PXD042815

PXD042815 is an original dataset announced via ProteomeXchange.

Title	Global acetylomics of Campylobacter jejuni shows lysine acetylation regulates CadF adhesin processing and fibronectin binding during in vivo-like growth
Description	Campylobacter jejuni is the leading cause of acute bacterial gastroenteritis in the developed world. Despite the prevalence of infection, the pathogenesis of C. jejuni remains poorly understood. Lysine acetylation (KAc) is a reversible post-translational modification (PTM) that can alter the protein structure / function paradigm, however specific roles for KAc are largely undefined in bacteria. Acetyl-lysine immunoprecipitation and liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) identified 5567 acetylated lysines on 1026 C. jejuni proteins (~63% of the predicted C. jejuni proteome). Functional enrichment confirmed acetylated proteins are involved in metabolism, transcription and translation, stress responses and chemotaxis. KAc was identified on proteins from all subcellular locations, including outer membrane (OM) and extracellular proteins. Label-based LC-MS/MS identified acetylated proteins and modified sites associated with growth in 0.1% sodium deoxycholate (DOC, a component of gut bile salts). A total of 3571 acetylated peptides were quantified and 761 (from 409 proteins) were differentially abundant following growth in DOC. Changes in KAc involved multiple pathways suggesting a dynamic role for this PTM in bile resistance. As observed in other bacteria, we show that KAc is primarily non-enzymatically mediated via acetyl-phosphate; however, the sole deacetylase CobB also contributes to a global elevation of this modification in DOC. We observed several multiply acetylated OM proteins and altered DOC abundance of acetylated peptides in the major fibronectin (Fn)-binding adhesin CadF. We show that KAc influences CadF Fn binding and prevalence of processed lower mass variants. This study provides the first system-wide analysis of the C. jejuni lysine acetylome and contributes to our understanding of KAc as an emerging PTM in bacteria.
HostingRepository	PRIDE
AnnounceDate	2025-03-11
AnnouncementXML	Submission_2025-03-11_07:51:36.647.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD042815
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Ashleigh Dale
SpeciesList	scientific name: Campylobacter jejuni subsp. jejuni NCTC 11168; NCBI TaxID: NCBITaxon:192222;
ModificationList	acetylated residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2023-06-08 00:03:51	ID requested
⏵ 1	2025-03-11 07:51:38	announced

10.6019/PXD042815;

Dale AL, Man L, Cordwell SJ, Shows Lysine Acetylation Regulates CadF Adhesin Processing and Human Fibronectin Binding. J Proteome Res, 22(11):3519-3533(2023) [pubmed]

10.1021/acs.jproteome.3c00391;

submitter keyword: metabolism, lysine acetylation, post-translational modifications,Bacterial virulence, membrane proteins

Stuart James Cordwell
contact affiliation	School of Life and Environmental Sciences,Charles Perkins Centre, and Sydney Mass Spectrometry, The University of Sydney, Australia
contact email	stuart.cordwell@sydney.edu.au
lab head
Ashleigh Dale
contact affiliation	University of Sydney
contact email	ashleigh.dale@sydney.edu.au
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/03/PXD042815

PRIDE project URI

• PRIDE
  1. PXD042815
     1. Label: PRIDE project
     2. Name: Global acetylomics of Campylobacter jejuni shows lysine acetylation regulates CadF adhesin processing and fibronectin binding during in vivo-like growth