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

• DOI: 10.1099/mic.0.26721-0
• Publication Date: 2004-06-07T21:16:31Z
• Authors: A. V. Karlyshev; P. Everest; D. Linton; S. Cawthraw; D. G. Newell; B. W. Wren
• Keywords: 0303 health sciences; Glycosylation; Colony Count, Microbial; Epithelial Cells; Bacterial Adhesion; Campylobacter jejuni; 03 medical and health sciences; Bacterial Proteins; Campylobacter Infections; Animals; Humans; Caco-2 Cells; Cecum; Chickens; Poultry Diseases

It has recently been shown that the enteropathogen Campylobacter jejuni an N -linked general p rotein gl ycosylation pathway (Pgl) modifies many of organism's proteins. To determine role glycosylation in C , authors studied pglH gene, which shows high similarity to a family sugar transferases. mutants were constructed strains 81116 and 11168H. Both be deficient their ability glycosylate number C. proteins, but lipooligosaccharide capsule unaffected. The had significantly reduced adhere invade human epithelial Caco-2 cells. Additionally, mutant was severely affected its colonize chicks. These results suggest is important for attachment chicken host cells imply glycoproteins pathogenesis .