Helicobacter pylori is a Gram-negative bacteria that can lead to the development of gastric and duodenal ulcers, gastritis, and gastric cancer in infected individuals. H. pylori is growing increasingly resistant to current antibiotic treatments; therefore a novel approach for treating H. pylori is essential. H. pylori’s ability to sugar-modify, or glycosylate, its proteins is imperative for the function of many proteins involved in H. pylori pathogenesis; therefore, the protein glycosylation pathway is a good candidate for future drug targeting. Our lab has identified several mutant strains of H. pylori deficient in protein glycosylation. Interestingly, some of the identified putative H. pylori protein glycosylation genes are implicated in glycosylating lipids to produce lipopolysaccharide (LPS), a class of molecules that is crucial for H. pylori’s pathogenesis. Here we report our investigation of the potential overlap in protein glycosylation and LPS biosynthesis in H. pylori. In particular, we have analyzed the differences in glycosylation fingerprints of H. pylori mutant versus complemented strains and of LPS-enriched versus LPS depleted samples. Ultimately, this work will reveal genes involved in H. pylori’s protein glycosylation, which has the potential to reveal novel drug targets for H. pylori.

Analysis of Helicobacter pylori strains deficient in protein glycosylation

249th National Meeting (2015)

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