Helicobacter pylori (Hp) is a Gram-negative, pathogenic bacteria that colonizes the gastric tract of over 50% of humans and can cause ulcers and gastric cancer. As antibiotic resistant strains become more common, new methods of treatment are needed. One characteristic of Hp that could be used as a potential target for therapeutics is the link between its ability to glycosylate proteins and its pathogenesis. Glycosylation is crucial for proper flagella formation, motility, and colonization, so without glycosylation, Hp is unable to cause infection. More knowledge about these glycosylated proteins, such as the sugar structures, could lead to the development of novel therapeutics. Metabolic oligosaccharide engineering, a process that replaces natural sugars with slightly modified monosaccharaides, facilitates labeling and detection of Hp's glycosylated proteins. For this project, these modified monosaccharaides have an azide chemical tag that can be targeted to react with phosphine TAGs, which aid in purification and identification. Previous results using liquid chromatography mass spectrometry (LC-MS), a method of analysis that provides structural information about compounds, have produced spectra that complicate sugar analysis because intense TAG peaks overpower small sugar peaks. This result may occur because product ions formed by LC-MS need to be charged to be detected, but no basic sites are present on the sugar while several basic sites are present in the TAG. My work includes synthesizing and analyzing different TAGs to see if decreasing the number of basic sites on the TAG increases the intensity of the sugar peaks.

Structural identification of <i>Helicobacter pylori</i>'s glycoproteins

247th National Meeting (2014)

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Structural identification of Helicobacter pylori's glycoproteins