PXD011452

PXD011452 is an original dataset announced via ProteomeXchange.

Title	Quantitative analyses reveal novel roles for N-glycosylation in a major enteric bacterial pathogen
Description	In eukaryotes glycosylation plays a role in proteome stability, protein quality control and modulating protein function, however, similar studies in bacteria are lacking. Here, we investigate the role of general protein glycosylation systems in bacteria using the enteropathogen Campylobacter jejuni as a well-defined example. By using a quantitative proteomics strategy, we were able to monitor changes in the C. jejuni proteome when glycosylation is disrupted. We demonstrate that in C. jejuni, N-glycosylation is essential to maintain proteome stability and protein quality control. These findings guided us to investigate the role of N-glycosylation in modulating bacterial cellular activities. In glycosylation deficient C. jejuni, the multidrug efflux pump and electron transport pathways were significantly impaired. In vivo, we demonstrate that fully glycosylation deficient C. jejuni were unable to colonise its natural avian host. These results provide the first evidence of a link between proteome stability and complex functions via a bacterial general glycosylation system.
HostingRepository	PRIDE
AnnounceDate	2021-09-08
AnnouncementXML	Submission_2021-09-08_07:42:48.183.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Sherif Abouelhadid
SpeciesList	scientific name: Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819; NCBI TaxID: 192222;
ModificationList	No PTMs are included in the dataset
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2018-10-23 01:49:39	ID requested
⏵ 1	2021-09-08 07:42:49	announced

Abouelhadid S, North SJ, Hitchen P, Vohra P, Chintoan-Uta C, Stevens M, Dell A, Cuccui J, Wren BW, Glycosylation in a Major Enteric Bacterial Pathogen. mBio, 10(2):(2019) [pubmed]

curator keyword: Biological

submitter keyword: Campylobacter, TMT, quantitative proteomics, Glycosylation

Sherif Abouelhadid
contact affiliation	Wren Lab London School of Hygiene & Tropical Medicine
contact email	Sherif.abouelhadid@lshtm.ac.uk
lab head
Sherif Abouelhadid
contact affiliation	London School of Hygiene & Tropical Medicine
contact email	sherif.abouelhadid@lshtm.ac.uk
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD011452
     1. Label: PRIDE project
     2. Name: Quantitative analyses reveal novel roles for N-glycosylation in a major enteric bacterial pathogen