Date of Award
Master of Science
Microbiology and Immunology
Dr. Carole Creuzenet
Protein glycosylation in Helicobacter pylori is known to modify the flagellins with pseudaminic acid (pse). This modification is required for proper flagellum production and H pylori motility, which implicates protein glycosylation in H. pylori’s pathogenesis. We investigated whether protein glycosylation extends beyond pse-specific flagellin glycosylation by the use of H pylori pse biosynthesis mutants and the detection of glycoproteins by glycoprotein-specific chemical labelling. Using these methods, we demonstrated the presence of novel protein glycosylation in H pylori, in terms of both the identification of membrane glycoproteins and at least two alternative glycosylation pathways. In addition, a link between protein glycosylation and lipopolysaccharide (LPS) biosynthesis was elucidated, in which the O-antigen ligase, WaaL, is a candidate glycoprotein and was shown to exhibit general oligosaccharyltransferase activity. Overall, this study highlights that protein glycosylation affects several proteins in H pylori and has a key role in the production of multiple virulence factors.
Ford, Rachel Stephanie, "The characterization ofnovel protein glycosylation in Helicobacter pylori" (2011). Digitized Theses. 3530.