The Campylobacter jejuni general glycosylation system is important for attachment to human epithelial cells and in the colonization of chicks

Abstract

It has recently been shown that the enteropathogenCampylobacter jejunihas anN-linked generalproteinglycosylation pathway (Pgl) that modifies many of the organism's proteins. To determine the role of theN-linked general glycosylation inC jejuni, the authors studied thepglHgene, which shows high similarity to a family of sugar transferases.pglHmutants were constructed in strains 81116 and 11168H. Both mutants were shown to be deficient in their ability to glycosylate a number ofC. jejuniproteins, but their lipooligosaccharide and capsule were unaffected. ThepglHmutants had significantly reduced ability to adhere to and invade human epithelial Caco-2 cells. Additionally, the 81116pglHmutant was severely affected in its ability to colonize chicks. These results suggest that glycosylation is important for the attachment ofC. jejunito human and chicken host cells and imply a role for glycoproteins in the pathogenesis ofC. jejuni.