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Escherichia coli str. K-12 substr. W3110

ABSTRACT: Next-Generation Antimicrobial Discovery through Bacterial Self-Screening of Surface-Displayed Peptide Libraries [HiSeq]

PROVIDER: PRJNA371428 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR5230340.fastq.gz	Fastqsanger.gz
	SRR5230350.fastq.gz	Fastqsanger.gz
	SRR5230360.fastq.gz	Fastqsanger.gz
	SRR5230341.fastq.gz	Fastqsanger.gz
	SRR5230351.fastq.gz	Fastqsanger.gz

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Escherichia coli str. K-12 substr. W3110

Project description:Next-Generation Antimicrobial Discovery through Bacterial Self-Screening of Surface-Displayed Peptide Libraries [MiSeq]

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Next-Generation Antimicrobial Discovery through Bacterial Self-Screening of Surface-Displayed Peptide Libraries

Project description:Next-Generation Antimicrobial Discovery through Bacterial Self-Screening of Surface-Displayed Peptide Libraries

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Project description:We show here that the antimicrobial peptide RNase 7 enables human pDCs to recognize self-DNA, and promotes their rapid sensing of bacterial DNA.

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The Trypanosoma cruzi Antigen and Epitope Atlas: discovery of antibody specificities in human Chagas Disease patients across human populations

Project description:These assays represent an antigen discovery screening, and epitope mapping characterization. In this screening two complete proteomes from Trypanosoma cruzi, from two different strains (CL-Brener, Sylvio X10), were displayed in the form of short peptides (tiling array, overlapped) and assayed with pooled serum samples (antibodies) from Chagas Disease patients and matched negative (healthy) subjects selected from 6 geographic regions across the Americas. Peptide arrays (slides) were incubated with pooled serum samples (primary antibodies), washed, and then incubated with a fluorescently-labeled anti-human IgG commercial antibody (secondary antibodies). Raw readouts of fluoresence (signal), as well as normalized signal values are provided in this submission for all samples analyzed. All samples were analyzed in duplicate.

2022-08-20 | E-MTAB-11651 | biostudies-arrayexpress

Next-Generation Antimicrobial Discovery through Bacterial Self-Screening of Surface-Displayed Peptide Libraries [MiSeq]

Project description:Peptides have great potential to combat antibiotic resistance. While many platforms can screen peptides for their ability to bind to target cells, there are virtually no platforms that directly assess the functionality of peptides. This limitation is exacerbated when identifying antimicrobial peptides, since the phenotype, death, selects against itself, and has caused a scientific bottleneck confining research to only a few naturally occurring classes of antimicrobial peptides. We have used this seeming dissonance to develop Surface Localized Antimicrobial displaY (SLAY); a platform that allows screening of unlimited numbers of peptides of any length, composition, and structure in a single tube for antimicrobial activity. Using SLAY, we screened ~800,000 random peptide sequences for antimicrobial function and identified thousands of active sequences doubling the number of known antimicrobial sequences. SLAY hits present with different potential mechanisms of peptide action and access to areas of antimicrobial physicochemical space beyond what nature has evolved.

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Next-Generation Antimicrobial Discovery through Bacterial Self-Screening of Surface-Displayed Peptide Libraries [HiSeq]

2018-01-03 | GSE94529 | GEO

Exploring bioactive peptides from bacterial secretomes using PepSAVI-MS: identification and characterization of Bac-21 from Enterococcus faecalis pPD1

Project description:Background. As current methods for antibiotic drug discovery are being outpaced by the rise of antimicrobial resistance, new methods and innovative technologies are necessary to replenish our dwindling arsenal of antimicrobial agents. To this end, we developed the PepSAVI-MS pipeline to expedite the search for natural product bioactive peptides. Results. Herein we demonstrate expansion of PepSAVI-MS for the discovery of bacterial-sourced bioactive peptides through identification of the bacteriocin Bac-21 from Enterococcus faecalis pPD1. Minor pipeline modifications including implementation of bacteria-infused agar diffusion assays and optional digestion of peptide libraries highlight the versatility and wide adaptability of the PepSAVI-MS pipeline. Additionally, we have experimentally validated the primary protein sequence of the active, mature Bac-21 peptide for the first time and have confirmed identity with respect to primary sequence and post-translational processing. Conclusions: Successful application of PepSAVI-MS to bacterial secretomes as demonstrated herein establishes proof-of-principle for use in novel microbial bioactive peptide discovery.

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Project description:antimicrobial peptide

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LL10000 hybridization

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2011-11-08 | E-MEXP-3104 | biostudies-arrayexpress

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