Journal: Scientific Reports

Article Title: Effect of the type of reducing agents of silver ions in interpolyelectrolyte-metal complexes on the structure, morphology and properties of silver-containing nanocomposites

doi: 10.1038/s41598-020-64079-0

Figure Lengend Snippet: Images of antimicrobial test results of agar plates Ag-containing nanocomposites, obtained via chemical reduction of Ag + ions in the polymer films against S. aureus ( a ) and E. coli ( b ).

Article Snippet: The antimicrobial activity of IPEC–Ag nanocomposites, prepared by chemical reduction of Ag + ions in IMC was investigated using reference strains of opportunistic bacteria Staphylococcus aureus ATCC 6538 and Escherichia coli ATCC 35218 (as a model gram-positive and gram-negative bacteriа) .

Techniques: Polymer

Journal: bioRxiv

Article Title: DPP9 directly sequesters the NLRP1 C-terminus to repress inflammasome activation

doi: 10.1101/2020.08.14.246132

Figure Lengend Snippet: a , Domain organization. b , SDS-PAGE of the purified NLRP1-DPP9 complex. HSP70 contamination is noted with an asterisk (*). c , Cryo-EM map (left) and the model (right) of the ternary NLRP1 A -NLRP1 B -DPP9 complex. The DPP9 dimer and the two copies of NLRP1 (A and B) are labelled with the colour scheme in (a). A schematic diagram (middle) denotes the entire NLRP1 and DPP9 molecules versus the ordered, resolved portions of the proteins (red circle). d , FIIND A overview with ZU5 (blue) and UPA (light pink) subdomains. The catalytic triad residues (H1186, E1195, and S1213) are shown in sticks. e , Topology of the FIIND with secondary structures labelled. f , Superimposition of FIIND A onto the UPA B . NLRP1 B has to be free NLRP1-CT because a ZU5 subdomain at site B would have clashed with ZU5 and UPA at site A and with DPP9.

Article Snippet: Primary antibodies used in this study include: DPP9 rabbit polyclonal Ab (Abcam, Ab42080), FLAG® M2 mouse monoclonal Ab (Sigma, F3165), GAPDH rabbit monoclonal Ab (Cell Signaling Technology, 14C10), NLRP1 mouse monoclonal Ab (R&D Systems, MAB6788), CASP1 rabbit polyclonal Ab (Cell Signaling Technology, 2225), GSDMDC1 rabbit polyclonal Ab (Novus, NBP2-33422), V5 rabbit polyclonal Ab (Abcam, Ab9116).

Techniques: SDS Page, Purification, Cryo-EM Sample Prep

Journal: bioRxiv

Article Title: DPP9 directly sequesters the NLRP1 C-terminus to repress inflammasome activation

doi: 10.1101/2020.08.14.246132

Figure Lengend Snippet: a , Purification of the NLRP1-DPP9 complex by ion exchange chromatography. The ternary complex peak is shaded in green and labelled with an arrow. b , A representative cryo-EM micrograph. c , Representative 2D class averages. d , Workflow for the NLRP1-DPP9 complex structure determination. e , Map-map and map-model FSC curves. f , Local resolution distribution of the final map calculated with ResMap .

Article Snippet: Primary antibodies used in this study include: DPP9 rabbit polyclonal Ab (Abcam, Ab42080), FLAG® M2 mouse monoclonal Ab (Sigma, F3165), GAPDH rabbit monoclonal Ab (Cell Signaling Technology, 14C10), NLRP1 mouse monoclonal Ab (R&D Systems, MAB6788), CASP1 rabbit polyclonal Ab (Cell Signaling Technology, 2225), GSDMDC1 rabbit polyclonal Ab (Novus, NBP2-33422), V5 rabbit polyclonal Ab (Abcam, Ab9116).

Techniques: Purification, Ion Exchange Chromatography, Cryo-EM Sample Prep

Journal: bioRxiv

Article Title: DPP9 directly sequesters the NLRP1 C-terminus to repress inflammasome activation

doi: 10.1101/2020.08.14.246132

Figure Lengend Snippet: a , Summary of BS3 crosslinking between DPP9 and NLRP1. High confidence crosslinked peptides are displayed, with residue ranges labelled and colours coded by domains. Crosslinked lysine pairs are indicated in red. Cα-Cα distances between these lysine residues interpreted by the final NLRP1-DPP9 model are shown, along with the figure panel names for their detailed depictions. b , Overview of BS3-mediated crosslinks. c-h , Zoom-ins highlighting crosslinked lysine pairs (red) interpreted by the final NLRP1-DPP9 model.

Article Snippet: Primary antibodies used in this study include: DPP9 rabbit polyclonal Ab (Abcam, Ab42080), FLAG® M2 mouse monoclonal Ab (Sigma, F3165), GAPDH rabbit monoclonal Ab (Cell Signaling Technology, 14C10), NLRP1 mouse monoclonal Ab (R&D Systems, MAB6788), CASP1 rabbit polyclonal Ab (Cell Signaling Technology, 2225), GSDMDC1 rabbit polyclonal Ab (Novus, NBP2-33422), V5 rabbit polyclonal Ab (Abcam, Ab9116).

Techniques: Residue

Journal: bioRxiv

Article Title: DPP9 directly sequesters the NLRP1 C-terminus to repress inflammasome activation

doi: 10.1101/2020.08.14.246132

Figure Lengend Snippet: a , ClustalW multiple sequence alignment between human NLRP1 (hNLRP1), mouse NLRP1 (mNLRP1, different isoforms), and rat NLRP1 (rNLRP1, different isoforms). COP: Copenhagen; ZUC: Zucker; LEW: Lewis; SD: Sprague Dawley; and CDF: Fischer. Secondary structures and residue numbers are denoted based on the human FIIND A structure in the NLRP1-DPP9 ternary complex. Interfacial residues in the NLRP1-DPP9 complex are annotated with asterisks, and residues in the catalytic triad (H1186, E1195, S1213) are boxed in black. b , The ZU5 A -UPA A -UPA B module that binds DPP9. UPA A and UPA B interact with each other in a front-to-back manner with only a 9° rotation between them. c , Altered conformation of the UPA B N-terminus that binds in the DPP9 active site tunnel in comparison to UPA A in a complete FIIND A .

Article Snippet: Primary antibodies used in this study include: DPP9 rabbit polyclonal Ab (Abcam, Ab42080), FLAG® M2 mouse monoclonal Ab (Sigma, F3165), GAPDH rabbit monoclonal Ab (Cell Signaling Technology, 14C10), NLRP1 mouse monoclonal Ab (R&D Systems, MAB6788), CASP1 rabbit polyclonal Ab (Cell Signaling Technology, 2225), GSDMDC1 rabbit polyclonal Ab (Novus, NBP2-33422), V5 rabbit polyclonal Ab (Abcam, Ab9116).

Techniques: Sequencing, Residue, Comparison

Journal: bioRxiv

Article Title: DPP9 directly sequesters the NLRP1 C-terminus to repress inflammasome activation

doi: 10.1101/2020.08.14.246132

Figure Lengend Snippet: a , Insertion of the N-terminal peptide of UPA B into the DPP9 active site. b , Displacement of the UPA B N-terminal peptide from the DPP9 active site by VbP. c , Cryo-EM map of the NLRP1-DPP9 complex in the presence of VbP. VbP binding reduces UPA B occupancy. d , Ability of DPP9 to cleave an isolated UPA N-terminal peptide, but not an entire UPA. e , Comparison of the binding modes of the UPA B N-terminal peptide in the NLRP1-DPP9 complex and the Ile-Pro dipeptide in an acyl-enzyme intermediate . f , Overview of three interfaces important for NLRP1-DPP9 association. Regions blocked in rectangles are shown in detail in (a) and (g-i). g-i , Zoom-ins of each NLRP1-DPP9 binding interface. j , FLAG co-immunoprecipitation using FLAG-tagged WT NLRP1 and His-tagged WT and mutant DPP9. Anti-DPP9, anti-NLRP1-CT (NLRP1-FL and NLRP1-CT), and anti-GAPDH antibodies were used in the immunoblots. EV: empty vector. The Roman numerals in the parentheses represent the three interfaces in the NLRP1-DPP9 ternary complex. Each immunoblot is representative of > 2 independent experiments. k , FLAG co-immunoprecipitation using FLAG-tagged WT or mutant NLRP1 and His-tagged WT DPP9. FLAG-tagged GFP was used as a negative control. Anti-DPP9, anti-FLAG (NLRP1-FL, NLRP1-CT, and GFP), and anti-GAPDH antibodies were used in the immunoblots. The Roman numerals in parentheses represent the three interfaces in the NLRP1-DPP9 ternary complex. Each immunoblot is representative of > 2 independent experiments.

Article Snippet: Primary antibodies used in this study include: DPP9 rabbit polyclonal Ab (Abcam, Ab42080), FLAG® M2 mouse monoclonal Ab (Sigma, F3165), GAPDH rabbit monoclonal Ab (Cell Signaling Technology, 14C10), NLRP1 mouse monoclonal Ab (R&D Systems, MAB6788), CASP1 rabbit polyclonal Ab (Cell Signaling Technology, 2225), GSDMDC1 rabbit polyclonal Ab (Novus, NBP2-33422), V5 rabbit polyclonal Ab (Abcam, Ab9116).

Techniques: Cryo-EM Sample Prep, Binding Assay, Isolation, Comparison, Immunoprecipitation, Mutagenesis, Western Blot, Plasmid Preparation, Negative Control

Journal: bioRxiv

Article Title: DPP9 directly sequesters the NLRP1 C-terminus to repress inflammasome activation

doi: 10.1101/2020.08.14.246132

Figure Lengend Snippet: a , Purification of the NLRP1-DPP9 complex in the presence of VbP by ion exchange chromatography. The ternary complex peak is shaded in green and labelled with an arrow. b , A representative cryo-EM micrograph. c , Representative 2D class averages. d , Workflow for the NLRP1-DPP9-VbP complex structure determination. e , Map-map and map-model FSC curves. f , Local resolution distribution of the final map calculated with ResMap .

Article Snippet: Primary antibodies used in this study include: DPP9 rabbit polyclonal Ab (Abcam, Ab42080), FLAG® M2 mouse monoclonal Ab (Sigma, F3165), GAPDH rabbit monoclonal Ab (Cell Signaling Technology, 14C10), NLRP1 mouse monoclonal Ab (R&D Systems, MAB6788), CASP1 rabbit polyclonal Ab (Cell Signaling Technology, 2225), GSDMDC1 rabbit polyclonal Ab (Novus, NBP2-33422), V5 rabbit polyclonal Ab (Abcam, Ab9116).

Techniques: Purification, Ion Exchange Chromatography, Cryo-EM Sample Prep

Journal: bioRxiv

Article Title: DPP9 directly sequesters the NLRP1 C-terminus to repress inflammasome activation

doi: 10.1101/2020.08.14.246132

Figure Lengend Snippet: a , N-terminal sequencing of the purified NLRP1-DPP9 complex showing that the NLRP1-CT is not cleaved by the co-expressed DPP9. b , CHOPS assay showing that DPP9 does not cleave NLRP1-CT. Briefly, WT NLRP1 expressed in DPP8/9 DKO HEK293T cells was incubated with PBS or recombinant DPP9 prior to labelling with the 2PCA biotin probe to capture biotinylated proteins. The inputs and the eluents were analysed by immunoblots using anti-NLRP1-CT (NLRP1-FL and NLRP1-CT), anti-GAPDH, and anti-Biotin antibodies. c , Evidence of cleavage of the isolated 15 residue N-terminal peptide in NLRP1-CT by recombinant DPP9 from mass spectrometry analysis. d , Inhibition of DPP9 catalytic activity against AP-AMC by the isolated NLRP1-CT peptide. All data are representative of > 2 independent experiments.

Article Snippet: Primary antibodies used in this study include: DPP9 rabbit polyclonal Ab (Abcam, Ab42080), FLAG® M2 mouse monoclonal Ab (Sigma, F3165), GAPDH rabbit monoclonal Ab (Cell Signaling Technology, 14C10), NLRP1 mouse monoclonal Ab (R&D Systems, MAB6788), CASP1 rabbit polyclonal Ab (Cell Signaling Technology, 2225), GSDMDC1 rabbit polyclonal Ab (Novus, NBP2-33422), V5 rabbit polyclonal Ab (Abcam, Ab9116).

Techniques: Sequencing, Purification, Incubation, Recombinant, Western Blot, Isolation, Residue, Mass Spectrometry, Inhibition, Activity Assay

Journal: bioRxiv

Article Title: DPP9 directly sequesters the NLRP1 C-terminus to repress inflammasome activation

doi: 10.1101/2020.08.14.246132

Figure Lengend Snippet: a , Disorder to order transition of several DPP9 surface loops from the isolated DPP9 crystal structure (PDB ID: 6EOQ) to the NLRP1-bound DPP9 cryo-EM structure. b , Genomic confirmation of DPP8 KO in DPP8/9 DKO HEK293T cells. Single guide RNA (sgRNA) sequence is highlighted. c , Immunoblots of the input lysates for the FLAG co-immunoprecipitation with WT or mutant DPP9 and WT NLRP1-FLAG. d , Cleavage rate of a model DPP9 substrate, GP-AMC, by WT DPP9 and its structure-guided mutants. Only the catalytically dead mutant S730A disrupts catalytic activity and sensitivity to the DPP9 inhibitor, VbP. e , Immunoblots of the input lysates for the FLAG co-immunoprecipitation with WT or mutant NLRP1-FLAG and WT DPP9. All data are representative of > 2 independent experiments.

Article Snippet: Primary antibodies used in this study include: DPP9 rabbit polyclonal Ab (Abcam, Ab42080), FLAG® M2 mouse monoclonal Ab (Sigma, F3165), GAPDH rabbit monoclonal Ab (Cell Signaling Technology, 14C10), NLRP1 mouse monoclonal Ab (R&D Systems, MAB6788), CASP1 rabbit polyclonal Ab (Cell Signaling Technology, 2225), GSDMDC1 rabbit polyclonal Ab (Novus, NBP2-33422), V5 rabbit polyclonal Ab (Abcam, Ab9116).

Techniques: Isolation, Cryo-EM Sample Prep, Sequencing, Western Blot, Immunoprecipitation, Mutagenesis, Activity Assay

Journal: bioRxiv

Article Title: DPP9 directly sequesters the NLRP1 C-terminus to repress inflammasome activation

doi: 10.1101/2020.08.14.246132

Figure Lengend Snippet: Interface I and II mutants cause NLRP1 autoactivation and UPA-UPA interactions are required for inflammasome activity. a , LDH release (top) and GSDMD processing (bottom) from transient expression of empty vector (EV), WT or mutant NLRP1-FL, or UPA-CARD in a reconstituted HEK293 inflammasome system, with and without addition of VbP. Anti-NLRP1-CT (FL and CT), anti-GSDMD, and anti-GAPDH antibodies were used in the immunoblots. *: non-specific bands; p30: GSDND N-terminal fragment from caspase-1 cleavage. b , Quantification of speck formation induced by expression of EV, WT or mutant NLRP1-FL, or UPA-CARD in the presence and absence of VbP. c , LDH release (top) and GSDMD processing (bottom) by direct expression of WT or mutant NLRP1 UPA-CARDs. CARD alone was also included. d , Quantification of speck formation induced by expression of WT or mutant NLRP1 UPA-CARD. e , A modelled UPA oligomer based on the near front-to-back interaction in the NLRP1-DPP9 ternary complex. In the model, the N-terminal tails of free UPAs are shown in either the UPA A or UPA B conformation in complex with DPP9, but in reality, this conformation is likely to be different. All data are representative of > 3 independent experiments. **** in (a) and (b): p < 0.0001 compared to EV by 2-way ANOVA with Tukey multiple comparison correction. *** in (c) and (d): p < 0.001 by two-sided Student’s t test.

Article Snippet: Primary antibodies used in this study include: DPP9 rabbit polyclonal Ab (Abcam, Ab42080), FLAG® M2 mouse monoclonal Ab (Sigma, F3165), GAPDH rabbit monoclonal Ab (Cell Signaling Technology, 14C10), NLRP1 mouse monoclonal Ab (R&D Systems, MAB6788), CASP1 rabbit polyclonal Ab (Cell Signaling Technology, 2225), GSDMDC1 rabbit polyclonal Ab (Novus, NBP2-33422), V5 rabbit polyclonal Ab (Abcam, Ab9116).

Techniques: Activity Assay, Expressing, Plasmid Preparation, Mutagenesis, Western Blot, Comparison

Journal: bioRxiv

Article Title: DPP9 directly sequesters the NLRP1 C-terminus to repress inflammasome activation

doi: 10.1101/2020.08.14.246132

Figure Lengend Snippet: a , Co-expression of GFP-ASC and NLRP1-FL (WT and mutants) or UPA-CARD (positive control). Autoactive constructs form GFP-ASC specks in the absence of VbP. Image quantitation is shown in . b , Enlarged GFP-ASC panels from (a). c , Co-expression of GFP-ASC and UPA-CARD (WT and interface III mutants). Image quantitation is shown in . d , Enlarged GFP-ASC panels from (c). All data are representative of > 3 independent experiments.

Article Snippet: Primary antibodies used in this study include: DPP9 rabbit polyclonal Ab (Abcam, Ab42080), FLAG® M2 mouse monoclonal Ab (Sigma, F3165), GAPDH rabbit monoclonal Ab (Cell Signaling Technology, 14C10), NLRP1 mouse monoclonal Ab (R&D Systems, MAB6788), CASP1 rabbit polyclonal Ab (Cell Signaling Technology, 2225), GSDMDC1 rabbit polyclonal Ab (Novus, NBP2-33422), V5 rabbit polyclonal Ab (Abcam, Ab9116).

Techniques: Expressing, Positive Control, Construct, Quantitation Assay

Journal: bioRxiv

Article Title: DPP9 directly sequesters the NLRP1 C-terminus to repress inflammasome activation

doi: 10.1101/2020.08.14.246132

Figure Lengend Snippet: a , Modelling of a FIIND polymer using the observed UPA A -UPA B relationship. Adjacent ZU5 molecules would clash, suggesting that UPA polymerization can only occur for free NLRP1-CTs. b , Modelled recruitment of free UPA at both UPA A and UPA B in the ternary complex with DPP9. The additional UPA subdomain next to FIND A clashes with the ZU5 subdomain, and the additional UPA next to UPA B clashes with both DPP9 monomers in the complex, suggesting that DPP9 inhibits UPA oligomerization.

Article Snippet: Primary antibodies used in this study include: DPP9 rabbit polyclonal Ab (Abcam, Ab42080), FLAG® M2 mouse monoclonal Ab (Sigma, F3165), GAPDH rabbit monoclonal Ab (Cell Signaling Technology, 14C10), NLRP1 mouse monoclonal Ab (R&D Systems, MAB6788), CASP1 rabbit polyclonal Ab (Cell Signaling Technology, 2225), GSDMDC1 rabbit polyclonal Ab (Novus, NBP2-33422), V5 rabbit polyclonal Ab (Abcam, Ab9116).

Techniques: Polymer

Journal: bioRxiv

Article Title: DPP9 directly sequesters the NLRP1 C-terminus to repress inflammasome activation

doi: 10.1101/2020.08.14.246132

Figure Lengend Snippet: a , Schematic representation of tertiary complex formation between the autocatalysis-deficient NLRP1-S1213A-FL, Ub-NLRP1-CT, and DPP9. Ub-NLRP1-CT is co- or post-translationally processed by endogenous deubiquitinases, resulting in NLRP1-CT with the native S1213 N-terminus. b , FLAG co-immunoprecipitation using FLAG-tagged WT NLRP1-FL or S1213A-FL and V5-tagged Ub-NLRP1-CT. Neither S1213A-FL (site A) nor NLRP1-CT (site B) alone pulled down endogenous DPP9. In contrast, co-expression of the two constructs formed a ternary complex with DPP9. c , Suppressed NLRP1-CT-induced cell death measured by LDH release in a reconstituted HEK293 inflammasome system when co-expressed with increasing amount of S1213A-FL. All data are representative of > 2 independent experiments. *: p < 0.05 and ***: p < 0.001 by two-sided Student’s t test. d , Schematic of NLRP1 activation and repression by DPP9. NLRP1-FL, together with DPP9, represses some threshold of free NLRP1-CTs. Enhanced degradation of NLRP1-FL, or displacement of the NLRP1-CT, leads to inflammasome signalling.

Article Snippet: Primary antibodies used in this study include: DPP9 rabbit polyclonal Ab (Abcam, Ab42080), FLAG® M2 mouse monoclonal Ab (Sigma, F3165), GAPDH rabbit monoclonal Ab (Cell Signaling Technology, 14C10), NLRP1 mouse monoclonal Ab (R&D Systems, MAB6788), CASP1 rabbit polyclonal Ab (Cell Signaling Technology, 2225), GSDMDC1 rabbit polyclonal Ab (Novus, NBP2-33422), V5 rabbit polyclonal Ab (Abcam, Ab9116).

Techniques: Immunoprecipitation, Expressing, Construct, Activation Assay

Journal: C

Article Title: Pathogen-Imprinted Organosiloxane Polymers as Selective Biosensors for the Detection of Targeted E. coli

doi: 10.3390/c4020029

Figure Lengend Snippet: Capture of targeted inactivated E. coli -GFP bacteria on OSX and polydimethylsiloxane (PDMS) polymers imprinted with the same inactivated bacterium. Selectivity ratios based on capture of non-targeted inactivated S. typhimurium . Total captured is based on number of targeted or non-targeted bacterial cells in 10 view fields. Selectivity was determined with S. typhimurium as the non-targeted bacterium ( n = 2).

Article Snippet: E. coli -GFP (25922GFP) and S. typhimurium -GFP (subspecies enterica serovar Typhimurium GFP, 14028GFP) were purchased from ATCC (Manassas, VA, USA).

Techniques: Bacteria

Journal: C

Article Title: Pathogen-Imprinted Organosiloxane Polymers as Selective Biosensors for the Detection of Targeted E. coli

doi: 10.3390/c4020029

Figure Lengend Snippet: Scanning electron microscopy (SEM) images of ( A ) imprinted OSX-B polymer prepared with heat-fixed E. coli -GFP (OD 600 1.0 suspension) on polystyrene substrate, ( B ) glutaraldehyde-inactivated E. coli -GFP on OSX-C polymer prepared with E. coli -GFP (OD 600 0.44 suspension) on Thermanox, and ( C ) bright-field image of glutaraldehyde-inactivated E. coli -GFP template at 40X magnification.

Article Snippet: E. coli -GFP (25922GFP) and S. typhimurium -GFP (subspecies enterica serovar Typhimurium GFP, 14028GFP) were purchased from ATCC (Manassas, VA, USA).

Techniques: Electron Microscopy, Polymer, Suspension

Journal: C

Article Title: Pathogen-Imprinted Organosiloxane Polymers as Selective Biosensors for the Detection of Targeted E. coli

doi: 10.3390/c4020029

Figure Lengend Snippet: Fluorescent images of captured ( A ) glutaraldehyde-inactivated E. coli -GFP (OD 600 0.38 capture solution) and ( B ) glutaraldehyde-inactivated S. typhimurium -GFP (OD 600 0.38 capture solution) on a glutaraldehyde-inactivated E. coli -GFP-imprinted OSX-C polymer.

Article Snippet: E. coli -GFP (25922GFP) and S. typhimurium -GFP (subspecies enterica serovar Typhimurium GFP, 14028GFP) were purchased from ATCC (Manassas, VA, USA).

Techniques: Polymer

Journal: C

Article Title: Pathogen-Imprinted Organosiloxane Polymers as Selective Biosensors for the Detection of Targeted E. coli

doi: 10.3390/c4020029

Figure Lengend Snippet: Capture of live E. coli -GFP (OD 600 0.38 suspension) on a glutaraldehyde-inactivated E. coli -GFP-imprinted OSX-C polymer (R = 1.32; cells captured 7 ± 2; green bar) and PDMS (cells captured 20 ± 4; purple bar), n = 2.

Article Snippet: E. coli -GFP (25922GFP) and S. typhimurium -GFP (subspecies enterica serovar Typhimurium GFP, 14028GFP) were purchased from ATCC (Manassas, VA, USA).

Techniques: Suspension, Polymer

Journal: C

Article Title: Pathogen-Imprinted Organosiloxane Polymers as Selective Biosensors for the Detection of Targeted E. coli

doi: 10.3390/c4020029

Figure Lengend Snippet: Negative ion mode desorption electrospray (DESI) mass spectra obtained from ( A ) imprinted OSX-C polymer (unused) and ( B ) glutaraldehyde-inactivated E. coli -GFP on Thermanox (template). 1 : palmitic acid, 2 : stearic acid, b: background. Inset: schematic diagram of DESI-MS setup.

Article Snippet: E. coli -GFP (25922GFP) and S. typhimurium -GFP (subspecies enterica serovar Typhimurium GFP, 14028GFP) were purchased from ATCC (Manassas, VA, USA).

Techniques: Polymer

Journal: C

Article Title: Pathogen-Imprinted Organosiloxane Polymers as Selective Biosensors for the Detection of Targeted E. coli

doi: 10.3390/c4020029

Figure Lengend Snippet: Capture of targeted glutaraldehyde-inactivated E. coli -GFP (~6 × 10 5 cells/mL) on imprinted inactivated E. coli -GFP OSX-C polymer (cells captured 49 ± 9; green bar) and PDMS (22 ± 4), n = 1. Imprinting was done with template prepared from a glutaraldehyde-inactivated bacterial suspension (OD 600 2.0).

Article Snippet: E. coli -GFP (25922GFP) and S. typhimurium -GFP (subspecies enterica serovar Typhimurium GFP, 14028GFP) were purchased from ATCC (Manassas, VA, USA).

Techniques: Polymer, Suspension