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1 London School of Hygiene and Tropical Medicine, University of London, Keppel Street, London EC1A 7HT, UK
2 Department of Veterinary Pathology, Glasgow University, Bearsden, Glasgow G61 1QH, UK
3 Veterinary Laboratories Agency, New Haw, Addlestone, Surrey KT15 3NB, UK
Correspondence
B. W. Wren
brendan.wren{at}lshtm.ac.uk
It has recently been shown that the enteropathogen Campylobacter jejuni has an N-linked general protein glycosylation pathway (Pgl) that modifies many of the organism's proteins. To determine the role of the N-linked general glycosylation in C jejuni, the authors studied the pglH gene, which shows high similarity to a family of sugar transferases. pglH mutants were constructed in strains 81116 and 11168H. Both mutants were shown to be deficient in their ability to glycosylate a number of C. jejuni proteins, but their lipooligosaccharide and capsule were unaffected. The pglH mutants had significantly reduced ability to adhere to and invade human epithelial Caco-2 cells. Additionally, the 81116 pglH mutant was severely affected in its ability to colonize chicks. These results suggest that glycosylation is important for the attachment of C. jejuni to human and chicken host cells and imply a role for glycoproteins in the pathogenesis of C. jejuni.
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