MassIVE MSV000099871

Partial Public PXD070658

Commensal derived short chain fatty acids disrupt Staphylococcus aureus lipid membrane homeostasis

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Description

Quantitative, tandem mass tag (TMT) based proteomics for Staphylococcus aureus JE2 grown in LB alone or LB supplemented with the commensal short-chain fatty acids propionate or butyrate. Mid-log cells (OD600 0.3) were lysed (urea/thiourea/TEAB buffer), reduced/alkylated, barocycled, digested, TMT-labeled, and analyzed on an Orbitrap Eclipse using HCD. Raw files and search results (Proteome Discoverer; UniProt S. aureus pan-proteome UP000008816 plus common contaminants) are included. The dataset supports the mBio study Commensal-derived short-chain fatty acids disrupt membrane lipid homeostasis in Staphylococcus aureus (Fletcher et al.) and enables assessment of global protein abundance changes elicited by SCFAs that converge on lipid/branched-chain fatty acid metabolism, cell envelope homeostasis, and virulence regulation. Differential proteins highlighted in the manuscript include induction of acetolactate synthase components (BudA/AlsS) and NanA in propionate, increased dihydropicolinate synthases (DapA/B/H) in butyrate, and decreased RecR and NrdI in both conditions. These data provide a resource to explore SCFA-driven remodeling of the S. aureus proteome linked to membrane physiology and antimicrobial sensitivity. [doi:10.25345/C54T6FG8T] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Staphylococcus aureus ; Propionate ; butyrate ; short chain fatty acids ; DatasetType:Proteomics

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Principal Investigators:
(in alphabetical order) 		Ryan Hunter, University at Buffalo, USA
Submitting User: rhunter2
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