutination, Autoagglutination, and Immunoglobulin D-Binding Activities "

Article Title: A hag Mutant of Moraxella catarrhalis Strain O35E Is Deficient in Hemagglutination, Autoagglutination, and Immunoglobulin D-Binding Activities

Journal: Infection and Immunity

doi: 10.1128/IAI.70.8.4523-4533.2002

Autoagglutination ability of wild-type and mutant strains of M. catarrhalis O35E. Cells grown on BHI agar plates overnight were suspended in PBS, and the change in turbidity over time was measured.
Figure Legend Snippet: Autoagglutination ability of wild-type and mutant strains of M. catarrhalis O35E. Cells grown on BHI agar plates overnight were suspended in PBS, and the change in turbidity over time was measured.

Techniques Used: Mutagenesis

14) Product Images from "Differential response of Porphyromonas gingivalis to varying levels and duration of hydrogen peroxide-induced oxidative stress"

Article Title: Differential response of Porphyromonas gingivalis to varying levels and duration of hydrogen peroxide-induced oxidative stress

Journal: Microbiology

doi: 10.1099/mic.0.056416-0

Sensitivity of P. gingivalis strains W83, FLL363 and FLL393 to H 2 O 2 . Strains were grown to early exponential phase (OD 600 ~0.2) in BHI broth, 0.25 mM of H 2 O 2 was then added to the cultures, and the cultures were further incubated for 36 h. Cell cultures
Figure Legend Snippet: Sensitivity of P. gingivalis strains W83, FLL363 and FLL393 to H 2 O 2 . Strains were grown to early exponential phase (OD 600 ~0.2) in BHI broth, 0.25 mM of H 2 O 2 was then added to the cultures, and the cultures were further incubated for 36 h. Cell cultures

Techniques Used: Incubation

15) Product Images from "Involvement of extracytoplasmic function sigma factors in virulence regulation in Porphyromonas gingivalis W83"

Article Title: Involvement of extracytoplasmic function sigma factors in virulence regulation in Porphyromonas gingivalis W83

Journal: FEMS microbiology letters

doi: 10.1111/j.1574-6968.2010.02093.x

(a) Proteolytic activity of ECF sigma factor mutants. P. gingivalis strains were grown to stationary phase in BHI media supplemented with hemin and vitamin K. Activities against Rgp or Kgp were tested in whole cell culture. The gingipain activities were
Figure Legend Snippet: (a) Proteolytic activity of ECF sigma factor mutants. P. gingivalis strains were grown to stationary phase in BHI media supplemented with hemin and vitamin K. Activities against Rgp or Kgp were tested in whole cell culture. The gingipain activities were

Techniques Used: Activity Assay, Cell Culture

16) Product Images from "Identification of the agr Locus of Listeria monocytogenes: Role in Bacterial Virulence "

Article Title: Identification of the agr Locus of Listeria monocytogenes: Role in Bacterial Virulence

Journal: Infection and Immunity

doi: 10.1128/IAI.71.8.4463-4471.2003

Invasiveness of the agrA mutant was evaluated in two different cell lines, Caco-2 cells (A) and HepG-2 cells (B), and in bone marrow macrophages (C). Cell monolayers were incubated for 1 h at 37°C with approximately 100 bacteria per cell. After washing, the cells were reincubated for 4 h in fresh culture medium. At 2, 3, and 4 h, the cells were washed again and lysed and viable bacteria were counted on BHI plates. Values and error bars represent the means and standard deviations of the numbers of bacteria per well (three wells per assay, two different assays). •, EGD-e; □, agrA mutant.
Figure Legend Snippet: Invasiveness of the agrA mutant was evaluated in two different cell lines, Caco-2 cells (A) and HepG-2 cells (B), and in bone marrow macrophages (C). Cell monolayers were incubated for 1 h at 37°C with approximately 100 bacteria per cell. After washing, the cells were reincubated for 4 h in fresh culture medium. At 2, 3, and 4 h, the cells were washed again and lysed and viable bacteria were counted on BHI plates. Values and error bars represent the means and standard deviations of the numbers of bacteria per well (three wells per assay, two different assays). •, EGD-e; □, agrA mutant.

Techniques Used: Mutagenesis, Incubation

Genetic organization of the agr locus and transcriptional analysis. (A) Genetic organization of the agr locus. (Upper panel) agr locus of S. aureus . The grey arrows indicate the orientations and approximate sizes of the different genes. The dotted lines ending in arrows indicate the two main divergent transcripts RNAII and RNAIII. To the right, a schematic representation of the various components of the agr locus is shown, with letters representing the proteins encoded A, AgrA; B, AgrB; C, AgrC; D, AgrD; asterisk, phosphorylated group; P2 and P3, promoters of RNAII and RNAIII, respectively. (Lower panel) agr locus of L. monocytogenes . The arrows indicate approximate sizes and orientations of the different genes. The predicted length of each protein is indicated below (in amino acids [aas]). The stop sign-shaped symbols indicate putative transcription terminators. The values in percentages below agrB , agrC , and agrA indicate the percentage of amino acid identity between the L. monocytogenes and S. aureus orthologues encoded by the genes of the agr loci. Numbers between parentheses indicate the sizes (in base pairs) of the intergenic regions. The site of Tn 1545 insertion is represented by an inverted black triangle. (B) Transcriptional analysis by RT-PCR. The dotted lines enclosed by arrows in the lower half of panel A indicate the positions of the primers and PCR products used in the RT-PCR analysis. The amplified products, numbered 1 to 5, were subjected to Tris acetate-EDTA-agarose gel electrophoresis. The arrows preceded by numbers (in kilobases) to the left of the panel correspond to the molecular weight (MW) DNA ladder. (C) Expression of the agr genes in stationary (Stat) and exponential (Exp) phases. The expression was measured by real-time quantitative RT-PCR. The amount of agr mRNA relative to that of the normalizing gene gyr (upper panel) and the 16S gene (lower panel) was determined by real-time quantitative RT-PCR with bacteria grown in BHI in the exponential or stationary phase of growth. The amounts of gyr mRNA and 16S rRNA were constant under these conditions (data not shown). The values shown are means of results from three assays; the error bars indicate the standard deviations.
Figure Legend Snippet: Genetic organization of the agr locus and transcriptional analysis. (A) Genetic organization of the agr locus. (Upper panel) agr locus of S. aureus . The grey arrows indicate the orientations and approximate sizes of the different genes. The dotted lines ending in arrows indicate the two main divergent transcripts RNAII and RNAIII. To the right, a schematic representation of the various components of the agr locus is shown, with letters representing the proteins encoded A, AgrA; B, AgrB; C, AgrC; D, AgrD; asterisk, phosphorylated group; P2 and P3, promoters of RNAII and RNAIII, respectively. (Lower panel) agr locus of L. monocytogenes . The arrows indicate approximate sizes and orientations of the different genes. The predicted length of each protein is indicated below (in amino acids [aas]). The stop sign-shaped symbols indicate putative transcription terminators. The values in percentages below agrB , agrC , and agrA indicate the percentage of amino acid identity between the L. monocytogenes and S. aureus orthologues encoded by the genes of the agr loci. Numbers between parentheses indicate the sizes (in base pairs) of the intergenic regions. The site of Tn 1545 insertion is represented by an inverted black triangle. (B) Transcriptional analysis by RT-PCR. The dotted lines enclosed by arrows in the lower half of panel A indicate the positions of the primers and PCR products used in the RT-PCR analysis. The amplified products, numbered 1 to 5, were subjected to Tris acetate-EDTA-agarose gel electrophoresis. The arrows preceded by numbers (in kilobases) to the left of the panel correspond to the molecular weight (MW) DNA ladder. (C) Expression of the agr genes in stationary (Stat) and exponential (Exp) phases. The expression was measured by real-time quantitative RT-PCR. The amount of agr mRNA relative to that of the normalizing gene gyr (upper panel) and the 16S gene (lower panel) was determined by real-time quantitative RT-PCR with bacteria grown in BHI in the exponential or stationary phase of growth. The amounts of gyr mRNA and 16S rRNA were constant under these conditions (data not shown). The values shown are means of results from three assays; the error bars indicate the standard deviations.

Techniques Used: Atomic Absorption Spectroscopy, Reverse Transcription Polymerase Chain Reaction, Polymerase Chain Reaction, Amplification, Agarose Gel Electrophoresis, Molecular Weight, Expressing, Quantitative RT-PCR

Western blot analyses. Culture supernatants and membrane fractions from cells grown overnight at 37°C with agitation in BHI medium were tested in exponential phase (EP) and stationary phase (SP). Identical amounts of each culture supernatant were loaded onto SDS-10% polyacrylamide gels. Proteins were transferred electrophoretically onto nitrocellulose and detected with specific antibodies. (Upper panel) Anti-LLO MAb. Decreasing amounts of supernatant were loaded, corresponding to 10 7 , 5 × 10 6 , and 2.5 × 10 6 bacteria (b). The anti-LLO MAbs SE1 and SE2 were used at a final dilution of 1/1,000. (Middle panel) Anti-PC-PLC. Decreasing amounts of supernatant were loaded, corresponding to 10 7 and 5 × 10 6 bacteria. The anti-PlcB polyclonal antibody was used at a final dilution of 1/200. (Lower panel) Anti-ActA. Membrane fractions corresponding to 10 7 bacteria were loaded. The anti-ActA polyclonal antibody was used at a final dilution of 1/1,000. WT, strain EGD-e; agr , agrA -Tn 1545 insertion mutant.
Figure Legend Snippet: Western blot analyses. Culture supernatants and membrane fractions from cells grown overnight at 37°C with agitation in BHI medium were tested in exponential phase (EP) and stationary phase (SP). Identical amounts of each culture supernatant were loaded onto SDS-10% polyacrylamide gels. Proteins were transferred electrophoretically onto nitrocellulose and detected with specific antibodies. (Upper panel) Anti-LLO MAb. Decreasing amounts of supernatant were loaded, corresponding to 10 7 , 5 × 10 6 , and 2.5 × 10 6 bacteria (b). The anti-LLO MAbs SE1 and SE2 were used at a final dilution of 1/1,000. (Middle panel) Anti-PC-PLC. Decreasing amounts of supernatant were loaded, corresponding to 10 7 and 5 × 10 6 bacteria. The anti-PlcB polyclonal antibody was used at a final dilution of 1/200. (Lower panel) Anti-ActA. Membrane fractions corresponding to 10 7 bacteria were loaded. The anti-ActA polyclonal antibody was used at a final dilution of 1/1,000. WT, strain EGD-e; agr , agrA -Tn 1545 insertion mutant.

Techniques Used: Western Blot, Planar Chromatography, Mutagenesis

17) Product Images from "VimA-Dependent Modulation of Acetyl Coenzyme A Levels and Lipid A Biosynthesis Can Alter Virulence in Porphyromonas gingivalis"

Article Title: VimA-Dependent Modulation of Acetyl Coenzyme A Levels and Lipid A Biosynthesis Can Alter Virulence in Porphyromonas gingivalis

Journal: Infection and Immunity

doi: 10.1128/IAI.06062-11

Gingipain, non-gingipain protease, and sialidase activities of P. gingivalis strains. P. gingivalis strains were grown to exponential phase (OD 600 , 0.8) in BHI broth with supplements. (A) Gingipain activity of P. gingivalis strains were tested against
Figure Legend Snippet: Gingipain, non-gingipain protease, and sialidase activities of P. gingivalis strains. P. gingivalis strains were grown to exponential phase (OD 600 , 0.8) in BHI broth with supplements. (A) Gingipain activity of P. gingivalis strains were tested against

Techniques Used: Activity Assay

18) Product Images from "Lipoprotein biosynthesis by prolipoprotein diacylglyceryl transferase is required for efficient spore germination and full virulence of Bacillus anthracis"

Article Title: Lipoprotein biosynthesis by prolipoprotein diacylglyceryl transferase is required for efficient spore germination and full virulence of Bacillus anthracis

Journal: Molecular microbiology

doi: 10.1111/j.1365-2958.2011.07915.x

Lack of lipidation in lgt mutant. Cells were cultivated in BHI medium with shaking for 4 h at 37°C. Lipoproteins were labeled with [ 14 C]-palmitic acid and detected by autoradiography. (A) Wild-type strain with empty vector pSW4, lgt mutant with
Figure Legend Snippet: Lack of lipidation in lgt mutant. Cells were cultivated in BHI medium with shaking for 4 h at 37°C. Lipoproteins were labeled with [ 14 C]-palmitic acid and detected by autoradiography. (A) Wild-type strain with empty vector pSW4, lgt mutant with

Techniques Used: Mutagenesis, Labeling, Autoradiography, Plasmid Preparation

Lipoproteins of B. anthracis influence bacterial surface hydrophobicity. Bacteria were cultured in BHI medium to an A 600 of 4.0 and the washed bacterial suspensions were tested for adherence to hexadecane, which results in reduced optical density in the
Figure Legend Snippet: Lipoproteins of B. anthracis influence bacterial surface hydrophobicity. Bacteria were cultured in BHI medium to an A 600 of 4.0 and the washed bacterial suspensions were tested for adherence to hexadecane, which results in reduced optical density in the

Techniques Used: Cell Culture

19) Product Images from "The sloABCR Operon of Streptococcus mutans Encodes an Mn and Fe Transport System Required for Endocarditis Virulence and Its Mn-Dependent Repressor"

Article Title: The sloABCR Operon of Streptococcus mutans Encodes an Mn and Fe Transport System Required for Endocarditis Virulence and Its Mn-Dependent Repressor

Journal: Journal of Bacteriology

doi: 10.1128/JB.185.20.5967-5975.2003

Western blot analysis of the effect of Mn and Fe on SloC expression. Equal amounts of total protein isolated from cultures of S. mutans V403 (wild-type), V2643 ( sloR mutant), and V2613 (Δ sloC mutant) were separated by SDS-PAGE. Proteins were transferred to a nitrocellulose membrane for Western blot detection with rabbit polyclonal anti-FimA antiserum. (A) Overnight cultures grown in BHI broth under anaerobic conditions were diluted 100-fold into fresh BHI broth or BHI broth supplemented with MnSO 4 or FeSO 4 ). Gels were 12% Bio-Rad Ready cast, and the ECL enhanced chemiluminescence system (Amersham, Piscataway, N.J.) was used for visualization of Western blots. (B) Cultures were grown anaerobically in BHI broth with MnCl 2 , Fe(III)C 6 H 5 O 7 , or Fe(II)SO 4 at the concentrations indicated. Lysates were prepared as described above, except that a Fast Prep, FP120 (Bio101, Savant, Vista, Calif.) bead beater was used at level 6 for 30 s to lyse cells.
Figure Legend Snippet: Western blot analysis of the effect of Mn and Fe on SloC expression. Equal amounts of total protein isolated from cultures of S. mutans V403 (wild-type), V2643 ( sloR mutant), and V2613 (Δ sloC mutant) were separated by SDS-PAGE. Proteins were transferred to a nitrocellulose membrane for Western blot detection with rabbit polyclonal anti-FimA antiserum. (A) Overnight cultures grown in BHI broth under anaerobic conditions were diluted 100-fold into fresh BHI broth or BHI broth supplemented with MnSO 4 or FeSO 4 ). Gels were 12% Bio-Rad Ready cast, and the ECL enhanced chemiluminescence system (Amersham, Piscataway, N.J.) was used for visualization of Western blots. (B) Cultures were grown anaerobically in BHI broth with MnCl 2 , Fe(III)C 6 H 5 O 7 , or Fe(II)SO 4 at the concentrations indicated. Lysates were prepared as described above, except that a Fast Prep, FP120 (Bio101, Savant, Vista, Calif.) bead beater was used at level 6 for 30 s to lyse cells.

Techniques Used: Western Blot, Expressing, Isolation, Mutagenesis, SDS Page

Aerobic growth of wild-type and mutant strains of S. mutans . (A and B) Growth in (A) BHI broth and BCMg81 plus 10 μM Fe(III) C 6 H 5 O 7 (B). OD 600 was measured at 0, 12, 16, 20, 24, 39, and 47 h of incubation. (C and D) Culture densities at a single time point in BCMg81 containing Fe(III) C 6 H 5 O 7 or MnCl 2 at the concentrations indicated. (C) OD 600 at 38 h of incubation with Fe(III) C 6 H 5 O 7 . (D) OD 600 at 16 h of incubation with MnCl 2 . ⧫, wild-type; ▵, sloC mutant; ▴, sloR -complemented sloC mutant; •, sloA mutant; □, sloR mutant; ▪, sloR -complemented sloR mutant. The two sloR -complemented strains were not included in panels C and D. Error bars indicate standard deviations from duplicate cultures.
Figure Legend Snippet: Aerobic growth of wild-type and mutant strains of S. mutans . (A and B) Growth in (A) BHI broth and BCMg81 plus 10 μM Fe(III) C 6 H 5 O 7 (B). OD 600 was measured at 0, 12, 16, 20, 24, 39, and 47 h of incubation. (C and D) Culture densities at a single time point in BCMg81 containing Fe(III) C 6 H 5 O 7 or MnCl 2 at the concentrations indicated. (C) OD 600 at 38 h of incubation with Fe(III) C 6 H 5 O 7 . (D) OD 600 at 16 h of incubation with MnCl 2 . ⧫, wild-type; ▵, sloC mutant; ▴, sloR -complemented sloC mutant; •, sloA mutant; □, sloR mutant; ▪, sloR -complemented sloR mutant. The two sloR -complemented strains were not included in panels C and D. Error bars indicate standard deviations from duplicate cultures.

Techniques Used: Mutagenesis, Incubation

20) Product Images from "Simultaneous Deficiency of both MurA and p60 Proteins Generates a Rough Phenotype in Listeria monocytogenes"

Article Title: Simultaneous Deficiency of both MurA and p60 Proteins Generates a Rough Phenotype in Listeria monocytogenes

Journal: Journal of Bacteriology

doi: 10.1128/JB.187.24.8385-8394.2005

Microscopic morphology of EGDe and rough isolates. (a) The edges of colonies of the various strains grown on BHI agar plates at 37°C were compared by microscopic analysis (50× original magnification). The wild type showed a smooth outline
Figure Legend Snippet: Microscopic morphology of EGDe and rough isolates. (a) The edges of colonies of the various strains grown on BHI agar plates at 37°C were compared by microscopic analysis (50× original magnification). The wild type showed a smooth outline

Techniques Used:

21) Product Images from "Sialidase and Sialoglycoproteases Can Modulate Virulence in Porphyromonas gingivalis ▿ ▿ †"

Article Title: Sialidase and Sialoglycoproteases Can Modulate Virulence in Porphyromonas gingivalis ▿ ▿ †

Journal: Infection and Immunity

doi: 10.1128/IAI.00106-11

Comparison of total protease and sialidase activities in P. gingivalis . P. gingivalis was grown to exponential phase (OD 600 of 0.8) in 10 ml of BHI broth supplemented with hemin and vitamin K. (A) Total protease and sialidase activities of P. gingivalis mutants FLL401, FLL402, FLL403, and FLL92. Total protease activity was estimated using a FRET-based assay, and sialidase was estimated using an enzyme-based assay method. *, P
Figure Legend Snippet: Comparison of total protease and sialidase activities in P. gingivalis . P. gingivalis was grown to exponential phase (OD 600 of 0.8) in 10 ml of BHI broth supplemented with hemin and vitamin K. (A) Total protease and sialidase activities of P. gingivalis mutants FLL401, FLL402, FLL403, and FLL92. Total protease activity was estimated using a FRET-based assay, and sialidase was estimated using an enzyme-based assay method. *, P

Techniques Used: Activity Assay, Enzymatic Assay

22) Product Images from "Role of HtrA in Growth and Competence of Streptococcus mutans UA159"

Article Title: Role of HtrA in Growth and Competence of Streptococcus mutans UA159

Journal: Journal of Bacteriology

doi: 10.1128/JB.187.9.3028-3038.2005

Growth phenotypes of S. mutans UA159 (wild type) and two htrA -disrupted mutants, SAB2 (polar) and SAB2-13 (nonpolar). (A) Growth curves grown in BHI broth at 37°C (top) and 42°C (bottom). The data shown are from a single experiment representative
Figure Legend Snippet: Growth phenotypes of S. mutans UA159 (wild type) and two htrA -disrupted mutants, SAB2 (polar) and SAB2-13 (nonpolar). (A) Growth curves grown in BHI broth at 37°C (top) and 42°C (bottom). The data shown are from a single experiment representative

Techniques Used:

23) Product Images from "Universal Stress Proteins Contribute Edwardsiella ictaluri Virulence in Catfish"

Article Title: Universal Stress Proteins Contribute Edwardsiella ictaluri Virulence in Catfish

Journal: Frontiers in Microbiology

doi: 10.3389/fmicb.2018.02931

Growth of E. ictaluri USP mutants and WT in BHI broth. The data represent means of four replicates. Ei Δ usp03 and Ei Δ usp04 have a significantly ( p
Figure Legend Snippet: Growth of E. ictaluri USP mutants and WT in BHI broth. The data represent means of four replicates. Ei Δ usp03 and Ei Δ usp04 have a significantly ( p

Techniques Used:

The survival assay of E. ictaluri WT and USP mutants exposed to 0.1% H 2 O 2 . (A) Each strain had four replicates (column A–D). Strains start with E. ictaluri WT , Ei Δ usp02-13 and BHI control. (B) The bars show the difference between bioluminescence of USP mutants and WT. ∗ indicates a significant difference between stress and non-stress at P
Figure Legend Snippet: The survival assay of E. ictaluri WT and USP mutants exposed to 0.1% H 2 O 2 . (A) Each strain had four replicates (column A–D). Strains start with E. ictaluri WT , Ei Δ usp02-13 and BHI control. (B) The bars show the difference between bioluminescence of USP mutants and WT. ∗ indicates a significant difference between stress and non-stress at P

Techniques Used: Clonogenic Cell Survival Assay

The survival assay of E. ictaluri WT and USP mutants in pH 5.5. (A) Each strain had four replicates (column A–D). Strains start with E. ictaluri WT , Ei Δ usp02-13 and BHI control. (B) The bars show the difference between bioluminescence of USP mutants and WT. ∗ indicates a significant difference between stress and non-stress at P
Figure Legend Snippet: The survival assay of E. ictaluri WT and USP mutants in pH 5.5. (A) Each strain had four replicates (column A–D). Strains start with E. ictaluri WT , Ei Δ usp02-13 and BHI control. (B) The bars show the difference between bioluminescence of USP mutants and WT. ∗ indicates a significant difference between stress and non-stress at P

Techniques Used: Clonogenic Cell Survival Assay

24) Product Images from "The Small RNA Chaperone Hfq Is Required for the Virulence of Yersinia pseudotuberculosis ▿"

Article Title: The Small RNA Chaperone Hfq Is Required for the Virulence of Yersinia pseudotuberculosis ▿

Journal: Infection and Immunity

doi: 10.1128/IAI.01046-09

Growth of Y. pseudotuberculosis Δ hfq strain in rich media. Y. pseudotuberculosis wild-type, Δ hfq , and Δ hfq +p hfq strains were cultured in BHI broth at 26°C, 37°C, and 37°C plus 2.5 mM CaCl 2 , and the OD 620 of each culture was measured over the course of the growth curve. Each graph represents the mean of three independent biological replicates grown on three different days. The error bars represent the standard deviation of the optical density at each time point. Significance was calculated by Student's unpaired t test at 4 and 12 h (*, P = 0.0419; ***, P = 0.0003).
Figure Legend Snippet: Growth of Y. pseudotuberculosis Δ hfq strain in rich media. Y. pseudotuberculosis wild-type, Δ hfq , and Δ hfq +p hfq strains were cultured in BHI broth at 26°C, 37°C, and 37°C plus 2.5 mM CaCl 2 , and the OD 620 of each culture was measured over the course of the growth curve. Each graph represents the mean of three independent biological replicates grown on three different days. The error bars represent the standard deviation of the optical density at each time point. Significance was calculated by Student's unpaired t test at 4 and 12 h (*, P = 0.0419; ***, P = 0.0003).

Techniques Used: Cell Culture, Standard Deviation

25) Product Images from "Streptococcus pneumoniae Folate Biosynthesis Responds to Environmental CO2 Levels"

Article Title: Streptococcus pneumoniae Folate Biosynthesis Responds to Environmental CO2 Levels

Journal: Journal of Bacteriology

doi: 10.1128/JB.01942-12

CO 2 -dependent growth restriction of the S. pneumoniae Δ pca and Δ folC strains. The growth of the S. pneumoniae R6, LKIPB01 (R6Δ pca ), and LKIPB02 (R6Δ folC ) strains in CO 2 -poor (open squares) or CO 2 -rich (closed squares) BHI
Figure Legend Snippet: CO 2 -dependent growth restriction of the S. pneumoniae Δ pca and Δ folC strains. The growth of the S. pneumoniae R6, LKIPB01 (R6Δ pca ), and LKIPB02 (R6Δ folC ) strains in CO 2 -poor (open squares) or CO 2 -rich (closed squares) BHI

Techniques Used:

Metabolic complementation of the S. pneumoniae R6 Δ folC strain. The results of competitive growth of the LKIPB02 (Δ folC ) strain with the R6 strain under CO 2 -poor versus CO 2 -rich conditions in BHI broth cultures without (−) or with
Figure Legend Snippet: Metabolic complementation of the S. pneumoniae R6 Δ folC strain. The results of competitive growth of the LKIPB02 (Δ folC ) strain with the R6 strain under CO 2 -poor versus CO 2 -rich conditions in BHI broth cultures without (−) or with

Techniques Used:

The level of intracellular long-chain polyglutamyl folate in S. pneumoniae depends on the presence of the folC gene. The R6 and LKIPB02 (Δ folC ) strains were cultured in CO 2 -rich (+) and CO 2 -poor (−) BHI broth, and bacterial cells were
Figure Legend Snippet: The level of intracellular long-chain polyglutamyl folate in S. pneumoniae depends on the presence of the folC gene. The R6 and LKIPB02 (Δ folC ) strains were cultured in CO 2 -rich (+) and CO 2 -poor (−) BHI broth, and bacterial cells were

Techniques Used: Cell Culture

26) Product Images from "Role of the Porphyromonas gingivalis iron-binding protein PG1777 in oxidative stress resistance"

Article Title: Role of the Porphyromonas gingivalis iron-binding protein PG1777 in oxidative stress resistance

Journal: Microbiology

doi: 10.1099/mic.0.000213

Sensitivity and survival of P. gingivalis isogenic mutants to hydrogen peroxide treatment. (a) All P. gingivalis cultures were grown to early exponential phase (OD 600 of ∼0.2) in BHI broth; 0.25 mM hydrogen peroxide was added to cell cultures
Figure Legend Snippet: Sensitivity and survival of P. gingivalis isogenic mutants to hydrogen peroxide treatment. (a) All P. gingivalis cultures were grown to early exponential phase (OD 600 of ∼0.2) in BHI broth; 0.25 mM hydrogen peroxide was added to cell cultures

Techniques Used:

27) Product Images from "Temporal transcriptomic analysis of the Listeria monocytogenes EGD-e ?B regulon"

Article Title: Temporal transcriptomic analysis of the Listeria monocytogenes EGD-e ?B regulon

Journal: BMC Microbiology

doi: 10.1186/1471-2180-8-20

(A) Copy number of the sigB gene in L. monocytogenes EGD-e grown in BHI medium for 3 h, 4 h, 8 h and 16 h. Data shown here is representative of three independent biological replicates. (B) Immuno-blot analysis quantifying σ B from L. monocytogenes EGD-e at different growth phases. Proteins were isolated from cultures of L. monocytogenes EGD-e grown for 3 h (lane 1), 4 h (lane 2), 8 h (lane 3) and 16 h (lane 4) in BHI at 37°C and σ B was detected using rabbit polyclonal anti-serum produced against S. aureus COL σ B . The L. monocytogenes Δ sigB deletion mutant (lane 5) was used as negative control and S. aureus COL (lane 6) was used as positive control for specific binding of the antibody. Molecular masses (in kilodaltons) of prestained SDS-PAGE standard marker (Bio-Rad) are indicated on the left and σ B is marked on the right.
Figure Legend Snippet: (A) Copy number of the sigB gene in L. monocytogenes EGD-e grown in BHI medium for 3 h, 4 h, 8 h and 16 h. Data shown here is representative of three independent biological replicates. (B) Immuno-blot analysis quantifying σ B from L. monocytogenes EGD-e at different growth phases. Proteins were isolated from cultures of L. monocytogenes EGD-e grown for 3 h (lane 1), 4 h (lane 2), 8 h (lane 3) and 16 h (lane 4) in BHI at 37°C and σ B was detected using rabbit polyclonal anti-serum produced against S. aureus COL σ B . The L. monocytogenes Δ sigB deletion mutant (lane 5) was used as negative control and S. aureus COL (lane 6) was used as positive control for specific binding of the antibody. Molecular masses (in kilodaltons) of prestained SDS-PAGE standard marker (Bio-Rad) are indicated on the left and σ B is marked on the right.

Techniques Used: Isolation, Produced, Mutagenesis, Negative Control, Positive Control, Binding Assay, SDS Page, Marker

28) Product Images from "regT can modulate gingipain activity and response to oxidative stress in Porphyromonas gingivalis"

Article Title: regT can modulate gingipain activity and response to oxidative stress in Porphyromonas gingivalis

Journal: Microbiology

doi: 10.1099/mic.0.038315-0

(a, b) Western immunoblot analysis of the extracellular proteins from P. gingivalis using specific anti-RGP and anti-KGP antibodies as probes. All lanes contained 20 μg of acetone (60 %)-precipitated proteins from the supernatant fractions of cultures grown in BHI medium at 37 °C (a) or 42 °C (b). The blots were reacted with antiserum raised in rabbits or chicken against the Arg-X- and Lys-X-specific protease from P. gingivalis . Secondary antibody was goat anti-rabbit or anti-chicken IgG alkaline (heavy plus light chains)–horseradish peroxidase conjugate. Lanes 1 and 3, W83; lanes 2 and 4, FLL205. In (a), lanes 1 and 2 were reacted with chicken anti-Kgp; lanes 3 and 4 were reacted with rabbit anti-RgpA. In (b), lanes 1 and 2 were reacted with rabbit anti-RgpB; lanes 3 and 4 were reacted with rabbit anti-RgpA. (c) Immunoblot analysis of membrane fractions. Lanes 1 amd 3, W83; lanes 2 and 4, FLL205. Lanes 1 and 2 were reacted with rabbit anti-RgpB; lanes 3 and 4 were reacted with rabbit anti-Kgp.
Figure Legend Snippet: (a, b) Western immunoblot analysis of the extracellular proteins from P. gingivalis using specific anti-RGP and anti-KGP antibodies as probes. All lanes contained 20 μg of acetone (60 %)-precipitated proteins from the supernatant fractions of cultures grown in BHI medium at 37 °C (a) or 42 °C (b). The blots were reacted with antiserum raised in rabbits or chicken against the Arg-X- and Lys-X-specific protease from P. gingivalis . Secondary antibody was goat anti-rabbit or anti-chicken IgG alkaline (heavy plus light chains)–horseradish peroxidase conjugate. Lanes 1 and 3, W83; lanes 2 and 4, FLL205. In (a), lanes 1 and 2 were reacted with chicken anti-Kgp; lanes 3 and 4 were reacted with rabbit anti-RgpA. In (b), lanes 1 and 2 were reacted with rabbit anti-RgpB; lanes 3 and 4 were reacted with rabbit anti-RgpA. (c) Immunoblot analysis of membrane fractions. Lanes 1 amd 3, W83; lanes 2 and 4, FLL205. Lanes 1 and 2 were reacted with rabbit anti-RgpB; lanes 3 and 4 were reacted with rabbit anti-Kgp.

Techniques Used: Western Blot

29) Product Images from "Inhibitory effect of surface pre-reacted glass-ionomer (S-PRG) eluate against adhesion and colonization by Streptococcus mutans"

Article Title: Inhibitory effect of surface pre-reacted glass-ionomer (S-PRG) eluate against adhesion and colonization by Streptococcus mutans

Journal: Scientific Reports

doi: 10.1038/s41598-018-23354-x

In vitro properties of S. mutans MT8148 in the late logarithmic phase in the presence of various concentrations of S-PRG eluate. ( A , B ) Bacterial growth by adding 1 × 10 9 CFU/ml of S. mutans with 18-h incubation, which was determined by OD 550 values in BHI broth ( A ) and recovered bacterial numbers on MSB plates ( B ). ( C ) Bacterial growth by adding 1 × 10 9 CFU/ml of S. mutans at multiple time points, which was determined by OD 550 values in BHI broth. ( D ) Sucrose-dependent adhesion rates. ( E ) Quantitation of biofilm formation. Significant differences were determined using ANOVA with Bonferroni correction. * P
Figure Legend Snippet: In vitro properties of S. mutans MT8148 in the late logarithmic phase in the presence of various concentrations of S-PRG eluate. ( A , B ) Bacterial growth by adding 1 × 10 9 CFU/ml of S. mutans with 18-h incubation, which was determined by OD 550 values in BHI broth ( A ) and recovered bacterial numbers on MSB plates ( B ). ( C ) Bacterial growth by adding 1 × 10 9 CFU/ml of S. mutans at multiple time points, which was determined by OD 550 values in BHI broth. ( D ) Sucrose-dependent adhesion rates. ( E ) Quantitation of biofilm formation. Significant differences were determined using ANOVA with Bonferroni correction. * P

Techniques Used: In Vitro, Incubation, Quantitation Assay

Biofilm formation by S. mutans MT8148 grown in BHI with 0.25% sucrose in the presence of various concentrations of S-PRG eluate. ( A ) Quantity of biofilm formation. ( B ) Representative images of formed biofilms using confocal scanning laser microscopy. ( C ) Biofilm thickness. ( D ) Representative images of biofilm thickness using confocal scanning laser microscopy. Significant differences were determined using ANOVA with Bonferroni correction. *** P
Figure Legend Snippet: Biofilm formation by S. mutans MT8148 grown in BHI with 0.25% sucrose in the presence of various concentrations of S-PRG eluate. ( A ) Quantity of biofilm formation. ( B ) Representative images of formed biofilms using confocal scanning laser microscopy. ( C ) Biofilm thickness. ( D ) Representative images of biofilm thickness using confocal scanning laser microscopy. Significant differences were determined using ANOVA with Bonferroni correction. *** P

Techniques Used: Microscopy

Inhibition on S. mutans MT8148 grown by the S-PRG eluate. ( A , B ) Bacterial growth by adding varying concentration of the eluate followed by 18 h incubation. Growth was determined by OD 550 values in BHI broth ( A ) and recovered bacterial numbers on MSB plates ( B ). ( C ) Bacterial growth by adding 1 × 10 7 CFU/ml of S. mutans at multiple time points, which was determined by OD 550 values in BHI broth. ( D ) Bacterial survival by adding 1 × 10 7 CFU/ml of S. mutans at multiple time points, which was determined by adding serial dilutions of the bacterial suspensions to MSB plates.
Figure Legend Snippet: Inhibition on S. mutans MT8148 grown by the S-PRG eluate. ( A , B ) Bacterial growth by adding varying concentration of the eluate followed by 18 h incubation. Growth was determined by OD 550 values in BHI broth ( A ) and recovered bacterial numbers on MSB plates ( B ). ( C ) Bacterial growth by adding 1 × 10 7 CFU/ml of S. mutans at multiple time points, which was determined by OD 550 values in BHI broth. ( D ) Bacterial survival by adding 1 × 10 7 CFU/ml of S. mutans at multiple time points, which was determined by adding serial dilutions of the bacterial suspensions to MSB plates.

Techniques Used: Inhibition, Concentration Assay, Incubation

30) Product Images from "Characterization of a Potential Listeria monocytogenes Virulence Factor Associated with Attachment to Fresh Produce"

Article Title: Characterization of a Potential Listeria monocytogenes Virulence Factor Associated with Attachment to Fresh Produce

Journal: Applied and Environmental Microbiology

doi: 10.1128/AEM.01006-13

Attachment assay and detection for all strains on lettuce leaves. (A) Attached wild-type, Δ lcp , and F2365::pMAD:: cat :: lcp strains on lettuce leaves were homogenized, and the homogenates were plated on BHI agar plates. Data were obtained from three
Figure Legend Snippet: Attachment assay and detection for all strains on lettuce leaves. (A) Attached wild-type, Δ lcp , and F2365::pMAD:: cat :: lcp strains on lettuce leaves were homogenized, and the homogenates were plated on BHI agar plates. Data were obtained from three

Techniques Used:

Attachment of L. monocytogenes strains on spinach and cantaloupe. Baby spinach leaves and cantaloupe skins inoculated with the wild-type, Δ lcp , or F2365::pMAD:: cat :: lcp strain were homogenized, and the homogenates were plated on BHI agar plates.
Figure Legend Snippet: Attachment of L. monocytogenes strains on spinach and cantaloupe. Baby spinach leaves and cantaloupe skins inoculated with the wild-type, Δ lcp , or F2365::pMAD:: cat :: lcp strain were homogenized, and the homogenates were plated on BHI agar plates.

Techniques Used:

31) Product Images from "Lymphocytes serve as a reservoir for Listeria monocytogenes growth during infection of mice"

Article Title: Lymphocytes serve as a reservoir for Listeria monocytogenes growth during infection of mice

Journal: Microbial pathogenesis

doi: 10.1016/j.micpath.2009.01.003

CFU recovery from the lymphocytes of BALB/c mice infected with a lethal dose of L. monocytogenes . (A) BALB/c mice were infected with Lm 10403s at the indicated dose and splenocytes were harvested 24 h later. CD22.2 + (B), TCR β + (T), DX5 + (NK), F4/80 + (Mϕ), and CD11c + (DC) cells were isolated by positive selection using antibody-coated magnetic beads. The cells were washed extensively, lysed in sterile H 2 O, and plated on BHI agar to recover viable bacteria. (B) Groups of BALB/c mice (n=3) were infected with 1 × 10 4 Lm 10403s (1 LD 50 ). Splenocytes were harvested at the indicated times post-infection and the total number of intracellular bacteria associated with either B cells (CD22.2 + ) or Mϕ (F4/80 + ) cells was determined. Mean values +/- SD are shown.
Figure Legend Snippet: CFU recovery from the lymphocytes of BALB/c mice infected with a lethal dose of L. monocytogenes . (A) BALB/c mice were infected with Lm 10403s at the indicated dose and splenocytes were harvested 24 h later. CD22.2 + (B), TCR β + (T), DX5 + (NK), F4/80 + (Mϕ), and CD11c + (DC) cells were isolated by positive selection using antibody-coated magnetic beads. The cells were washed extensively, lysed in sterile H 2 O, and plated on BHI agar to recover viable bacteria. (B) Groups of BALB/c mice (n=3) were infected with 1 × 10 4 Lm 10403s (1 LD 50 ). Splenocytes were harvested at the indicated times post-infection and the total number of intracellular bacteria associated with either B cells (CD22.2 + ) or Mϕ (F4/80 + ) cells was determined. Mean values +/- SD are shown.

Techniques Used: Mouse Assay, Infection, Isolation, Selection, Magnetic Beads

32) Product Images from "Inhibitory effect of surface pre-reacted glass-ionomer (S-PRG) eluate against adhesion and colonization by Streptococcus mutans"

Article Title: Inhibitory effect of surface pre-reacted glass-ionomer (S-PRG) eluate against adhesion and colonization by Streptococcus mutans

Journal: Scientific Reports

doi: 10.1038/s41598-018-23354-x

In vitro properties of S. mutans MT8148 in the late logarithmic phase in the presence of various concentrations of S-PRG eluate. ( A , B ) Bacterial growth by adding 1 × 10 9 CFU/ml of S. mutans with 18-h incubation, which was determined by OD 550 values in BHI broth ( A ) and recovered bacterial numbers on MSB plates ( B ). ( C ) Bacterial growth by adding 1 × 10 9 CFU/ml of S. mutans at multiple time points, which was determined by OD 550 values in BHI broth. ( D ) Sucrose-dependent adhesion rates. ( E ) Quantitation of biofilm formation. Significant differences were determined using ANOVA with Bonferroni correction. * P
Figure Legend Snippet: In vitro properties of S. mutans MT8148 in the late logarithmic phase in the presence of various concentrations of S-PRG eluate. ( A , B ) Bacterial growth by adding 1 × 10 9 CFU/ml of S. mutans with 18-h incubation, which was determined by OD 550 values in BHI broth ( A ) and recovered bacterial numbers on MSB plates ( B ). ( C ) Bacterial growth by adding 1 × 10 9 CFU/ml of S. mutans at multiple time points, which was determined by OD 550 values in BHI broth. ( D ) Sucrose-dependent adhesion rates. ( E ) Quantitation of biofilm formation. Significant differences were determined using ANOVA with Bonferroni correction. * P

Techniques Used: In Vitro, Incubation, Quantitation Assay

Inhibition on S. mutans MT8148 grown by the S-PRG eluate. ( A , B ) Bacterial growth by adding varying concentration of the eluate followed by 18 h incubation. Growth was determined by OD 550 values in BHI broth ( A ) and recovered bacterial numbers on MSB plates ( B ). ( C ) Bacterial growth by adding 1 × 10 7 CFU/ml of S. mutans at multiple time points, which was determined by OD 550 values in BHI broth. ( D ) Bacterial survival by adding 1 × 10 7 CFU/ml of S. mutans at multiple time points, which was determined by adding serial dilutions of the bacterial suspensions to MSB plates.
Figure Legend Snippet: Inhibition on S. mutans MT8148 grown by the S-PRG eluate. ( A , B ) Bacterial growth by adding varying concentration of the eluate followed by 18 h incubation. Growth was determined by OD 550 values in BHI broth ( A ) and recovered bacterial numbers on MSB plates ( B ). ( C ) Bacterial growth by adding 1 × 10 7 CFU/ml of S. mutans at multiple time points, which was determined by OD 550 values in BHI broth. ( D ) Bacterial survival by adding 1 × 10 7 CFU/ml of S. mutans at multiple time points, which was determined by adding serial dilutions of the bacterial suspensions to MSB plates.

Techniques Used: Inhibition, Concentration Assay, Incubation

Biofilm formation by S. mutans MT8148 grown in BHI with 0.25% sucrose in the presence of various concentrations of S-PRG eluate. ( A ) Quantity of biofilm formation. ( B ) Representative images of formed biofilms using confocal scanning laser microscopy. ( C ) Biofilm thickness. ( D ) Representative images of biofilm thickness using confocal scanning laser microscopy. Significant differences were determined using ANOVA with Bonferroni correction. *** P
Figure Legend Snippet: Biofilm formation by S. mutans MT8148 grown in BHI with 0.25% sucrose in the presence of various concentrations of S-PRG eluate. ( A ) Quantity of biofilm formation. ( B ) Representative images of formed biofilms using confocal scanning laser microscopy. ( C ) Biofilm thickness. ( D ) Representative images of biofilm thickness using confocal scanning laser microscopy. Significant differences were determined using ANOVA with Bonferroni correction. *** P

Techniques Used: Microscopy

33) Product Images from "Temporal transcriptomic analysis of the Listeria monocytogenes EGD-e ?B regulon"

Article Title: Temporal transcriptomic analysis of the Listeria monocytogenes EGD-e ?B regulon

Journal: BMC Microbiology

doi: 10.1186/1471-2180-8-20

(A) Copy number of the sigB gene in L. monocytogenes EGD-e grown in BHI medium for 3 h, 4 h, 8 h and 16 h. Data shown here is representative of three independent biological replicates. (B) Immuno-blot analysis quantifying σ B from L. monocytogenes EGD-e at different growth phases. Proteins were isolated from cultures of L. monocytogenes EGD-e grown for 3 h (lane 1), 4 h (lane 2), 8 h (lane 3) and 16 h (lane 4) in BHI at 37°C and σ B was detected using rabbit polyclonal anti-serum produced against S. aureus COL σ B . The L. monocytogenes Δ sigB deletion mutant (lane 5) was used as negative control and S. aureus COL (lane 6) was used as positive control for specific binding of the antibody. Molecular masses (in kilodaltons) of prestained SDS-PAGE standard marker (Bio-Rad) are indicated on the left and σ B is marked on the right.
Figure Legend Snippet: (A) Copy number of the sigB gene in L. monocytogenes EGD-e grown in BHI medium for 3 h, 4 h, 8 h and 16 h. Data shown here is representative of three independent biological replicates. (B) Immuno-blot analysis quantifying σ B from L. monocytogenes EGD-e at different growth phases. Proteins were isolated from cultures of L. monocytogenes EGD-e grown for 3 h (lane 1), 4 h (lane 2), 8 h (lane 3) and 16 h (lane 4) in BHI at 37°C and σ B was detected using rabbit polyclonal anti-serum produced against S. aureus COL σ B . The L. monocytogenes Δ sigB deletion mutant (lane 5) was used as negative control and S. aureus COL (lane 6) was used as positive control for specific binding of the antibody. Molecular masses (in kilodaltons) of prestained SDS-PAGE standard marker (Bio-Rad) are indicated on the left and σ B is marked on the right.

Techniques Used: Isolation, Produced, Mutagenesis, Negative Control, Positive Control, Binding Assay, SDS Page, Marker

34) Product Images from "DNA Repair of 8-Oxo-7,8-Dihydroguanine Lesions in Porphyromonas gingivalis ▿ ▿ †"

Article Title: DNA Repair of 8-Oxo-7,8-Dihydroguanine Lesions in Porphyromonas gingivalis ▿ ▿ †

Journal:

doi: 10.1128/JB.00919-08

Sensitivity of P. gingivalis strains W83 and FLL144 to hydrogen peroxide. P. gingivalis was grown to early log phase (OD 600 of 0.2) in BHI broth, 0.25 mM (A) or 0.5 mM (B) H 2 O 2 was then added to the cell cultures, and the cultures were further incubated
Figure Legend Snippet: Sensitivity of P. gingivalis strains W83 and FLL144 to hydrogen peroxide. P. gingivalis was grown to early log phase (OD 600 of 0.2) in BHI broth, 0.25 mM (A) or 0.5 mM (B) H 2 O 2 was then added to the cell cultures, and the cultures were further incubated

Techniques Used: Incubation

Proteolytic activity of P. gingivalis FLL144. P. gingivalis strains were grown to late log phase (OD 600 of 1.2) in 50 ml of BHI broth supplemented with hemin and vitamin K. (A) A whole-cell culture was analyzed for Rgp (BAPNA) activity. (B) A whole-cell
Figure Legend Snippet: Proteolytic activity of P. gingivalis FLL144. P. gingivalis strains were grown to late log phase (OD 600 of 1.2) in 50 ml of BHI broth supplemented with hemin and vitamin K. (A) A whole-cell culture was analyzed for Rgp (BAPNA) activity. (B) A whole-cell

Techniques Used: Activity Assay, Cell Culture

UV sensitivity of P. gingivalis is increased by inactivation of uvrB. P. gingivalis strains W83 and FLL144 were grown to mid-log phase (OD 600 of 0.6), spread on BHI plates, and then subjected to irradiation at increasing doses (0 μJ, 500 μJ,
Figure Legend Snippet: UV sensitivity of P. gingivalis is increased by inactivation of uvrB. P. gingivalis strains W83 and FLL144 were grown to mid-log phase (OD 600 of 0.6), spread on BHI plates, and then subjected to irradiation at increasing doses (0 μJ, 500 μJ,

Techniques Used: Irradiation

35) Product Images from "Fluorescence Tools Adapted for Real-Time Monitoring of the Behaviors of Streptococcus Species"

Article Title: Fluorescence Tools Adapted for Real-Time Monitoring of the Behaviors of Streptococcus Species

Journal: Applied and Environmental Microbiology

doi: 10.1128/AEM.00620-19

Stability of pDL278_Pveg-sfgfp in the presence and absence of spectinomycin. The numbers of spectinomycin-resistant S. mutans pDL278_Pveg-sfgfp cells cultured in the presence (A) or absence (B) of spectinomycin were compared. S. mutans cells harboring pDL278_Pveg-sfgfp were diluted 1:1,000 into BHI and cultured for 12 h. After 12 h the total numbers of S. mutans cells (blue) and spectinomycin-resistant S. mutans cells (red) were determined via serial dilution and agar plating. This assay was repeated five times for approximately 50 generations.
Figure Legend Snippet: Stability of pDL278_Pveg-sfgfp in the presence and absence of spectinomycin. The numbers of spectinomycin-resistant S. mutans pDL278_Pveg-sfgfp cells cultured in the presence (A) or absence (B) of spectinomycin were compared. S. mutans cells harboring pDL278_Pveg-sfgfp were diluted 1:1,000 into BHI and cultured for 12 h. After 12 h the total numbers of S. mutans cells (blue) and spectinomycin-resistant S. mutans cells (red) were determined via serial dilution and agar plating. This assay was repeated five times for approximately 50 generations.

Techniques Used: Cell Culture, Serial Dilution

36) Product Images from "In Vitro Resistance to Thrombin-Induced Platelet Microbicidal Protein Is Associated with Enhanced Progression and Hematogenous Dissemination in Experimental Staphylococcus aureus Infective Endocarditis"

Article Title: In Vitro Resistance to Thrombin-Induced Platelet Microbicidal Protein Is Associated with Enhanced Progression and Hematogenous Dissemination in Experimental Staphylococcus aureus Infective Endocarditis

Journal: Infection and Immunity

doi:

Comparison of S. aureus ISP479C and ISP479R growth kinetics in vitro. Log-phase organisms were dually inoculated (10 3 CFU of each strain) into 10 ml of BHI broth, and the cultures were incubated on a rotary shaker (for aeration) at 37°C. At selected time points, aliquots were quantitatively cultured on BHI agar with or without erythromycin (10 μg/ml; as described in Materials and Methods). Data points represent the mean values from two independent experiments performed in duplicate. In no case was the deviation from the mean greater than 0.2 log CFU/ml; error bars were intentionally excluded to improve clarity. These results mirrored those of identical dual-culture experiments performed with nutrient or Trypticase soy broth (see Materials and Methods). These results were not significantly different from those for either organism cultured alone (data not shown).
Figure Legend Snippet: Comparison of S. aureus ISP479C and ISP479R growth kinetics in vitro. Log-phase organisms were dually inoculated (10 3 CFU of each strain) into 10 ml of BHI broth, and the cultures were incubated on a rotary shaker (for aeration) at 37°C. At selected time points, aliquots were quantitatively cultured on BHI agar with or without erythromycin (10 μg/ml; as described in Materials and Methods). Data points represent the mean values from two independent experiments performed in duplicate. In no case was the deviation from the mean greater than 0.2 log CFU/ml; error bars were intentionally excluded to improve clarity. These results mirrored those of identical dual-culture experiments performed with nutrient or Trypticase soy broth (see Materials and Methods). These results were not significantly different from those for either organism cultured alone (data not shown).

Techniques Used: In Vitro, Incubation, Cell Culture

37) Product Images from "A Novel Action of the Proton Pump Inhibitor Rabeprazole and Its Thioether Derivative against the Motility of Helicobacter pylori"

Article Title: A Novel Action of the Proton Pump Inhibitor Rabeprazole and Its Thioether Derivative against the Motility of Helicobacter pylori

Journal: Antimicrobial Agents and Chemotherapy

doi:

(A) Temperature-dependent and -independent manners of motility of H. pylori and V. cholerae O1. Bacteria were grown at 37°C and then suspended in BHI broth containing FBS (pH 7.4) prewarmed at the indicated temperatures. Symbols: open square, H. pylori strain C7M (results similar to those shown in the figure were also obtained with six other H. pylori strains); closed square, V. cholerae O1 strain EO8 (results similar to those shown in the figure were also obtained with V. cholerae O1 strain CI3). The data represent means ± standard deviations (error bars) of three trials. (B) Swimming speed of the motile bacteria shown in panel A.
Figure Legend Snippet: (A) Temperature-dependent and -independent manners of motility of H. pylori and V. cholerae O1. Bacteria were grown at 37°C and then suspended in BHI broth containing FBS (pH 7.4) prewarmed at the indicated temperatures. Symbols: open square, H. pylori strain C7M (results similar to those shown in the figure were also obtained with six other H. pylori strains); closed square, V. cholerae O1 strain EO8 (results similar to those shown in the figure were also obtained with V. cholerae O1 strain CI3). The data represent means ± standard deviations (error bars) of three trials. (B) Swimming speed of the motile bacteria shown in panel A.

Techniques Used:

38) Product Images from "PCR Detection of Salmonella enterica Serotype Montevideo in and on Raw Tomatoes Using Primers Derived from hilA"

Article Title: PCR Detection of Salmonella enterica Serotype Montevideo in and on Raw Tomatoes Using Primers Derived from hilA

Journal: Applied and Environmental Microbiology

doi:

Limits of detection of HILA2-based PCR assay with different enrichment times. Cell cultures containing 10 9 CFU/ml were serially diluted to concentrations of 10 8 to 10 0 CFU/ml, and 100-μl portions of the dilutions were transferred to 900-μl portions of BHI broth, which were then incubated at 37°C with shaking for 3, 6 and 9 h. The cells were treated, and DNA was amplified by PCR. Lanes 1 and 21, 100-bp DNA ladders; lanes 2 through 7, PCR products from preparations containing 10 5 , 10 4 , 10 3 , 10 2 , 10 1 , and 10 0 CFU/ml, respectively, after 3 h of enrichment; lanes 8 through 13, PCR products from preparations containing 10 5 , 10 4 , 10 3 , 10 2 , 10 1 , and 10 0 CFU/ml respectively, after 6 h of enrichment; lanes 14 through 19, PCR products from preparations containing 10 5 , 10 4 , 10 3 , 10 2 , 10 1 , and 10 0 CFU/ml, respectively, after 9 h of enrichment; Lane 20, negative control.
Figure Legend Snippet: Limits of detection of HILA2-based PCR assay with different enrichment times. Cell cultures containing 10 9 CFU/ml were serially diluted to concentrations of 10 8 to 10 0 CFU/ml, and 100-μl portions of the dilutions were transferred to 900-μl portions of BHI broth, which were then incubated at 37°C with shaking for 3, 6 and 9 h. The cells were treated, and DNA was amplified by PCR. Lanes 1 and 21, 100-bp DNA ladders; lanes 2 through 7, PCR products from preparations containing 10 5 , 10 4 , 10 3 , 10 2 , 10 1 , and 10 0 CFU/ml, respectively, after 3 h of enrichment; lanes 8 through 13, PCR products from preparations containing 10 5 , 10 4 , 10 3 , 10 2 , 10 1 , and 10 0 CFU/ml respectively, after 6 h of enrichment; lanes 14 through 19, PCR products from preparations containing 10 5 , 10 4 , 10 3 , 10 2 , 10 1 , and 10 0 CFU/ml, respectively, after 9 h of enrichment; Lane 20, negative control.

Techniques Used: Polymerase Chain Reaction, Incubation, Amplification, Negative Control

39) Product Images from "The Major Autolysin of Streptococcus gordonii Is Subject to Complex Regulation and Modulates Stress Tolerance, Biofilm Formation, and Extracellular-DNA Release ▿"

Article Title: The Major Autolysin of Streptococcus gordonii Is Subject to Complex Regulation and Modulates Stress Tolerance, Biofilm Formation, and Extracellular-DNA Release ▿

Journal: Journal of Bacteriology

doi: 10.1128/JB.00056-11

eDNA release by SgWT and AtlS-deficient S. gordonii as a function of growth domain. Cells were cultured in BHI broth under aerobic or anaerobic conditions. (A) Agarose gel electrophoresis (0.8%) of eDNA stained with ethidium bromide as described in the Materials and Methods section. The optical density (OD 600 ) of the culture when harvested is presented below each panel, and the photographs are representative of three independent experiments that yielded similar results. (B) Quantitative real-time PCR of eDNA using the 16S rRNA gene as the amplification target. Data were normalized as detailed in Materials and Methods and represent the means and standard deviations of results of two independent experiments done in duplicate on different days. *, statistically significant differences among the same strain collected at different growth phases ( P
Figure Legend Snippet: eDNA release by SgWT and AtlS-deficient S. gordonii as a function of growth domain. Cells were cultured in BHI broth under aerobic or anaerobic conditions. (A) Agarose gel electrophoresis (0.8%) of eDNA stained with ethidium bromide as described in the Materials and Methods section. The optical density (OD 600 ) of the culture when harvested is presented below each panel, and the photographs are representative of three independent experiments that yielded similar results. (B) Quantitative real-time PCR of eDNA using the 16S rRNA gene as the amplification target. Data were normalized as detailed in Materials and Methods and represent the means and standard deviations of results of two independent experiments done in duplicate on different days. *, statistically significant differences among the same strain collected at different growth phases ( P

Techniques Used: Cell Culture, Agarose Gel Electrophoresis, Staining, Real-time Polymerase Chain Reaction, Amplification

40) Product Images from "Feedback Inhibition in the PhoQ/PhoP Signaling System by a Membrane Peptide"

Article Title: Feedback Inhibition in the PhoQ/PhoP Signaling System by a Membrane Peptide

Journal: PLoS Genetics

doi: 10.1371/journal.pgen.1000788

Inhibition of PhoP-regulated transcription by MgrB in Salmonella typhimurium and Yersinia pestis . (A) Salmonella enterica serovar Typhimurium strain 14028s carrying the P phoN - lacZ reporter plasmid pNL2 and either a plasmid expressing Salmonella mgrB (pAL43) or a control plasmid (pEB52) were grown in LB with antibiotics and 1 mM IPTG. The amino acid sequence of MgrB from strain 14028s (data not shown) is identical to the sequence from strain LT2 (shown in Figure 6 ). (B) Y. pestis KIM6 carrying pNL2 and either a plasmid expressing the Yersinia pestis mgrB (pAL42) or a control plasmid (pEB52) were grown in BHI with antibiotics and 1mM IPTG. For each strain, the mean and standard deviation for at least three independent cultures are shown.
Figure Legend Snippet: Inhibition of PhoP-regulated transcription by MgrB in Salmonella typhimurium and Yersinia pestis . (A) Salmonella enterica serovar Typhimurium strain 14028s carrying the P phoN - lacZ reporter plasmid pNL2 and either a plasmid expressing Salmonella mgrB (pAL43) or a control plasmid (pEB52) were grown in LB with antibiotics and 1 mM IPTG. The amino acid sequence of MgrB from strain 14028s (data not shown) is identical to the sequence from strain LT2 (shown in Figure 6 ). (B) Y. pestis KIM6 carrying pNL2 and either a plasmid expressing the Yersinia pestis mgrB (pAL42) or a control plasmid (pEB52) were grown in BHI with antibiotics and 1mM IPTG. For each strain, the mean and standard deviation for at least three independent cultures are shown.

Techniques Used: Inhibition, Plasmid Preparation, Expressing, Sequencing, Standard Deviation

41) Product Images from "Identification of New Genes Involved in the Virulence of Listeria monocytogenes by Signature-Tagged Transposon Mutagenesis"

Article Title: Identification of New Genes Involved in the Virulence of Listeria monocytogenes by Signature-Tagged Transposon Mutagenesis

Journal: Infection and Immunity

doi: 10.1128/IAI.69.4.2054-2065.2001

Invasiveness of the attenuated strains. Invasiveness was evaluated in three different types of cell lines (A, Caco2 cells; B, Vero cells; and C, HepG-2 cells). Cell monolayers were incubated for 1 h at 37°C with approximately 200 bacteria per cell. After being washed, the cells were reincubated for 8 h in fresh culture medium containing gentamicin (10 mg liter −1 ). At intervals, the cells were washed again and lysed, and viable bacteria were counted on BHI-ERY plates. Datum points and error bars (indicated only for the wild-type strain for clarity) represent the mean and standard deviation of the number of bacteria per well. Three different assays were performed. Symbols: ■, EGD; □, ORF626; ●, PbpX; ▴, GtcA; ○, YtgP.
Figure Legend Snippet: Invasiveness of the attenuated strains. Invasiveness was evaluated in three different types of cell lines (A, Caco2 cells; B, Vero cells; and C, HepG-2 cells). Cell monolayers were incubated for 1 h at 37°C with approximately 200 bacteria per cell. After being washed, the cells were reincubated for 8 h in fresh culture medium containing gentamicin (10 mg liter −1 ). At intervals, the cells were washed again and lysed, and viable bacteria were counted on BHI-ERY plates. Datum points and error bars (indicated only for the wild-type strain for clarity) represent the mean and standard deviation of the number of bacteria per well. Three different assays were performed. Symbols: ■, EGD; □, ORF626; ●, PbpX; ▴, GtcA; ○, YtgP.

Techniques Used: Incubation, Standard Deviation

42) Product Images from "A GntR Family Transcription Factor in Streptococcus mutans Regulates Biofilm Formation and Expression of Multiple Sugar Transporter Genes"

Article Title: A GntR Family Transcription Factor in Streptococcus mutans Regulates Biofilm Formation and Expression of Multiple Sugar Transporter Genes

Journal: Frontiers in Microbiology

doi: 10.3389/fmicb.2018.03224

Determination of growth curves of S. mutans UA159, S. mutans Δ stsR , and Δ stsR/pDL278-stsR . S. mutans UA159, S. mutans Δ stsR , and Δ stsR/pDL278-stsR strains were cultivated in BHI to mid-exponential phase and then diluted into (A) fresh BHI broth or (B) TV base medium supplemented with either 10 mM (limiting) or 100 mM (excess) sucrose, glucose, or lactose. Growth curves were monitored with a Multiskan Spectrum (Thermo, Multiskan Go, United States), and the OD 600 was measured in 1 h intervals. (A) For CFU counts, after diluted, the bacteria were cultured at 37°C for 1, 4, 8, and 12 h. Then bacterial suspension was serially diluted in BHI and plated on BHI agar plates. CFU values were calculated after the plates were incubated anaerobically at 37°C for 48 h. Error bars represent standard deviations based on results from at least three biological replicates.
Figure Legend Snippet: Determination of growth curves of S. mutans UA159, S. mutans Δ stsR , and Δ stsR/pDL278-stsR . S. mutans UA159, S. mutans Δ stsR , and Δ stsR/pDL278-stsR strains were cultivated in BHI to mid-exponential phase and then diluted into (A) fresh BHI broth or (B) TV base medium supplemented with either 10 mM (limiting) or 100 mM (excess) sucrose, glucose, or lactose. Growth curves were monitored with a Multiskan Spectrum (Thermo, Multiskan Go, United States), and the OD 600 was measured in 1 h intervals. (A) For CFU counts, after diluted, the bacteria were cultured at 37°C for 1, 4, 8, and 12 h. Then bacterial suspension was serially diluted in BHI and plated on BHI agar plates. CFU values were calculated after the plates were incubated anaerobically at 37°C for 48 h. Error bars represent standard deviations based on results from at least three biological replicates.

Techniques Used: Cell Culture, Incubation

43) Product Images from "Inactivation of vimF, a Putative Glycosyltransferase Gene Downstream of vimE, Alters Glycosylation and Activation of the Gingipains in Porphyromonas gingivalis W83 "

Article Title: Inactivation of vimF, a Putative Glycosyltransferase Gene Downstream of vimE, Alters Glycosylation and Activation of the Gingipains in Porphyromonas gingivalis W83

Journal: Infection and Immunity

doi: 10.1128/IAI.73.7.3971-3982.2005

Proteolytic activity of P. gingivalis vimF -defective mutant. P. gingivalis was grown to stationary phase in BHI broth supplemented with hemin and vitamin K. Activities against Rgp (A) and Kgp (B) were tested in whole-cell culture.
Figure Legend Snippet: Proteolytic activity of P. gingivalis vimF -defective mutant. P. gingivalis was grown to stationary phase in BHI broth supplemented with hemin and vitamin K. Activities against Rgp (A) and Kgp (B) were tested in whole-cell culture.

Techniques Used: Activity Assay, Mutagenesis, Cell Culture

44) Product Images from "A Novel Mutation within the Central Listeria monocytogenes Regulator PrfA That Results in Constitutive Expression of Virulence Gene Products"

Article Title: A Novel Mutation within the Central Listeria monocytogenes Regulator PrfA That Results in Constitutive Expression of Virulence Gene Products

Journal: Journal of Bacteriology

doi: 10.1128/JB.186.18.6265-6276.2004

PlcB (lecithinase) phenotypes of L. monocytogenes mutants and corresponding control strains on BHI medium overlaid with molten agar containing activated-charcoal-treated (0.2% [wt/vol]) BHI and 5% (vol/vol) 1:1 egg yolk-PBS solution. The plates were incubated at 37°C overnight. 476, NF-L476 (WT); 879, NF-L879 (EMS L140F mutant); 1003, NF-L1003 (Δ prfA ); 1006, NF-L1006 (WT + pPL2 i ); 1039, NF-L1039 (WT + WT i ); 1040, NF-L1040 (WT + L147P i ); 1008, NF-L1008 (WT + L140F i ); 1009, NF-L1009 (Δ prfA + pPL2 i ); 1041, NF-L1041 (Δ prfA + WT i ); 1042, NF-L1042 (Δ prfA + L147P i ); 1011, NF-L1011 (Δ prfA + L140F i ); 1067, NF-L1067 (L140F + L140F i ).
Figure Legend Snippet: PlcB (lecithinase) phenotypes of L. monocytogenes mutants and corresponding control strains on BHI medium overlaid with molten agar containing activated-charcoal-treated (0.2% [wt/vol]) BHI and 5% (vol/vol) 1:1 egg yolk-PBS solution. The plates were incubated at 37°C overnight. 476, NF-L476 (WT); 879, NF-L879 (EMS L140F mutant); 1003, NF-L1003 (Δ prfA ); 1006, NF-L1006 (WT + pPL2 i ); 1039, NF-L1039 (WT + WT i ); 1040, NF-L1040 (WT + L147P i ); 1008, NF-L1008 (WT + L140F i ); 1009, NF-L1009 (Δ prfA + pPL2 i ); 1041, NF-L1041 (Δ prfA + WT i ); 1042, NF-L1042 (Δ prfA + L147P i ); 1011, NF-L1011 (Δ prfA + L140F i ); 1067, NF-L1067 (L140F + L140F i ).

Techniques Used: Incubation, Mutagenesis

Overnight cultures of L. monocytogenes strains grown in BHI broth at 37°C without shaking. The strain numbers and relevant genotypes are shown underneath the respective culture tubes. 476, NF-L476 (WT); 879, NF-L879 (EMS L140F mutant); 1041, NF-L1041 (Δ prfA + WT i ); 1011, NF-L1011 (Δ prfA + L140F i ); 1067, NF-L1067 (L140F + L140F i ); 1006, NF-L1006 (WT + pPL2 i ); 1008, NF-L1008 (WT + L140F i ).
Figure Legend Snippet: Overnight cultures of L. monocytogenes strains grown in BHI broth at 37°C without shaking. The strain numbers and relevant genotypes are shown underneath the respective culture tubes. 476, NF-L476 (WT); 879, NF-L879 (EMS L140F mutant); 1041, NF-L1041 (Δ prfA + WT i ); 1011, NF-L1011 (Δ prfA + L140F i ); 1067, NF-L1067 (L140F + L140F i ); 1006, NF-L1006 (WT + pPL2 i ); 1008, NF-L1008 (WT + L140F i ).

Techniques Used: Mutagenesis

45) Product Images from "Effects of Oxygen on Biofilm Formation and the AtlA Autolysin of Streptococcus mutans ▿"

Article Title: Effects of Oxygen on Biofilm Formation and the AtlA Autolysin of Streptococcus mutans ▿

Journal:

doi: 10.1128/JB.00546-07

Growth of S. mutans strains (wild type and 630NP). (A) Growth in BHI broth was monitored in a Bioscreen C system which was set to shake for 15 s every 30 min (aerobic conditions). For anaerobic growth, sterile mineral oil was placed on top of the broth
Figure Legend Snippet: Growth of S. mutans strains (wild type and 630NP). (A) Growth in BHI broth was monitored in a Bioscreen C system which was set to shake for 15 s every 30 min (aerobic conditions). For anaerobic growth, sterile mineral oil was placed on top of the broth

Techniques Used:

Effects of aerobic growth of S. mutans strains (UA159, 629NP, and 629P). For aerobic growth, the cultures were grown on a rotary shaker (150 rpm). (A) Growth curves. The cultures were grown in BHI medium at 37°C. The data shown are from a single
Figure Legend Snippet: Effects of aerobic growth of S. mutans strains (UA159, 629NP, and 629P). For aerobic growth, the cultures were grown on a rotary shaker (150 rpm). (A) Growth curves. The cultures were grown in BHI medium at 37°C. The data shown are from a single

Techniques Used:

46) Product Images from "relA-Independent Amino Acid Starvation Response Network of Streptococcus pyogenes"

Article Title: relA-Independent Amino Acid Starvation Response Network of Streptococcus pyogenes

Journal: Journal of Bacteriology

doi: 10.1128/JB.183.24.7354-7364.2001

Stimulation of ileS (A) and valS (B) transcription in response to, respectively, mupirocin treatment (plus) and amino acid (AA) deprivation [minus (isoleucine plus valine)] of NZ131 wild-type and relA mutant cells. Control cells were incubated in BHI broth in the absence of mupirocin (minus) for the indicated period of time or grown in complete CDM (+AA). The sizes of the hybridizing bands in the Northern blots are consistent with the genetic organization of the two transcription units shown below the blots.
Figure Legend Snippet: Stimulation of ileS (A) and valS (B) transcription in response to, respectively, mupirocin treatment (plus) and amino acid (AA) deprivation [minus (isoleucine plus valine)] of NZ131 wild-type and relA mutant cells. Control cells were incubated in BHI broth in the absence of mupirocin (minus) for the indicated period of time or grown in complete CDM (+AA). The sizes of the hybridizing bands in the Northern blots are consistent with the genetic organization of the two transcription units shown below the blots.

Techniques Used: Mutagenesis, Incubation, Northern Blot

47) Product Images from "Contribution of Mn-Cofactored Superoxide Dismutase (SodA) to the Virulence of Streptococcus agalactiae"

Article Title: Contribution of Mn-Cofactored Superoxide Dismutase (SodA) to the Virulence of Streptococcus agalactiae

Journal: Infection and Immunity

doi: 10.1128/IAI.69.8.5098-5106.2001

Growth curves of S. agalactiae NEM316, the sodA mutant, NEM1640, and the complemented strain, NEM1641, in BHI broth at 37°C under aerobic conditions with and without paraquat (10 mM). Strains and growth conditions are represented as follows: wild-type strain without (▴) or with 10 mM paraquat (▵); sodA mutant without (■) or with 10 mM paraquat (□); sodA -complemented mutant without (●) or with 10 mM paraquat (○). The results shown are representative of at least three independent experiments showing less than 10% variation.
Figure Legend Snippet: Growth curves of S. agalactiae NEM316, the sodA mutant, NEM1640, and the complemented strain, NEM1641, in BHI broth at 37°C under aerobic conditions with and without paraquat (10 mM). Strains and growth conditions are represented as follows: wild-type strain without (▴) or with 10 mM paraquat (▵); sodA mutant without (■) or with 10 mM paraquat (□); sodA -complemented mutant without (●) or with 10 mM paraquat (○). The results shown are representative of at least three independent experiments showing less than 10% variation.

Techniques Used: Mutagenesis

Sensitivity of S. agalactiae to H 2 O 2 . The wild-type strain, NEM316 (▴), the sodA mutant, NEM1640 (■), and the complemented strain, NEM1641 (●) were grown and treated with H 2 O 2 as described in Materials and Methods. Exponential-phase cells were exposed to 20 mM H 2 O 2 for 30, 60, or 120 min at 37°C. Viability was determined by plating on BHI agar. Error bars represent the standard deviations of three independent experiments.
Figure Legend Snippet: Sensitivity of S. agalactiae to H 2 O 2 . The wild-type strain, NEM316 (▴), the sodA mutant, NEM1640 (■), and the complemented strain, NEM1641 (●) were grown and treated with H 2 O 2 as described in Materials and Methods. Exponential-phase cells were exposed to 20 mM H 2 O 2 for 30, 60, or 120 min at 37°C. Viability was determined by plating on BHI agar. Error bars represent the standard deviations of three independent experiments.

Techniques Used: Mutagenesis

48) Product Images from "Nitric Oxide Stress Resistance in Porphyromonas gingivalis Is Mediated by a Putative Hydroxylamine Reductase"

Article Title: Nitric Oxide Stress Resistance in Porphyromonas gingivalis Is Mediated by a Putative Hydroxylamine Reductase

Journal: Journal of Bacteriology

doi: 10.1128/JB.06457-11

Sensitivity of P. gingivalis W83, FLL32, FLL455, and FLL456 to UV irradiation. Dilutions of fresh cultures of the P. gingivalis strains were grown anaerobically to exponential phase in BHI broth from overnight cultures and spread on BHI agar. The cells
Figure Legend Snippet: Sensitivity of P. gingivalis W83, FLL32, FLL455, and FLL456 to UV irradiation. Dilutions of fresh cultures of the P. gingivalis strains were grown anaerobically to exponential phase in BHI broth from overnight cultures and spread on BHI agar. The cells

Techniques Used: Irradiation

Sensitivity of P. gingivalis W83, FLL455 and FLL456 to single NO stress. P. gingivalis strains were grown anaerobically to early exponential phase in BHI broth at 37°C, DEA NONOate (NO) was added to the cultures, and the cultures were further
Figure Legend Snippet: Sensitivity of P. gingivalis W83, FLL455 and FLL456 to single NO stress. P. gingivalis strains were grown anaerobically to early exponential phase in BHI broth at 37°C, DEA NONOate (NO) was added to the cultures, and the cultures were further

Techniques Used:

Sensitivity of P. gingivalis W83, FLL455, and complemented (comp) FLL455 to NO stress. P. gingivalis strains were grown anaerobically to early exponential phase in BHI broth at 37°C, DEA NONOate (NO) was added to the cultures, and the cultures
Figure Legend Snippet: Sensitivity of P. gingivalis W83, FLL455, and complemented (comp) FLL455 to NO stress. P. gingivalis strains were grown anaerobically to early exponential phase in BHI broth at 37°C, DEA NONOate (NO) was added to the cultures, and the cultures

Techniques Used:

(A) Sensitivity of P. gingivalis W83 to single NO stress. P. gingivalis W83 strain was grown anaerobically to early exponential phase in BHI broth at 37°C, DEA NONOate (NO) or NaOH was added to the cultures, and the cultures were further incubated
Figure Legend Snippet: (A) Sensitivity of P. gingivalis W83 to single NO stress. P. gingivalis W83 strain was grown anaerobically to early exponential phase in BHI broth at 37°C, DEA NONOate (NO) or NaOH was added to the cultures, and the cultures were further incubated

Techniques Used: Incubation

Glutamate concentration in P. gingivalis W83, FLL455, and complemented FLL455. P. gingivalis strains were grown anaerobically to early exponential phase in BHI broth at 37°C, and cultures were either left untreated or treated with the indicated
Figure Legend Snippet: Glutamate concentration in P. gingivalis W83, FLL455, and complemented FLL455. P. gingivalis strains were grown anaerobically to early exponential phase in BHI broth at 37°C, and cultures were either left untreated or treated with the indicated

Techniques Used: Concentration Assay

Sensitivity of P. gingivalis W83, FLL455, and FLL456 to H 2 O 2 stress. P. gingivalis strains were grown anaerobically to early exponential phase in BHI broth at 37°C, H 2 O 2 was added to the cultures, and the cultures further incubated for 24 h. Each
Figure Legend Snippet: Sensitivity of P. gingivalis W83, FLL455, and FLL456 to H 2 O 2 stress. P. gingivalis strains were grown anaerobically to early exponential phase in BHI broth at 37°C, H 2 O 2 was added to the cultures, and the cultures further incubated for 24 h. Each

Techniques Used: Incubation

49) Product Images from "Comparison of the Contributions of Heat-Labile Enterotoxin and Heat-Stable Enterotoxin b to the Virulence of Enterotoxigenic Escherichia coli in F4ac Receptor-Positive Young Pigs "

Article Title: Comparison of the Contributions of Heat-Labile Enterotoxin and Heat-Stable Enterotoxin b to the Virulence of Enterotoxigenic Escherichia coli in F4ac Receptor-Positive Young Pigs

Journal: Infection and Immunity

doi: 10.1128/IAI.01743-07

GM 1 ELISA to detect LT expression by different isogenic ETEC strains following in vitro culture. Individual wells of 96-well plates were coated with 100 μl of GM 1 ganglioside (1.0 μg/ml) in 0.1 M carbonate buffer (pH 9.6). Following overnight incubation, 100 μl of a 1:2 dilution of cell-free supernatant of culture material was dispensed into each well. The following strains were tested: Nal r F4ac + ETEC strain WAM2317 (LT + STb + ) and isogenic derivatives STb − (Δ estB ) mutant MUN297, STb-complemented Δ estB mutant MUN298, LT − STb − (Δ eltAB Δ estB ) mutant MUN300, and LT-complemented Δ eltAB Δ estB mutant MUN301. In addition, LT + clone MUN302 [ E. coli DH5α(pBR322/ eltAB )] and MUN303 [ E. coli DH5α(pBR322)] were used as positive and negative controls, respectively. Strains were cultured in BHI containing 2% Casamino Acids for 48 or 72 h, and cell-free supernatants were collected. The dilution of the primary antibodies (rabbit anti-cholera toxin serum) was 1:2,000, while that of the secondary antibodies (horseradish peroxidase-labeled goat anti-rabbit immunoglobulin G) was 1:2,500. For each experiment, the supernatant from each strain was tested in eight different wells (technical replicates). Mean ± SEM measurements of optical density at 492 nm are shown and represent the outcomes of two independent experiments (biological replicates). wt, wild type; c, complemented.
Figure Legend Snippet: GM 1 ELISA to detect LT expression by different isogenic ETEC strains following in vitro culture. Individual wells of 96-well plates were coated with 100 μl of GM 1 ganglioside (1.0 μg/ml) in 0.1 M carbonate buffer (pH 9.6). Following overnight incubation, 100 μl of a 1:2 dilution of cell-free supernatant of culture material was dispensed into each well. The following strains were tested: Nal r F4ac + ETEC strain WAM2317 (LT + STb + ) and isogenic derivatives STb − (Δ estB ) mutant MUN297, STb-complemented Δ estB mutant MUN298, LT − STb − (Δ eltAB Δ estB ) mutant MUN300, and LT-complemented Δ eltAB Δ estB mutant MUN301. In addition, LT + clone MUN302 [ E. coli DH5α(pBR322/ eltAB )] and MUN303 [ E. coli DH5α(pBR322)] were used as positive and negative controls, respectively. Strains were cultured in BHI containing 2% Casamino Acids for 48 or 72 h, and cell-free supernatants were collected. The dilution of the primary antibodies (rabbit anti-cholera toxin serum) was 1:2,000, while that of the secondary antibodies (horseradish peroxidase-labeled goat anti-rabbit immunoglobulin G) was 1:2,500. For each experiment, the supernatant from each strain was tested in eight different wells (technical replicates). Mean ± SEM measurements of optical density at 492 nm are shown and represent the outcomes of two independent experiments (biological replicates). wt, wild type; c, complemented.

Techniques Used: Enzyme-linked Immunosorbent Assay, Expressing, In Vitro, Incubation, Mutagenesis, Cell Culture, Labeling

ELISA to detect STb expression by different isogenic ETEC strains following in vitro culture. The following strains were tested: Nal r F4ac + ETEC strain WAM2317 (LT + STb + ) and isogenic derivatives STb − (Δ estB ) mutant MUN297, STb-complemented Δ estB mutant MUN298, LT − STb − (Δ eltAB Δ estB ) mutant MUN300, and LT-complemented Δ eltAB Δ estB mutant MUN301. Other strains used as controls included 2787 [STb − laboratory E. coli strain HB101(pBR322)] and 2329 [STb + )]. Strains were grown overnight in BHI containing 2% Casamino Acids and 100 μl of cell-free supernatants (1:2 dilutions) were used to coat individual wells in 96-well plates. A 1:2,000 dilution of primary antibodies (rabbit anti-STb serum) and a 1:2,500 dilution of secondary antibodies (alkaline phosphatase-labeled goat anti-rabbit immunoglobulin G) were used. For each experiment, the supernatant from each strain was tested in three different wells (technical replicates). Measurements of optical density at 405 nm (mean ± standard error of the mean [SEM]) are shown and represent the outcomes of two independent experiments (biological replicates). wt, wild type; c, complemented.
Figure Legend Snippet: ELISA to detect STb expression by different isogenic ETEC strains following in vitro culture. The following strains were tested: Nal r F4ac + ETEC strain WAM2317 (LT + STb + ) and isogenic derivatives STb − (Δ estB ) mutant MUN297, STb-complemented Δ estB mutant MUN298, LT − STb − (Δ eltAB Δ estB ) mutant MUN300, and LT-complemented Δ eltAB Δ estB mutant MUN301. Other strains used as controls included 2787 [STb − laboratory E. coli strain HB101(pBR322)] and 2329 [STb + )]. Strains were grown overnight in BHI containing 2% Casamino Acids and 100 μl of cell-free supernatants (1:2 dilutions) were used to coat individual wells in 96-well plates. A 1:2,000 dilution of primary antibodies (rabbit anti-STb serum) and a 1:2,500 dilution of secondary antibodies (alkaline phosphatase-labeled goat anti-rabbit immunoglobulin G) were used. For each experiment, the supernatant from each strain was tested in three different wells (technical replicates). Measurements of optical density at 405 nm (mean ± standard error of the mean [SEM]) are shown and represent the outcomes of two independent experiments (biological replicates). wt, wild type; c, complemented.

Techniques Used: Enzyme-linked Immunosorbent Assay, Expressing, In Vitro, Mutagenesis, Labeling

50) Product Images from "Deletion of the Gene Encoding p60 in Listeria monocytogenes Leads to Abnormal Cell Division and Loss of Actin-Based Motility "

Article Title: Deletion of the Gene Encoding p60 in Listeria monocytogenes Leads to Abnormal Cell Division and Loss of Actin-Based Motility

Journal: Infection and Immunity

doi: 10.1128/IAI.71.6.3473-3484.2003

Distribution of ActA (A) and InlA (C) at the surfaces of L. monocytogenes bacteria grown in BHI. Wild-type (wt) bacteria, the Δ iap mutant, and the iap + revertant were stained with an antiserum directed against either ActA (A) or InlA (C) and with DAPI (A and C). Wild-type bacteria and the iap + revertant show a typical polar localization of ActA and InlA, whereas both proteins are arranged differently at the surface of L. monocytogenes Δ iap . (B) Model showing how ActA distribution along the filament is generated during growth of the filament from a single bacterial cell over three rounds of replication without complete division. Filled arrowheads, center of the filament enriched in ActA. Open arrowheads, spots of ActA accumulation along the filament.
Figure Legend Snippet: Distribution of ActA (A) and InlA (C) at the surfaces of L. monocytogenes bacteria grown in BHI. Wild-type (wt) bacteria, the Δ iap mutant, and the iap + revertant were stained with an antiserum directed against either ActA (A) or InlA (C) and with DAPI (A and C). Wild-type bacteria and the iap + revertant show a typical polar localization of ActA and InlA, whereas both proteins are arranged differently at the surface of L. monocytogenes Δ iap . (B) Model showing how ActA distribution along the filament is generated during growth of the filament from a single bacterial cell over three rounds of replication without complete division. Filled arrowheads, center of the filament enriched in ActA. Open arrowheads, spots of ActA accumulation along the filament.

Techniques Used: Mutagenesis, Staining, Generated

51) Product Images from "RsbT and RsbV Contribute to ?B-Dependent Survival under Environmental, Energy, and Intracellular Stress Conditions in Listeria monocytogenes"

Article Title: RsbT and RsbV Contribute to ?B-Dependent Survival under Environmental, Energy, and Intracellular Stress Conditions in Listeria monocytogenes

Journal: Applied and Environmental Microbiology

doi: 10.1128/AEM.70.9.5349-5356.2004

Viabilities of L. monocytogenes 10403S (⧫), Δ sigB (□), Δ rsbT (▴), and Δ rsbV (○) cultures that had been grown statically in BHI at 37°C. Bacteria were harvested at indicated times, serially
Figure Legend Snippet: Viabilities of L. monocytogenes 10403S (⧫), Δ sigB (□), Δ rsbT (▴), and Δ rsbV (○) cultures that had been grown statically in BHI at 37°C. Bacteria were harvested at indicated times, serially

Techniques Used:

52) Product Images from "Understanding the Streptococcus mutans Cid/Lrg System through CidB Function"

Article Title: Understanding the Streptococcus mutans Cid/Lrg System through CidB Function

Journal: Applied and Environmental Microbiology

doi: 10.1128/AEM.01499-16

Aerobic growth curves of S. mutans UA159 (wild type) and cid derivatives (A) or lrg derivatives (B). Strains were grown in plain BHI medium. Optical density at 600 nm was monitored every 30 min at 37°C using the Bioscreen C lab system. To achieve
Figure Legend Snippet: Aerobic growth curves of S. mutans UA159 (wild type) and cid derivatives (A) or lrg derivatives (B). Strains were grown in plain BHI medium. Optical density at 600 nm was monitored every 30 min at 37°C using the Bioscreen C lab system. To achieve

Techniques Used:

53) Product Images from "Carbon Dioxide and Nisin Act Synergistically on Listeria monocytogenes"

Article Title: Carbon Dioxide and Nisin Act Synergistically on Listeria monocytogenes

Journal: Applied and Environmental Microbiology

doi:

Growth of L. monocytogenes Scott A Nis r (A) and wild-type (B) strains in B-BHI broth at 4°C. Closed symbols indicate results in air; open symbols indicate results in 100% CO 2 . Squares represent cultures in the absence of nisin, and circles represent cultures in the presence of nisin (2.5 μg/ml). Vertical bars represent the means and standard deviations from two independent experiments.
Figure Legend Snippet: Growth of L. monocytogenes Scott A Nis r (A) and wild-type (B) strains in B-BHI broth at 4°C. Closed symbols indicate results in air; open symbols indicate results in 100% CO 2 . Squares represent cultures in the absence of nisin, and circles represent cultures in the presence of nisin (2.5 μg/ml). Vertical bars represent the means and standard deviations from two independent experiments.

Techniques Used:

Nisin-induced CF efflux from liposomes derived from wild-type L. monocytogenes Scott A grown in B-BHI broth at 30°C in air (a), 4°C in air (b), and 4°C in 100% CO 2 (c). Nisin (2.5 μg/ml) was added at the time indicated by the arrow. The lipid concentration for cells preadapted at 30°C in air, 4°C in air, and 4°C in 100% CO 2 was 2.5, 2.45, and 3.0 μM, respectively. The assay temperature was 22°C.
Figure Legend Snippet: Nisin-induced CF efflux from liposomes derived from wild-type L. monocytogenes Scott A grown in B-BHI broth at 30°C in air (a), 4°C in air (b), and 4°C in 100% CO 2 (c). Nisin (2.5 μg/ml) was added at the time indicated by the arrow. The lipid concentration for cells preadapted at 30°C in air, 4°C in air, and 4°C in 100% CO 2 was 2.5, 2.45, and 3.0 μM, respectively. The assay temperature was 22°C.

Techniques Used: Derivative Assay, Concentration Assay

54) Product Images from "Growth Phase and pH Influence Peptide Signaling for Competence Development in Streptococcus mutans"

Article Title: Growth Phase and pH Influence Peptide Signaling for Competence Development in Streptococcus mutans

Journal: Journal of Bacteriology

doi: 10.1128/JB.00995-13

Competence gene expression and transformation efficiency in response to exogenously added sXIP as a function of growth phase. (A) LacZ activity measured from a reporter fusion with the comX promoter. The P comX - lacZ strain was grown to an OD 600 of 0.2 (early-exponential phase), 0.4 (mid-exponential phase), or 0.8 (late-exponential phase) in FMC medium and was then incubated with 1% DMSO (to match the concentration of the solvent for XIP) or 2 μM sXIP for 1 h. Then LacZ assays were performed. (B) Transformation efficiency of UA159 as a function of growth phase. A plasmid (pDL278) was added to growing cultures in FMC medium at OD 600 values of 0.2, 0.4, and 0.8 after the addition of 2 μM sXIP, as described in Materials and Methods. After 2.5 h, cultures were plated onto BHI agar plates, and CFU were enumerated after 48 h of incubation at 37°C under a 5% CO 2 aerobic atmosphere. Transformation efficiency was calculated by dividing the number of transformants by the total number of viable bacteria. Data are means ± standard deviations (error bars) for three biological replicates conducted in triplicate. Statistical analyses were performed using Student's t test. * , P
Figure Legend Snippet: Competence gene expression and transformation efficiency in response to exogenously added sXIP as a function of growth phase. (A) LacZ activity measured from a reporter fusion with the comX promoter. The P comX - lacZ strain was grown to an OD 600 of 0.2 (early-exponential phase), 0.4 (mid-exponential phase), or 0.8 (late-exponential phase) in FMC medium and was then incubated with 1% DMSO (to match the concentration of the solvent for XIP) or 2 μM sXIP for 1 h. Then LacZ assays were performed. (B) Transformation efficiency of UA159 as a function of growth phase. A plasmid (pDL278) was added to growing cultures in FMC medium at OD 600 values of 0.2, 0.4, and 0.8 after the addition of 2 μM sXIP, as described in Materials and Methods. After 2.5 h, cultures were plated onto BHI agar plates, and CFU were enumerated after 48 h of incubation at 37°C under a 5% CO 2 aerobic atmosphere. Transformation efficiency was calculated by dividing the number of transformants by the total number of viable bacteria. Data are means ± standard deviations (error bars) for three biological replicates conducted in triplicate. Statistical analyses were performed using Student's t test. * , P

Techniques Used: Expressing, Transformation Assay, Activity Assay, Incubation, Concentration Assay, Plasmid Preparation

55) Product Images from "Universal Stress Proteins Contribute Edwardsiella ictaluri Virulence in Catfish"

Article Title: Universal Stress Proteins Contribute Edwardsiella ictaluri Virulence in Catfish

Journal: Frontiers in Microbiology

doi: 10.3389/fmicb.2018.02931

Growth of E. ictaluri USP mutants and WT in BHI broth. The data represent means of four replicates. Ei Δ usp03 and Ei Δ usp04 have a significantly ( p
Figure Legend Snippet: Growth of E. ictaluri USP mutants and WT in BHI broth. The data represent means of four replicates. Ei Δ usp03 and Ei Δ usp04 have a significantly ( p

Techniques Used:

The survival assay of E. ictaluri WT and USP mutants exposed to 0.1% H 2 O 2 . (A) Each strain had four replicates (column A–D). Strains start with E. ictaluri WT , Ei Δ usp02-13 and BHI control. (B) The bars show the difference between bioluminescence of USP mutants and WT. ∗ indicates a significant difference between stress and non-stress at P
Figure Legend Snippet: The survival assay of E. ictaluri WT and USP mutants exposed to 0.1% H 2 O 2 . (A) Each strain had four replicates (column A–D). Strains start with E. ictaluri WT , Ei Δ usp02-13 and BHI control. (B) The bars show the difference between bioluminescence of USP mutants and WT. ∗ indicates a significant difference between stress and non-stress at P

Techniques Used: Clonogenic Cell Survival Assay

The survival assay of E. ictaluri WT and USP mutants in pH 5.5. (A) Each strain had four replicates (column A–D). Strains start with E. ictaluri WT , Ei Δ usp02-13 and BHI control. (B) The bars show the difference between bioluminescence of USP mutants and WT. ∗ indicates a significant difference between stress and non-stress at P
Figure Legend Snippet: The survival assay of E. ictaluri WT and USP mutants in pH 5.5. (A) Each strain had four replicates (column A–D). Strains start with E. ictaluri WT , Ei Δ usp02-13 and BHI control. (B) The bars show the difference between bioluminescence of USP mutants and WT. ∗ indicates a significant difference between stress and non-stress at P

Techniques Used: Clonogenic Cell Survival Assay

Related Articles

Clone Assay:

Article Title: LuxS Is Required for Persistent Pneumococcal Carriage and Expression of Virulence and Biosynthesis Genes
Article Snippet: E. coli DH5α (Bio-Rad Laboratories) and RR1 were used for cloning experiments. .. S. pneumoniae strain D39 and its derivatives (Table ) were grown in brain heart infusion (BHI) broth (Difco), Todd-Hewitt broth (Difco) supplemented with 5% horse serum (Gibco), and on tryptic soy agar (TSA; Difco) supplemented with 5% defibrinated sheep blood (Hemostat Laboratories, Dixon, Calif.).

Centrifugation:

Article Title: LuxS Is Required for Persistent Pneumococcal Carriage and Expression of Virulence and Biosynthesis Genes
Article Snippet: S. pneumoniae strain D39 and its derivatives (Table ) were grown in brain heart infusion (BHI) broth (Difco), Todd-Hewitt broth (Difco) supplemented with 5% horse serum (Gibco), and on tryptic soy agar (TSA; Difco) supplemented with 5% defibrinated sheep blood (Hemostat Laboratories, Dixon, Calif.). .. For in vitro time course experiments, tubes with optical densities between ∼0.01 and 0.02 were selected, and the cells were collected by centrifugation, washed once with sterile phosphate-buffered saline (PBS), back diluted to ∼3 × 105 CFU/ml into fresh BHI broth, and immediately incubated at 37°C in a 5% CO2 chamber for 45 min. At this point, the first sample was collected.

Selection:

Article Title: The Streptococcus mutans Cid and Lrg systems modulate virulence traits in response to multiple environmental signals
Article Snippet: Escherichia coli DH10B was grown in Luria broth and S. mutans UA159 and its derivatives were grown in brain heart infusion (BHI) broth (Difco). .. For selection of antibiotic-resistant colonies after genetic transformation, ampicillin (100 μg ml–1 for E. coli ), erythromycin (300 μg ml–1 for E. coli and 10 μg ml–1 for S. mutans ), kanamycin (50 μg ml–1 for E. coli and 1 mg ml–1 for S. mutans ) and spectinomycin (50 μg ml–1 for E. coli and 1 mg ml–1 for S. mutans ) were added to media, as required.

In Vitro:

Article Title: LuxS Is Required for Persistent Pneumococcal Carriage and Expression of Virulence and Biosynthesis Genes
Article Snippet: S. pneumoniae strain D39 and its derivatives (Table ) were grown in brain heart infusion (BHI) broth (Difco), Todd-Hewitt broth (Difco) supplemented with 5% horse serum (Gibco), and on tryptic soy agar (TSA; Difco) supplemented with 5% defibrinated sheep blood (Hemostat Laboratories, Dixon, Calif.). .. For in vitro time course experiments, tubes with optical densities between ∼0.01 and 0.02 were selected, and the cells were collected by centrifugation, washed once with sterile phosphate-buffered saline (PBS), back diluted to ∼3 × 105 CFU/ml into fresh BHI broth, and immediately incubated at 37°C in a 5% CO2 chamber for 45 min. At this point, the first sample was collected.

Co-Culture Assay:

Article Title: Identification of a bacteriocin and its cognate immunity factor expressed by Moraxella catarrhalis
Article Snippet: Moraxella catarrhalis strains were routinely grown in brain heart infusion (BHI) broth (Difco/Becton Dickinson, Sparks, MD) with aeration at 37°C, or on BHI solidified using 1.5% (wt/vol) agar. .. Mueller-Hinton (MH) broth (Difco/Becton Disckinson) was used for some growth experiments involving co-culture of two different M. catarrhalis strains.

Mutagenesis:

Article Title: LipA, a Tyrosine and Lipid Phosphatase Involved in the Virulence of Listeria monocytogenes ▿ ▿ †
Article Snippet: L. monocytogenes EGDe Δ prfA (BUG2214), Δ sigB (BUG2215), Δ plcAB , and Δ lipA (BUG1959) strains as well as the L. monocytogenes LO28 Δ lipA strain were the isogenic deletion mutant strains used in this study. .. L. monocytogenes strains were routinely grown in brain heart infusion (BHI) broth (Difco) at 37°C and 200 rpm or on Oxford agar plates (Merck) at 37°C.

Incubation:

Article Title: Identification of a bacteriocin and its cognate immunity factor expressed by Moraxella catarrhalis
Article Snippet: Moraxella catarrhalis strains were routinely grown in brain heart infusion (BHI) broth (Difco/Becton Dickinson, Sparks, MD) with aeration at 37°C, or on BHI solidified using 1.5% (wt/vol) agar. .. BHI agar plates were incubated at 37°C in an atmosphere containing 95% air-5% CO2 .

Article Title: Contribution of a Thickened Cell Wall and Its Glutamine Nonamidated Component to the Vancomycin Resistance Expressed by Staphylococcus aureus Mu50
Article Snippet: All cultures were grown in brain heart infusion (BHI) broth (Difco, Detroit, Mich.) at 37°C with aeration unless indicated otherwise. .. For each experiment, an overnight culture was diluted 100-fold in prewarmed fresh BHI broth and was further incubated with aeration to ensure exponential growth conditions before sampling.

Article Title: Gingipain RgpB Is Excreted as a Proenzyme in the vimA-Defective Mutant Porphyromonas gingivalis FLL92
Article Snippet: P. gingivalis W83 and P. gingivalis FLL92 ( vimA :: ermF- ermAM ) were grown in brain heart infusion (BHI) broth (Difco Laboratories, Detroit, Mich.) supplemented with hemin (5 μg/ml), vitamin K (0.5 μg/ml), and cysteine (1%). .. Unless otherwise stated, all cultures were incubated at 37°C and maintained in an anaerobic chamber (Coy Manufacturing, Ann Arbor, Mich.) in 10% H2 , 10% CO2 , and 80% N2 .

Infection:

Article Title: Contribution of a Thickened Cell Wall and Its Glutamine Nonamidated Component to the Vancomycin Resistance Expressed by Staphylococcus aureus Mu50
Article Snippet: After his discharge, the patient experienced three episodes of relapse of a surgical site wound infection and was rehospitalized in Juntendo Hospital for treatment. .. All cultures were grown in brain heart infusion (BHI) broth (Difco, Detroit, Mich.) at 37°C with aeration unless indicated otherwise.

Article Title: The TIR Domain Containing Locus of Enterococcus faecalis Is Predominant among Urinary Tract Infection Isolates and Downregulates Host Inflammatory Response
Article Snippet: E. faecalis was grown in brain-heart-infusion (BHI) broth or on BHI agar plates (Difco) at 37°C. .. For infection assays E. faecalis were grown in BHI broth to early exponential phase (OD600 0.1–0.5) and the bacterial concentration was calculated by optical density from a standardized growth curve.

Sampling:

Article Title: Contribution of a Thickened Cell Wall and Its Glutamine Nonamidated Component to the Vancomycin Resistance Expressed by Staphylococcus aureus Mu50
Article Snippet: All cultures were grown in brain heart infusion (BHI) broth (Difco, Detroit, Mich.) at 37°C with aeration unless indicated otherwise. .. For each experiment, an overnight culture was diluted 100-fold in prewarmed fresh BHI broth and was further incubated with aeration to ensure exponential growth conditions before sampling.

Concentration Assay:

Article Title: The Streptococcus mutans Cid and Lrg systems modulate virulence traits in response to multiple environmental signals
Article Snippet: Escherichia coli DH10B was grown in Luria broth and S. mutans UA159 and its derivatives were grown in brain heart infusion (BHI) broth (Difco). .. For biofilm formation assays, S. mutans strains were grown in microtitre plates in the semi-defined medium BM ( ) supplemented with glucose or sucrose at a final concentration of 20 mM.

Article Title: The TIR Domain Containing Locus of Enterococcus faecalis Is Predominant among Urinary Tract Infection Isolates and Downregulates Host Inflammatory Response
Article Snippet: E. faecalis was grown in brain-heart-infusion (BHI) broth or on BHI agar plates (Difco) at 37°C. .. For infection assays E. faecalis were grown in BHI broth to early exponential phase (OD600 0.1–0.5) and the bacterial concentration was calculated by optical density from a standardized growth curve.

Construct:

Article Title: LipA, a Tyrosine and Lipid Phosphatase Involved in the Virulence of Listeria monocytogenes ▿ ▿ †
Article Snippet: The last strain was used as a parental strain to construct the complemented L. monocytogenes LO28 Δ lipA :: lipA strain. .. L. monocytogenes strains were routinely grown in brain heart infusion (BHI) broth (Difco) at 37°C and 200 rpm or on Oxford agar plates (Merck) at 37°C.

other:

Article Title: The vimE Gene Downstream of vimA Is Independently Expressed and Is Involved in Modulating Proteolytic Activity in Porphyromonas gingivalis W83
Article Snippet: P. gingivalis strains were grown in brain heart infusion (BHI) broth supplemented with 0.5% yeast extract (both from Difco Laboratories, Detroit, Mich.), hemin (5 μg/ml), vitamin K (0.5 μg/ml), and cysteine (0.1%) (all from Sigma-Aldrich, St. Louis, Mo.).

Article Title: Protective Role of the PG1036-PG1037-PG1038 Operon in Oxidative Stress in Porphyromonas gingivalis W83
Article Snippet: P. gingivalis strains were grown in brain heart infusion (BHI) broth (Difco Laboratories, Detroit, MI) supplemented with hemin (5 µg/ml), vitamin K (0.5 µg/ml) and cysteine (0.1%).

Cell Culture:

Article Title: A GntR Family Transcription Factor in Streptococcus mutans Regulates Biofilm Formation and Expression of Multiple Sugar Transporter Genes
Article Snippet: .. S. mutans UA159 and its derivatives were cultured in brain heart infusion (BHI) broth (Difco, Sparks, MD, United States) and on BHI agar or in biofilm medium (BM). ..

Article Title: Moraxella catarrhalis AcrAB-OprM Efflux Pump Contributes to Antimicrobial Resistance and Is Enhanced during Cold Shock Response
Article Snippet: .. Bacteria were cultured at 37°C and 200 rpm in brain heart infusion (BHI) broth (Difco, Detroit, MI) or on BHI agar plates in an atmosphere containing 5% CO2 . ..

Article Title: Identification and Characterization of Di- and Tripeptide Transporter DtpT of Listeria monocytogenes EGD-e
Article Snippet: L. monocytogenes EGD-e was grown in brain heart infusion (BHI) broth (Difco) at 37°C. .. L. monocytogenes EGD-e and L. monocytogenes Δ dtpT were also cultured in chemically defined medium (CDM) as described previously by Premaratne et al. ( ).

Expressing:

Article Title: LipA, a Tyrosine and Lipid Phosphatase Involved in the Virulence of Listeria monocytogenes ▿ ▿ †
Article Snippet: L. monocytogenes strains were routinely grown in brain heart infusion (BHI) broth (Difco) at 37°C and 200 rpm or on Oxford agar plates (Merck) at 37°C. .. Growth conditions for L. monocytogenes gene expression analysis were described in our previous study ( ).

Transformation Assay:

Article Title: The Streptococcus mutans Cid and Lrg systems modulate virulence traits in response to multiple environmental signals
Article Snippet: Escherichia coli DH10B was grown in Luria broth and S. mutans UA159 and its derivatives were grown in brain heart infusion (BHI) broth (Difco). .. For selection of antibiotic-resistant colonies after genetic transformation, ampicillin (100 μg ml–1 for E. coli ), erythromycin (300 μg ml–1 for E. coli and 10 μg ml–1 for S. mutans ), kanamycin (50 μg ml–1 for E. coli and 1 mg ml–1 for S. mutans ) and spectinomycin (50 μg ml–1 for E. coli and 1 mg ml–1 for S. mutans ) were added to media, as required.

Spectrophotometry:

Article Title: Contribution of a Thickened Cell Wall and Its Glutamine Nonamidated Component to the Vancomycin Resistance Expressed by Staphylococcus aureus Mu50
Article Snippet: All cultures were grown in brain heart infusion (BHI) broth (Difco, Detroit, Mich.) at 37°C with aeration unless indicated otherwise. .. Cell growth was monitored by measuring the optical density of the culture at 578 nm (OD578 ) with a spectrophotometer (Pharmacia LKB Biotechnology, Inc., Uppsala, Sweden).

Plasmid Preparation:

Article Title: LipA, a Tyrosine and Lipid Phosphatase Involved in the Virulence of Listeria monocytogenes ▿ ▿ †
Article Snippet: L. monocytogenes strains were routinely grown in brain heart infusion (BHI) broth (Difco) at 37°C and 200 rpm or on Oxford agar plates (Merck) at 37°C. .. Escherichia coli DH5α, XL1-BlueMRF′, or Top10 was used as the host for plasmid constructions.

Pulsed-Field Gel:

Article Title: Contribution of a Thickened Cell Wall and Its Glutamine Nonamidated Component to the Vancomycin Resistance Expressed by Staphylococcus aureus Mu50
Article Snippet: The colony that was the exception was small in size, and the vancomycin MIC for the colony was 0.5 mg/liter, although it had a pulsed-field gel electrophoresis pattern identical to that of Mu50. .. All cultures were grown in brain heart infusion (BHI) broth (Difco, Detroit, Mich.) at 37°C with aeration unless indicated otherwise.

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    Difco brain heart infusion bhi broth
    Protease activation in the extracellular protein fraction from P. <t>gingivalis</t> FLL93. P. gingivalis was grown to stationary phase (OD 600 of 1.3) in 1 liter of <t>BHI</t> broth supplemented with hemin and vitamin K. Acetone (37.5%)-precipitated proteins were mixed with 8 M urea and were incubated at 4°C for 1 h. The urea was slowly removed from the mixture by centrifugation (10,000 × g ) in a Millipore filtration unit with the addition of increasing volumes of 100 mM Tris-HCl buffer (pH 7.4). Activities for Rgp and Kgp were tested. Error bars indicate the standard errors of the means of three independent trials.
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    Protease activation in the extracellular protein fraction from P. gingivalis FLL93. P. gingivalis was grown to stationary phase (OD 600 of 1.3) in 1 liter of BHI broth supplemented with hemin and vitamin K. Acetone (37.5%)-precipitated proteins were mixed with 8 M urea and were incubated at 4°C for 1 h. The urea was slowly removed from the mixture by centrifugation (10,000 × g ) in a Millipore filtration unit with the addition of increasing volumes of 100 mM Tris-HCl buffer (pH 7.4). Activities for Rgp and Kgp were tested. Error bars indicate the standard errors of the means of three independent trials.

    Journal: Infection and Immunity

    Article Title: The vimE Gene Downstream of vimA Is Independently Expressed and Is Involved in Modulating Proteolytic Activity in Porphyromonas gingivalis W83

    doi: 10.1128/IAI.72.10.5555-5564.2004

    Figure Lengend Snippet: Protease activation in the extracellular protein fraction from P. gingivalis FLL93. P. gingivalis was grown to stationary phase (OD 600 of 1.3) in 1 liter of BHI broth supplemented with hemin and vitamin K. Acetone (37.5%)-precipitated proteins were mixed with 8 M urea and were incubated at 4°C for 1 h. The urea was slowly removed from the mixture by centrifugation (10,000 × g ) in a Millipore filtration unit with the addition of increasing volumes of 100 mM Tris-HCl buffer (pH 7.4). Activities for Rgp and Kgp were tested. Error bars indicate the standard errors of the means of three independent trials.

    Article Snippet: P. gingivalis strains were grown in brain heart infusion (BHI) broth supplemented with 0.5% yeast extract (both from Difco Laboratories, Detroit, Mich.), hemin (5 μg/ml), vitamin K (0.5 μg/ml), and cysteine (0.1%) (all from Sigma-Aldrich, St. Louis, Mo.).

    Techniques: Activation Assay, Incubation, Centrifugation, Filtration

    Inactivation of vimE resulted in decreased proteolytic activity of P. gingivalis. P. gingivalis was grown to late log phase (OD 600 of 0.7 to 0.8) or stationary phase (OD 600 of 1.4 to 1.5) in BHI broth supplemented with yeast extract, hemin, and vitamin K. Activities against Rgp (A) and Kgp (B) were tested in whole-cell culture. The results shown are representative of three independent experiments in triplicate. E, exponential phase; L, stationary phase. Error bars indicate the standard errors of the means of three independent trials.

    Journal: Infection and Immunity

    Article Title: The vimE Gene Downstream of vimA Is Independently Expressed and Is Involved in Modulating Proteolytic Activity in Porphyromonas gingivalis W83

    doi: 10.1128/IAI.72.10.5555-5564.2004

    Figure Lengend Snippet: Inactivation of vimE resulted in decreased proteolytic activity of P. gingivalis. P. gingivalis was grown to late log phase (OD 600 of 0.7 to 0.8) or stationary phase (OD 600 of 1.4 to 1.5) in BHI broth supplemented with yeast extract, hemin, and vitamin K. Activities against Rgp (A) and Kgp (B) were tested in whole-cell culture. The results shown are representative of three independent experiments in triplicate. E, exponential phase; L, stationary phase. Error bars indicate the standard errors of the means of three independent trials.

    Article Snippet: P. gingivalis strains were grown in brain heart infusion (BHI) broth supplemented with 0.5% yeast extract (both from Difco Laboratories, Detroit, Mich.), hemin (5 μg/ml), vitamin K (0.5 μg/ml), and cysteine (0.1%) (all from Sigma-Aldrich, St. Louis, Mo.).

    Techniques: Activity Assay, Cell Culture

    Immunoreactivity of the RgpB proenzyme in P. gingivalis FLL93. Western blot analysis using specific RgpB proenzyme antibodies as probes was done on the extracellular fractions from P. gingivalis W83 (lane 1), FLL92 (lane 2), and FLL93 (lane 3). All lanes contained 20 μg of acetone (37.5%)-precipitated proteins from the supernatant fractions of cultures in BHI medium at exponential growth phase.

    Journal: Infection and Immunity

    Article Title: The vimE Gene Downstream of vimA Is Independently Expressed and Is Involved in Modulating Proteolytic Activity in Porphyromonas gingivalis W83

    doi: 10.1128/IAI.72.10.5555-5564.2004

    Figure Lengend Snippet: Immunoreactivity of the RgpB proenzyme in P. gingivalis FLL93. Western blot analysis using specific RgpB proenzyme antibodies as probes was done on the extracellular fractions from P. gingivalis W83 (lane 1), FLL92 (lane 2), and FLL93 (lane 3). All lanes contained 20 μg of acetone (37.5%)-precipitated proteins from the supernatant fractions of cultures in BHI medium at exponential growth phase.

    Article Snippet: P. gingivalis strains were grown in brain heart infusion (BHI) broth supplemented with 0.5% yeast extract (both from Difco Laboratories, Detroit, Mich.), hemin (5 μg/ml), vitamin K (0.5 μg/ml), and cysteine (0.1%) (all from Sigma-Aldrich, St. Louis, Mo.).

    Techniques: Western Blot

    Expression of L. monocytogenes lipA in human blood. Transcriptional tiling maps of L. monocytogenes EGDe grown in BHI to exponential phase at 37°C (black dots) or in human blood at 37°C for 60 min (red dots) show normalized hybridization

    Journal: Infection and Immunity

    Article Title: LipA, a Tyrosine and Lipid Phosphatase Involved in the Virulence of Listeria monocytogenes ▿ ▿ †

    doi: 10.1128/IAI.05073-11

    Figure Lengend Snippet: Expression of L. monocytogenes lipA in human blood. Transcriptional tiling maps of L. monocytogenes EGDe grown in BHI to exponential phase at 37°C (black dots) or in human blood at 37°C for 60 min (red dots) show normalized hybridization

    Article Snippet: L. monocytogenes strains were routinely grown in brain heart infusion (BHI) broth (Difco) at 37°C and 200 rpm or on Oxford agar plates (Merck) at 37°C.

    Techniques: Expressing, Hybridization

    Uptake of the Pro-[ 14 C]Ala peptide in L. monocytogenes EGD-e and L. monocytogenes Δ dtpT . Cells were grown in BHI to mid-exponential phase (OD 600 , 0.5) and washed twice in 240 mM sodium PIPES buffer (pH 6.0) containing 5 mM MgSO 4 . Assays of Pro-[

    Journal: Applied and Environmental Microbiology

    Article Title: Identification and Characterization of Di- and Tripeptide Transporter DtpT of Listeria monocytogenes EGD-e

    doi: 10.1128/AEM.71.10.5771-5778.2005

    Figure Lengend Snippet: Uptake of the Pro-[ 14 C]Ala peptide in L. monocytogenes EGD-e and L. monocytogenes Δ dtpT . Cells were grown in BHI to mid-exponential phase (OD 600 , 0.5) and washed twice in 240 mM sodium PIPES buffer (pH 6.0) containing 5 mM MgSO 4 . Assays of Pro-[

    Article Snippet: L. monocytogenes EGD-e was grown in brain heart infusion (BHI) broth (Difco) at 37°C.

    Techniques:

    Determination of growth curves of S. mutans UA159, S. mutans Δ stsR , and Δ stsR/pDL278-stsR . S. mutans UA159, S. mutans Δ stsR , and Δ stsR/pDL278-stsR strains were cultivated in BHI to mid-exponential phase and then diluted into (A) fresh BHI broth or (B) TV base medium supplemented with either 10 mM (limiting) or 100 mM (excess) sucrose, glucose, or lactose. Growth curves were monitored with a Multiskan Spectrum (Thermo, Multiskan Go, United States), and the OD 600 was measured in 1 h intervals. (A) For CFU counts, after diluted, the bacteria were cultured at 37°C for 1, 4, 8, and 12 h. Then bacterial suspension was serially diluted in BHI and plated on BHI agar plates. CFU values were calculated after the plates were incubated anaerobically at 37°C for 48 h. Error bars represent standard deviations based on results from at least three biological replicates.

    Journal: Frontiers in Microbiology

    Article Title: A GntR Family Transcription Factor in Streptococcus mutans Regulates Biofilm Formation and Expression of Multiple Sugar Transporter Genes

    doi: 10.3389/fmicb.2018.03224

    Figure Lengend Snippet: Determination of growth curves of S. mutans UA159, S. mutans Δ stsR , and Δ stsR/pDL278-stsR . S. mutans UA159, S. mutans Δ stsR , and Δ stsR/pDL278-stsR strains were cultivated in BHI to mid-exponential phase and then diluted into (A) fresh BHI broth or (B) TV base medium supplemented with either 10 mM (limiting) or 100 mM (excess) sucrose, glucose, or lactose. Growth curves were monitored with a Multiskan Spectrum (Thermo, Multiskan Go, United States), and the OD 600 was measured in 1 h intervals. (A) For CFU counts, after diluted, the bacteria were cultured at 37°C for 1, 4, 8, and 12 h. Then bacterial suspension was serially diluted in BHI and plated on BHI agar plates. CFU values were calculated after the plates were incubated anaerobically at 37°C for 48 h. Error bars represent standard deviations based on results from at least three biological replicates.

    Article Snippet: S. mutans UA159 and its derivatives were cultured in brain heart infusion (BHI) broth (Difco, Sparks, MD, United States) and on BHI agar or in biofilm medium (BM).

    Techniques: Cell Culture, Incubation