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Miniature of Hypersensitization of Helicobacter pylori to Antibiotics Through Perturbation of Bacterial Glycan Armor
Hypersensitization of Helicobacter pylori to Antibiotics Through Perturbation of Bacterial Glycan Armor
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      Date: 2022-01-01

      Creator: William J. Rackear

      Access: Access restricted to the Bowdoin Community

        Miniature of Metabolic Glycan Labeling-Based Screen to Identify Bacterial Glycosylation Genes
        Metabolic Glycan Labeling-Based Screen to Identify Bacterial Glycosylation Genes

        Date: 2020-12-11

        Creator: Karen D. Moulton, Adedunmola P. Adewale, Hallie A. Carol, Sage A. Mikami, Danielle H., Dube

        Access: Open access

        Bacterial cell surface glycans are quintessential drug targets due to their critical role in colonization of the host, pathogen survival, and immune evasion. The dense cell envelope glycocalyx contains distinctive monosaccharides that are stitched together into higher order glycans to yield exclusively bacterial structures that are critical for strain fitness and pathogenesis. However, the systematic study and inhibition of bacterial glycosylation enzymes remains challenging. Bacteria produce glycans containing rare sugars refractory to traditional glycan analysis, complicating the study of bacterial glycans and the identification of their biosynthesis machinery. To ease the study of bacterial glycans in the absence of detailed structural information, we used metabolic glycan labeling to detect changes in glycan biosynthesis. Here, we screened wild-type versus mutant strains of the gastric pathogen Helicobacter pylori, ultimately permitting the identification of genes involved in glycoprotein and lipopolysaccharide biosynthesis. Our findings provide the first evidence that H. pylori protein glycosylation proceeds via a lipid carrier-mediated pathway that overlaps with lipopolysaccharide biosynthesis. Protein glycosylation mutants displayed fitness defects consistent with those induced by small molecule glycosylation inhibitors. Broadly, our results suggest a facile approach to screen for bacterial glycosylation genes and gain insight into their biosynthesis and functional importance, even in the absence of glycan structural information.
        Miniature of Characterization of Bacterial Glycosylation Pathways with Fluorescent Monosaccharide Probes
        Characterization of Bacterial Glycosylation Pathways with Fluorescent Monosaccharide Probes
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            Date: 2023-01-01

            Creator: Lucas John DiCerbo

            Access: Access restricted to the Bowdoin Community

              Miniature of Thioglycosides modulate bacterial glycosylation
              Thioglycosides modulate bacterial glycosylation
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                  Date: 2023-01-01

                  Creator: Isabella de la Luz Quintana

                  Access: Access restricted to the Bowdoin Community