Proteomics

Dataset Information

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Proteomics of Campylobacter glycosylation


ABSTRACT: N-linked glycosylation is an essential virulence determinant in Campylobacter jejuni, the major causative agent of gastroenteritis in the developed world. Glycosylation is encoded by the pgl gene cluster which encodes for the biosynthesis and attachment of a conserved heptasaccharide glycan to proteins in the C. jejuni periplasm. Over 80 membrane-associated proteins have been identified, however the functional role played by glycan attachment is almost completely unknown. We used quantitative proteomics by label-based and targeted strategies to examine glycosylation negative C. jejuni in comparison to wild-type. These technical approaches were considered as ‘discovery’ (label-based) and ‘validation’ data sets in our subsequent analysis. Inclusion of a glycosylation restored strain enabled us to further exploit the proteomics data to exclude non-specific protein abundance changes that could be considered as off-target effects. These data have provided a reference set of changes associated with protein N-glycosylation that could subsequently be tested by phenotypic analysis to determine the role of this modification in Campylobacter biology.

INSTRUMENT(S): TripleTOF 6600, Q Exactive

ORGANISM(S): Campylobacter Jejuni Subsp. Jejuni Nctc 11168 = Atcc 700819

SUBMITTER: Stuart Cordwell  

LAB HEAD: Stuart Cordwell

PROVIDER: PXD011646 | Pride | 2019-01-11

REPOSITORIES: Pride

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Publications

Proteomics Reveals Multiple Phenotypes Associated with <i>N</i>-linked Glycosylation in <i>Campylobacter jejuni</i>.

Cain Joel A JA   Dale Ashleigh L AL   Niewold Paula P   Klare William P WP   Man Lok L   White Melanie Y MY   Scott Nichollas E NE   Cordwell Stuart J SJ  

Molecular & cellular proteomics : MCP 20190107 4


<i>Campylobacter jejuni</i> is a major gastrointestinal pathogen generally acquired <i>via</i> consumption of poorly prepared poultry. <i>N</i>-linked protein glycosylation encoded by the <i>pgl</i> gene cluster targets >80 membrane proteins and is required for both nonsymptomatic chicken colonization and full human virulence. Despite this, the biological functions of <i>N</i>-glycosylation remain unknown. We examined the effects of <i>pgl</i> gene deletion on the <i>C. jejuni</i> proteome using  ...[more]

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