Journal article

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

NE Scott, H Nothaft, AVG Edwards, M Labbate, SP Djordjevic, MR Larsen, CM Szymanski, SJ Cordwell

Journal of Biological Chemistry | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2012

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 glyco-engineering recombinant vaccines in Escherichia coli. To determine wh..

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University of Melbourne Researchers

Grants

Awarded by Australian Research Council


Awarded by National Health and Medical Research Council of Australia Overseas (Biomedical)


Funding Acknowledgements

This work was supported by Australian Research Council Discovery Project Grant ARC DP110103573 (to S. J. C.). Supported by an Australian Postgraduate Award and a current National Health and Medical Research Council of Australia Overseas (Biomedical) Fellow (APP1037373).