Dataset Information

Proteomic analysis of butyric acid inhibition of the growth of E. coli

ABSTRACT: To further characterize the mechanism of action of the organic acids, ultra-performance liquid chromatography-tandem mass spectrometry (LC-MS/MS) was used to analyze E. coli samples co-cultured with butyric acid using iTRAQ quantitative proteomics technology.

ORGANISM(S): Escherichia Coli

SUBMITTER: Haichang Yin

PROVIDER: PXD057728 | iProX | Mon Nov 11 00:00:00 GMT 2024

REPOSITORIES: iProX

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Publications

Butyric acid from ligilactobacillus animalis 2020MB acts on membrane BamA to control avian pathogenic escherichia coli.

Yin Haichang H Du Zunhe Z Jiang Xinjie X Zhou Yao Y Jin Zhenhua Z Cong Feng F

Poultry science 20250401 6

Avian pathogenic Escherichia coli can cause high morbidity, mortality, and serious economic losses to the global poultry industry. Lactic acid bacteria inhibit the growth of many pathogens, including E. coli, but the underlying mechanism remains unclear. In this study, we investigated the effect of the cell-free supernatant of Ligilactobacillus animalis 2020MB isolated from the intestinal tract of chickens on specific pathogen-free chickens infected with E. coli. The cell-free supernatant-induce ...[more]

PMID: 40187014

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Project description:This dataset contains E. coli W3110 samples grown in different growth conditions and harvested at different growth stages. A mapping between conditions and files is contained in the SDRF. This dataset is one of 40 projects included in the E. coli PanProteome PeptideAtlas build:Escherichia coli is a widely used model organism in molecular biology. Despite its pivotal role, a comprehensive proteome resource covering the E. coli pan-proteome and its post-translational modifications (PTMs) has been lacking. Here we present the E. coli PeptideAtlas build, the first comprehensive pan-proteome analysis of E. coli, generated from 40 high-quality public and in-house datasets spanning a broad diversity of strains, sample types, and experimental conditions, and comprising over 73 million MS/MS spectra. All datasets were reprocessed using both a closed search (Trans-Proteomic Pipeline using MSFragger) and an open search (ionbot). The E. coli PeptideAtlas build provides evidence for 4,755 proteins, including 1,410 previously lacking protein-level support in UniProt. The resource offers protein coverage, modification sites, raw spectra with matched peptides, and manually annotated metadata for the E. coli pan proteome. PTM profiling identified over 10,000 modification sites, including phosphorylation (3,806), acetylation (754), methylation (730), glutathionylation (352) and phosphoribosylation (226). Analysis of the glutathionylation sites revealed potential links to metal binding regulation. We also detected proteins likely associated with phages, underscoring the value of pan-proteomic approaches for studying host-phage interactions. All identifications are publicly accessible and traceable through the PeptideAtlas interface. We expect that the E. coli PeptideAtlas build will provide a useful resource for the community, which supports, for example, targeted MS experiment design, PTM enrichment method development, and strain typing. It allows straightforward lookups of protein and peptide identifications and facilitates comparative proteomic analyses by enabling the assessment of protein presence and variability across different E. coli strains. The build is available at https://db.systemsbiology.net/sbeams/cgi/PeptideAtlas/buildDetails?atlas_build_id=585.

Dataset Information

Proteomic analysis of butyric acid inhibition of the growth of E. coli

Publications

Butyric acid from ligilactobacillus animalis 2020MB acts on membrane BamA to control avian pathogenic escherichia coli.

Similar Datasets

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