pneumoniae  (Worthington Biochemical)


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    Worthington Biochemical pneumoniae
    Differential PLY production by S . <t>pneumoniae</t> strains is directly related to PLY production. Lysis of primary human erythrocytes as assessed by hemoglobin release assay correlates with (A) ply 5’ mRNA ΔG and (B) PLY as measured by ELISA (R 2 = 0.95; outside lines represent 95% CI). *, P
    Pneumoniae, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 93/100, based on 185 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 185 article reviews
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    Images

    1) Product Images from "Rational Manipulation of mRNA Folding Free Energy Allows Rheostat Control of Pneumolysin Production by Streptococcus pneumoniae"

    Article Title: Rational Manipulation of mRNA Folding Free Energy Allows Rheostat Control of Pneumolysin Production by Streptococcus pneumoniae

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0119823

    Differential PLY production by S . pneumoniae strains is directly related to PLY production. Lysis of primary human erythrocytes as assessed by hemoglobin release assay correlates with (A) ply 5’ mRNA ΔG and (B) PLY as measured by ELISA (R 2 = 0.95; outside lines represent 95% CI). *, P
    Figure Legend Snippet: Differential PLY production by S . pneumoniae strains is directly related to PLY production. Lysis of primary human erythrocytes as assessed by hemoglobin release assay correlates with (A) ply 5’ mRNA ΔG and (B) PLY as measured by ELISA (R 2 = 0.95; outside lines represent 95% CI). *, P

    Techniques Used: Lysis, Release Assay, Enzyme-linked Immunosorbent Assay

    2) Product Images from "Pneumococcal HtrA Protease Mediates Inhibition of Competence by the CiaRH Two-Component Signaling System"

    Article Title: Pneumococcal HtrA Protease Mediates Inhibition of Competence by the CiaRH Two-Component Signaling System

    Journal: Journal of Bacteriology

    doi: 10.1128/JB.187.12.3969-3979.2005

    Western immunoblots for HtrA. (A and B) HtrA expression in bacterial lysates (A) and concentrated supernatants (B) from the wild type (0100993) and Δ ciaRH (P1149) (concentration factor, 4.3× relative to the culture volumes from which lysates were harvested). (C and D) Expression of HtrA (C) and pneumolysin (D) in subcellular fractions of S. pneumoniae (P1389, htrA + ciaH + ). Fractionation samples derived from 4.3 ml of original culture were loaded in each lane. Sonicates of whole bacteria containing 2.5 μg of protein from strains P143 (wt) and P1378 ( htrA Δ 298-1152 ) are shown as a control for specificity of the HtrA antibody.
    Figure Legend Snippet: Western immunoblots for HtrA. (A and B) HtrA expression in bacterial lysates (A) and concentrated supernatants (B) from the wild type (0100993) and Δ ciaRH (P1149) (concentration factor, 4.3× relative to the culture volumes from which lysates were harvested). (C and D) Expression of HtrA (C) and pneumolysin (D) in subcellular fractions of S. pneumoniae (P1389, htrA + ciaH + ). Fractionation samples derived from 4.3 ml of original culture were loaded in each lane. Sonicates of whole bacteria containing 2.5 μg of protein from strains P143 (wt) and P1378 ( htrA Δ 298-1152 ) are shown as a control for specificity of the HtrA antibody.

    Techniques Used: Western Blot, Expressing, Concentration Assay, Fractionation, Derivative Assay

    3) Product Images from "The NanA Neuraminidase of Streptococcus pneumoniae Is Involved in Biofilm Formation "

    Article Title: The NanA Neuraminidase of Streptococcus pneumoniae Is Involved in Biofilm Formation

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00228-09

    Imaging of S. pneumoniae biofilms. (A) Images of crystal violet-stained biofilms in microtiter wells for wild-type (WT) and nanA strains with D39 (after exposure to epithelial cells) and R6 backgrounds. (B) Fluorescence microscopy of wild-type strain D39 and nanA biofilms grown in microtiter trays after exposure to epithelial cells and stained with BacLight live/dead stain. Magnification, ×200. (C) Three-dimensional reconstruction of the biofilm structure for the wild-type strain shown in panel B. (D) Three-dimensional reconstruction of cells of the nanA strain shown in panel B.
    Figure Legend Snippet: Imaging of S. pneumoniae biofilms. (A) Images of crystal violet-stained biofilms in microtiter wells for wild-type (WT) and nanA strains with D39 (after exposure to epithelial cells) and R6 backgrounds. (B) Fluorescence microscopy of wild-type strain D39 and nanA biofilms grown in microtiter trays after exposure to epithelial cells and stained with BacLight live/dead stain. Magnification, ×200. (C) Three-dimensional reconstruction of the biofilm structure for the wild-type strain shown in panel B. (D) Three-dimensional reconstruction of cells of the nanA strain shown in panel B.

    Techniques Used: Imaging, Staining, Fluorescence, Microscopy

    S. pneumoniae biofilm formation. (A) Encapsulated (D39 background) strains were grown in microtiter trays without (filled bars) or with (striped bars) previous exposure to epithelial cells. Unencapsulated R6 strains were grown in microtiter trays without exposure to epithelial cells. (B) Incubation with NANA results in reduced biofilm formation by wild-type strain D39 (WT). Biofilms were measured by using crystal violet staining. Biofilm formation was normalized to growth and expressed as a percentage compared to the R6 wild-type strain. *, P
    Figure Legend Snippet: S. pneumoniae biofilm formation. (A) Encapsulated (D39 background) strains were grown in microtiter trays without (filled bars) or with (striped bars) previous exposure to epithelial cells. Unencapsulated R6 strains were grown in microtiter trays without exposure to epithelial cells. (B) Incubation with NANA results in reduced biofilm formation by wild-type strain D39 (WT). Biofilms were measured by using crystal violet staining. Biofilm formation was normalized to growth and expressed as a percentage compared to the R6 wild-type strain. *, P

    Techniques Used: Incubation, Staining

    4) Product Images from "Influence of two anti-fungal Lactobacillus fermentum-Saccharomyces cerevisiae co-cultures on cocoa bean fermentation and final bean quality"

    Article Title: Influence of two anti-fungal Lactobacillus fermentum-Saccharomyces cerevisiae co-cultures on cocoa bean fermentation and final bean quality

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0239365

    Fermentation building (a), fermentation and drying processes of inoculated and spontaneous fermentations, and ambient temperatures (b). Positions a and b indicate the two parts of the fermentation box in (a). In (b), the positioning of the fermentation boxes F-A, F-B, and F-S during IF, IIF, and IIIF in positions P1-P3 is indicated on the y-axis. The horizontal axis indicates the time of fermentation (black line) and drying (grey line) and time when the fermenting pulp-bean mass in the centre of the box reached temperatures of 45–50 °C (bold black line). P = position; A min = minimal ambient temperature; A max = maximal ambient temperature.
    Figure Legend Snippet: Fermentation building (a), fermentation and drying processes of inoculated and spontaneous fermentations, and ambient temperatures (b). Positions a and b indicate the two parts of the fermentation box in (a). In (b), the positioning of the fermentation boxes F-A, F-B, and F-S during IF, IIF, and IIIF in positions P1-P3 is indicated on the y-axis. The horizontal axis indicates the time of fermentation (black line) and drying (grey line) and time when the fermenting pulp-bean mass in the centre of the box reached temperatures of 45–50 °C (bold black line). P = position; A min = minimal ambient temperature; A max = maximal ambient temperature.

    Techniques Used:

    Temperatures in the fermenting pulp-bean mass of inoculated and spontaneous fermentations (a) and temperature distribution in the fermentation mass of IIF-A, representative for the nine studied fermentations (b). In part (a), temperatures measured in the centre of the box are shown for fermentation IF-A (bold bright grey line), IF-B (dashed bright grey line), IF-S (dotted bright grey line), IIF-A (bold dark grey line), IIF-B (dashed dark grey line), IIF-S (dotted dark grey line), IIIF-A (bold black line), IIIF-B (dashed black line), and IIIF-S (dotted black line). Ambient temperatures were measured in the fermentation building during run I (thin bright grey line), run II (thin dark grey line), and run III (thin black line). Part (b) shows temperatures measured at nine positions in fermentation box IIA: bottom-centre (solid bright grey line), bottom-side (dashed bright grey line), bottom-corner (dotted bright grey line), centre-centre (solid dark grey line), centre-side (dashed dark grey line), centre-corner (dotted dark grey line), top-centre (solid black line), top-side (dashed black line), and top-corner (dotted black line). 1–2 values deviated due to cold air being mixed with the pulp-bean mass and these were deleted to provide a clearer indication of temperature trends.
    Figure Legend Snippet: Temperatures in the fermenting pulp-bean mass of inoculated and spontaneous fermentations (a) and temperature distribution in the fermentation mass of IIF-A, representative for the nine studied fermentations (b). In part (a), temperatures measured in the centre of the box are shown for fermentation IF-A (bold bright grey line), IF-B (dashed bright grey line), IF-S (dotted bright grey line), IIF-A (bold dark grey line), IIF-B (dashed dark grey line), IIF-S (dotted dark grey line), IIIF-A (bold black line), IIIF-B (dashed black line), and IIIF-S (dotted black line). Ambient temperatures were measured in the fermentation building during run I (thin bright grey line), run II (thin dark grey line), and run III (thin black line). Part (b) shows temperatures measured at nine positions in fermentation box IIA: bottom-centre (solid bright grey line), bottom-side (dashed bright grey line), bottom-corner (dotted bright grey line), centre-centre (solid dark grey line), centre-side (dashed dark grey line), centre-corner (dotted dark grey line), top-centre (solid black line), top-side (dashed black line), and top-corner (dotted black line). 1–2 values deviated due to cold air being mixed with the pulp-bean mass and these were deleted to provide a clearer indication of temperature trends.

    Techniques Used:

    5) Product Images from "Molecular Characterization of N-glycan Degradation and Transport in Streptococcus pneumoniae and Its Contribution to Virulence"

    Article Title: Molecular Characterization of N-glycan Degradation and Transport in Streptococcus pneumoniae and Its Contribution to Virulence

    Journal: PLoS Pathogens

    doi: 10.1371/journal.ppat.1006090

    Proposed model of N-glycan metabolism in Streptococcus pneumoniae . The two arms of N-glycan processing—complex N-glycan (top) and high-mannose N-glycan (bottom)—are shown as graphical representations and converge at ABC NG . Glycosidases are colour-coded according to their known or predicted activities: sialidase (purple), β-galactosidase (yellow), β-hexosaminidase (blue) and α-mannosidase (green). StrH is shown as a multimodular complex as it contains two catalytic domains [ 53 ]. NanA, BgaA, StrH and EndoD are extracellular and all bear LPXTG cell wall anchoring motifs. Complex N-glycan is sequentially depolymerized by NanA, BgaA and StrH [ 18 ], resulting in Man 3 GlcNAc 2 , which is then released from the glycoconjugate by EndoD [ 20 ]. High-mannose N-glycan is acted on by SpGH92, to produce Man 5 GlcNAc 2 , and is then released from the glycoconjugate by EndoD. Both Man 3 GlcNAc and Man 5 GlcNAc are transported by ABC NG into the cytoplasm, where further depolymerization is carried out by SpGH125 and SpGH38. Dedicated ABC and PTS transporters import the monosaccharides released by NanA, BgaA, StrH and SpGH92 [ 51 ]. The proposed architecture of ABC NG is shown inset. Abbreviations: cytoplasmic membrane (M); peptidoglycan (PG).
    Figure Legend Snippet: Proposed model of N-glycan metabolism in Streptococcus pneumoniae . The two arms of N-glycan processing—complex N-glycan (top) and high-mannose N-glycan (bottom)—are shown as graphical representations and converge at ABC NG . Glycosidases are colour-coded according to their known or predicted activities: sialidase (purple), β-galactosidase (yellow), β-hexosaminidase (blue) and α-mannosidase (green). StrH is shown as a multimodular complex as it contains two catalytic domains [ 53 ]. NanA, BgaA, StrH and EndoD are extracellular and all bear LPXTG cell wall anchoring motifs. Complex N-glycan is sequentially depolymerized by NanA, BgaA and StrH [ 18 ], resulting in Man 3 GlcNAc 2 , which is then released from the glycoconjugate by EndoD [ 20 ]. High-mannose N-glycan is acted on by SpGH92, to produce Man 5 GlcNAc 2 , and is then released from the glycoconjugate by EndoD. Both Man 3 GlcNAc and Man 5 GlcNAc are transported by ABC NG into the cytoplasm, where further depolymerization is carried out by SpGH125 and SpGH38. Dedicated ABC and PTS transporters import the monosaccharides released by NanA, BgaA, StrH and SpGH92 [ 51 ]. The proposed architecture of ABC NG is shown inset. Abbreviations: cytoplasmic membrane (M); peptidoglycan (PG).

    Techniques Used:

    Organization and conservation of a Carbohydrate Processing Locus (CPL) and other accessory proteins predicted to be associated with N-glycan processing. Genetic organization of a CPL and other accessory ORFs present in strains of S . pneumoniae whose protein products are putatively associated with N-glycan processing. The CPL consists of a characterized α-(1,6)-mannosidase (SpGH125) [ 21 ], two putative α-mannosidases (SpGH38 and SpGH92), a predicted α-fucosidase (GH29), a putative sugar kinase (ROK) and a known exo -β-hexosaminidase (SpGH20C) [ 28 ]. Other conserved proteins predicted to be associated with N-glycan processing include a characterized endo-β-N-acetylglucosaminidase (SpGH85 or EndoD) that is active on the core of N-linked glycans [ 24 ] and an ABC transporter (ABC NG ) that consists of a predicted solute binding protein (NgtS) and two putative permeases (NgtP1 and NgtP2). Locus tags shown underneath ORFs relate to the TIGR4 genome; black bars underneath ORFS indicate genes that are predicted to be co-transcribed. For the majority of the ORFs, coloring corresponds to the type of configured sugar acted on by the hydrolase: fucose (red), glucose (blue) and mannose (green).
    Figure Legend Snippet: Organization and conservation of a Carbohydrate Processing Locus (CPL) and other accessory proteins predicted to be associated with N-glycan processing. Genetic organization of a CPL and other accessory ORFs present in strains of S . pneumoniae whose protein products are putatively associated with N-glycan processing. The CPL consists of a characterized α-(1,6)-mannosidase (SpGH125) [ 21 ], two putative α-mannosidases (SpGH38 and SpGH92), a predicted α-fucosidase (GH29), a putative sugar kinase (ROK) and a known exo -β-hexosaminidase (SpGH20C) [ 28 ]. Other conserved proteins predicted to be associated with N-glycan processing include a characterized endo-β-N-acetylglucosaminidase (SpGH85 or EndoD) that is active on the core of N-linked glycans [ 24 ] and an ABC transporter (ABC NG ) that consists of a predicted solute binding protein (NgtS) and two putative permeases (NgtP1 and NgtP2). Locus tags shown underneath ORFs relate to the TIGR4 genome; black bars underneath ORFS indicate genes that are predicted to be co-transcribed. For the majority of the ORFs, coloring corresponds to the type of configured sugar acted on by the hydrolase: fucose (red), glucose (blue) and mannose (green).

    Techniques Used: Binding Assay

    EndoD and NgtS contribute to growth of S . pneumoniae on a model glycoconjugate. Growth of deletion mutants of S . pneumoniae TIGR4 Sm r on the model glycoconjugate fetuin. Deletion mutants of (A) endoD , (B) ngtS-P1-P2 and (C) endoD plus ngtS-P1-P2 were grown in chemically-defined medium supplemented with 20 mg ml -1 fetuin as the sole carbon source and compared against their genetically reconstituted strains. All OD 600nm readings shown are the mean from three independent experiments each performed in triplicate. Gray shading indicates the 95% confidence intervals for each strain and statistically significant differences in growth.
    Figure Legend Snippet: EndoD and NgtS contribute to growth of S . pneumoniae on a model glycoconjugate. Growth of deletion mutants of S . pneumoniae TIGR4 Sm r on the model glycoconjugate fetuin. Deletion mutants of (A) endoD , (B) ngtS-P1-P2 and (C) endoD plus ngtS-P1-P2 were grown in chemically-defined medium supplemented with 20 mg ml -1 fetuin as the sole carbon source and compared against their genetically reconstituted strains. All OD 600nm readings shown are the mean from three independent experiments each performed in triplicate. Gray shading indicates the 95% confidence intervals for each strain and statistically significant differences in growth.

    Techniques Used:

    6) Product Images from "The NanA Neuraminidase of Streptococcus pneumoniae Is Involved in Biofilm Formation "

    Article Title: The NanA Neuraminidase of Streptococcus pneumoniae Is Involved in Biofilm Formation

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00228-09

    Imaging of S. pneumoniae biofilms. (A) Images of crystal violet-stained biofilms in microtiter wells for wild-type (WT) and nanA strains with D39 (after exposure to epithelial cells) and R6 backgrounds. (B) Fluorescence microscopy of wild-type strain D39 and nanA biofilms grown in microtiter trays after exposure to epithelial cells and stained with BacLight live/dead stain. Magnification, ×200. (C) Three-dimensional reconstruction of the biofilm structure for the wild-type strain shown in panel B. (D) Three-dimensional reconstruction of cells of the nanA strain shown in panel B.
    Figure Legend Snippet: Imaging of S. pneumoniae biofilms. (A) Images of crystal violet-stained biofilms in microtiter wells for wild-type (WT) and nanA strains with D39 (after exposure to epithelial cells) and R6 backgrounds. (B) Fluorescence microscopy of wild-type strain D39 and nanA biofilms grown in microtiter trays after exposure to epithelial cells and stained with BacLight live/dead stain. Magnification, ×200. (C) Three-dimensional reconstruction of the biofilm structure for the wild-type strain shown in panel B. (D) Three-dimensional reconstruction of cells of the nanA strain shown in panel B.

    Techniques Used: Imaging, Staining, Fluorescence, Microscopy

    S. pneumoniae biofilm formation. (A) Encapsulated (D39 background) strains were grown in microtiter trays without (filled bars) or with (striped bars) previous exposure to epithelial cells. Unencapsulated R6 strains were grown in microtiter trays without exposure to epithelial cells. (B) Incubation with NANA results in reduced biofilm formation by wild-type strain D39 (WT). Biofilms were measured by using crystal violet staining. Biofilm formation was normalized to growth and expressed as a percentage compared to the R6 wild-type strain. *, P
    Figure Legend Snippet: S. pneumoniae biofilm formation. (A) Encapsulated (D39 background) strains were grown in microtiter trays without (filled bars) or with (striped bars) previous exposure to epithelial cells. Unencapsulated R6 strains were grown in microtiter trays without exposure to epithelial cells. (B) Incubation with NANA results in reduced biofilm formation by wild-type strain D39 (WT). Biofilms were measured by using crystal violet staining. Biofilm formation was normalized to growth and expressed as a percentage compared to the R6 wild-type strain. *, P

    Techniques Used: Incubation, Staining

    Inhibitory activity of potential NanA inhibitors. (A) Screening of potential inhibitors was performed with NanA and inhibitors at a concentration of 100 μM in the neuraminidase assay. Results are percentages of the level for the control without any inhibitor. (B) Dose-response curve for NanA with lead compound XX1. Data were fitted with a logarithmically based trend line. The data are the percentages of activity compared to the control with only the vehicle (dimethyl sulfoxide). (C) Biofilm formation by wild-type strain D39 (WT) grown in the presence of XX1 during exposure to epithelial cells and growth in microtiter trays. The nanA strain was used as a reference. Biofilm formation was normalized to growth and was expressed as a percentage compared to the results for the wild-type control. (D) Chemical structure of XX1. *, P
    Figure Legend Snippet: Inhibitory activity of potential NanA inhibitors. (A) Screening of potential inhibitors was performed with NanA and inhibitors at a concentration of 100 μM in the neuraminidase assay. Results are percentages of the level for the control without any inhibitor. (B) Dose-response curve for NanA with lead compound XX1. Data were fitted with a logarithmically based trend line. The data are the percentages of activity compared to the control with only the vehicle (dimethyl sulfoxide). (C) Biofilm formation by wild-type strain D39 (WT) grown in the presence of XX1 during exposure to epithelial cells and growth in microtiter trays. The nanA strain was used as a reference. Biofilm formation was normalized to growth and was expressed as a percentage compared to the results for the wild-type control. (D) Chemical structure of XX1. *, P

    Techniques Used: Activity Assay, Concentration Assay

    7) Product Images from "Cellular effectors mediating Th17-dependent clearance of pneumococcal colonization in mice"

    Article Title: Cellular effectors mediating Th17-dependent clearance of pneumococcal colonization in mice

    Journal: The Journal of Clinical Investigation

    doi: 10.1172/JCI36731

    Colonization with strain P1121 led to mucosal and systemic CD4 + T cell responses, which were attenuated in the absence of TLR2 signaling.
    Figure Legend Snippet: Colonization with strain P1121 led to mucosal and systemic CD4 + T cell responses, which were attenuated in the absence of TLR2 signaling.

    Techniques Used:

    Monocyte/macrophage influx is required for clearance of pneumococcal strain P1121.
    Figure Legend Snippet: Monocyte/macrophage influx is required for clearance of pneumococcal strain P1121.

    Techniques Used:

    Cytokine IL-17A and CD4 + but not CD8 + T cells are required for strain P1121 clearance and monocyte/macrophage recruitment.
    Figure Legend Snippet: Cytokine IL-17A and CD4 + but not CD8 + T cells are required for strain P1121 clearance and monocyte/macrophage recruitment.

    Techniques Used:

    Macrophages are recruited to nasopharynx in association with clearance of pneumococcal isolate P1121, and responses are attenuated in the absence of TLR2 signaling.
    Figure Legend Snippet: Macrophages are recruited to nasopharynx in association with clearance of pneumococcal isolate P1121, and responses are attenuated in the absence of TLR2 signaling.

    Techniques Used:

    8) Product Images from "Synergistic stimulation of type I interferons during influenza virus coinfection promotes Streptococcus pneumoniae colonization in mice"

    Article Title: Synergistic stimulation of type I interferons during influenza virus coinfection promotes Streptococcus pneumoniae colonization in mice

    Journal: The Journal of Clinical Investigation

    doi: 10.1172/JCI57762

    Macrophages and Nod2 contribute to production of type I IFN by S. pneumoniae .
    Figure Legend Snippet: Macrophages and Nod2 contribute to production of type I IFN by S. pneumoniae .

    Techniques Used:

    IFN-β inhibits production of CCL2 in peritoneal macrophage stimulated with heat-killed S. pneumoniae .
    Figure Legend Snippet: IFN-β inhibits production of CCL2 in peritoneal macrophage stimulated with heat-killed S. pneumoniae .

    Techniques Used:

    Related Articles

    Concentration Assay:

    Article Title: Variation in Plasmodium falciparum Erythrocyte Invasion Phenotypes and Merozoite Ligand Gene Expression across Different Populations in Areas of Malaria Endemicity
    Article Snippet: .. Neuraminidase ( Vibrio cholerae ; Sigma, United Kingdom) was used at a final concentration of 100 mU/ml, trypsin (TPCK [tosylsulfonyl phenylalanyl chloromethyl ketone] treated, bovine) (Sigma, United Kingdom) at 104 U/ml, and chymotrypsin (TLCK [ N α- p -tosyl- l -lysine chloromethyl ketone] treated) (Worthington, USA) at 45 U/ml. ..

    Article Title: Ecotin, a microbial inhibitor of serine proteases, blocks multiple complement dependent and independent microbicidal activities of human serum
    Article Snippet: .. Then, serial dilutions of the buffered periplasmic fractions were mixed with 20 nM final concentration of bovine chymotrypsin (Worthington, #LS001432) and incubated for 1 hour. .. Free residual enzyme concentration was determined by 250 μM Suc-Ala-Ala-Pro-Phe-PNA substrate (Bachem AG, #1067440).

    Incubation:

    Article Title: Lipids Cooperate with the Reovirus Membrane Penetration Peptide to Facilitate Particle Uncoating
    Article Snippet: .. Following the viral attachment incubation, the monolayers were overlaid with 4 ml of serum-free medium 199 (Sigma-Aldrich) supplemented with 1% Bacto Agar (BD Biosciences), 10 μg/ml TLCK-treated chymotrypsin (Worthington Biochemical), 2 m m l -glutamine (Invitrogen), 100 units/ml penicillin (Invitrogen), 100 μg/ml streptomycin (Invitrogen), and 25 ng/ml amphotericin B (Sigma-Aldrich) The infected cells were incubated at 37 °C, and plaques were counted 5 days after infection. .. The supernatant of preconverted ISVP*s was generated as described previously ( , ).

    Article Title: Cleavage of the C-Terminal Fragment of Reovirus μ1 Is Required for Optimal Infectivity
    Article Snippet: .. Following the viral attachment incubation, the monolayers were overlaid with 4 ml of serum-free medium 199 (Sigma-Aldrich) supplemented with 1% Bacto agar (BD Biosciences), 10 μg/ml of TLCK-treated chymotrypsin (Worthington Biochemical), 2 mM l -glutamine (Invitrogen), 100 U/ml of penicillin (Invitrogen), 100 μg/ml of streptomycin (Invitrogen), and 25 ng/ml of amphotericin B (Sigma-Aldrich). .. The infected cells were incubated at 37°C, and plaques were counted 5 days postinfection.

    Article Title: Selection and Characterization of a Reovirus Mutant with Increased Thermostability
    Article Snippet: .. Following the viral attachment incubation, the monolayers were overlaid with 4 ml of serum-free medium 199 (Sigma-Aldrich) supplemented with 1% Bacto agar (BD Biosciences), 10 μg/ml TLCK-treated chymotrypsin (Worthington Biochemical), 2 mM l -glutamine (Invitrogen), 100 U/ml penicillin (Invitrogen), 100 μg/ml streptomycin (Invitrogen), and 25 ng/ml amphotericin B (Sigma-Aldrich). .. The infected cells were incubated at 37°C, and plaques were counted at 5 days postinfection.

    Article Title: Components of the Reovirus Capsid Differentially Contribute to Stability
    Article Snippet: .. After the viral attachment incubation, the monolayers were overlaid with 4 ml of serum-free medium 199 (Sigma-Aldrich) supplemented with 1% Bacto Agar (BD Biosciences), 10 μg/ml TLCK-treated chymotrypsin (Worthington Biochemical), 2 mM l -glutamine (Invitrogen), 100 U/ml penicillin (Invitrogen), 100 μg/ml streptomycin (Invitrogen), and 25 ng/ml amphotericin B (Sigma-Aldrich). .. The infected cells were incubated at 37°C, and plaques were counted at 5 days postinfection.

    Article Title: Ecotin, a microbial inhibitor of serine proteases, blocks multiple complement dependent and independent microbicidal activities of human serum
    Article Snippet: .. Then, serial dilutions of the buffered periplasmic fractions were mixed with 20 nM final concentration of bovine chymotrypsin (Worthington, #LS001432) and incubated for 1 hour. .. Free residual enzyme concentration was determined by 250 μM Suc-Ala-Ala-Pro-Phe-PNA substrate (Bachem AG, #1067440).

    Infection:

    Article Title: Lipids Cooperate with the Reovirus Membrane Penetration Peptide to Facilitate Particle Uncoating
    Article Snippet: .. Following the viral attachment incubation, the monolayers were overlaid with 4 ml of serum-free medium 199 (Sigma-Aldrich) supplemented with 1% Bacto Agar (BD Biosciences), 10 μg/ml TLCK-treated chymotrypsin (Worthington Biochemical), 2 m m l -glutamine (Invitrogen), 100 units/ml penicillin (Invitrogen), 100 μg/ml streptomycin (Invitrogen), and 25 ng/ml amphotericin B (Sigma-Aldrich) The infected cells were incubated at 37 °C, and plaques were counted 5 days after infection. .. The supernatant of preconverted ISVP*s was generated as described previously ( , ).

    Purification:

    Article Title: Components of the Reovirus Capsid Differentially Contribute to Stability
    Article Snippet: .. Purified virions of T1L (3.2 × 1013 particles/ml), T1L/T3D M2 (4.0 × 1013 particles/ml), or T3D/T1L S4 (2.8 × 1013 particles/ml) were digested with 200 μg/ml TLCK-treated chymotrypsin (Worthington Biochemical) in a total volume of 500 μl for 2 h at 37°C ( ). .. The reactions were then incubated on ice for 20 min and quenched by the addition of 1 mM PMSF (Sigma-Aldrich).

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