Master of Science
Microbiology and Immunology
Helicobacter pylori colonizes 50% of the world’s population, whereby glycoproteins and Lewis Y-containing lipopolysaccharides contribute to its pathogenesis. We investigated whether the HopE porin is glycosylated, if the glycan is Lewis Y, and if this is mediated by the putative oligosaccharide transferase HP0946 or the O-antigen ligase WaaL. Western blotting was performed on outer membranes with anti-HopE antibodies, anti-Lewis Y antibodies and fucose-binding BambL lectin to ascertain HopE glycosylation. We discovered that HopE is likely glycosylated by a non-Lewis Y fucose-containing glycan and neither HP0946 nor WaaL are the transferase. Additionally, we investigated HopE’s role in antibiotic susceptibility via Etest strips and disk diffusion method. By comparing sets of mutants for HopE, HP0946, and WaaL, we found that HopE does not affect antibiotic sensitivity, while eliminating HP0946 increases antibiotic sensitivity. Overall, this study presents HopE as a novel fucosylated glycoprotein and introduces a possible role for HP0946 in antibiotic resistance.
Yogendirarajah, Keertika, "Elucidating the Importance of HopE and its Potential Lewis Glycosylation in Helicobacter pylori" (2018). Electronic Thesis and Dissertation Repository. 5589.
Available for download on Monday, August 31, 2020