Moreover, we observed highly significant diversity in αCgT amino acid sequences depending on clinical isolates and found that αCgT activity was highly correlated with progression of gastric mucosal atrophy. αCgT amino acid substitutions were not seen at the UDP-Glc binding site, which is located at an inner hydrophobic pocket of αCgT.
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Helicobacter pylori cholesteryl α-glucosides contribute to its pathogenicity and immune response by natural killer T cells.
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