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

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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.