Modification of the Campylobacter jejuni N-linked glycan by EptC protein-mediated addition of phosphoethanolamine.

ABSTRACT: Campylobacter jejuni is the major worldwide cause of bacterial gastroenteritis. C. jejuni possesses an extensive repertoire of carbohydrate structures that decorate both protein and non-protein surface-exposed structures. An N-linked glycosylation system encoded by the pgl gene cluster mediates the synthesis of a rigidly conserved heptasaccharide that is attached to protein substrates or released as free oligosaccharide in the periplasm. Removal of N-glycosylation results in reduced virulence and impeded host cell attachment. Since the N-glycan is conserved, the N-glycosylation system is also an attractive option for glycoengineering recombinant vaccines in Escherichia coli. To determine whether non-canonical N-glycans are present in C. jejuni, we utilized high throughput glycoproteomics t

SUBMITTER: Scott NE 

PROVIDER: S-EPMC3436159 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature