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saba/carbohydrate

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3 results

Helicobacter pylori SabA adhesin evokes a strong inflammatory response in human neutrophils which is down-regulated by the neutrophil-activating protein.

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The human pathogen Helicobacter pylori expresses two dominant adhesins; the Lewis b blood group antigen binding adhesin, BabA, and the sialic acid-binding adhesin, SabA. These adhesins recognize specific carbohydrate moieties of the gastric epithelium, i.e. the Lewis b antigen, Le(b), and the

Peptides from Pisum sativum L. enzymatic protein digest with anti-adhesive activity against Helicobacter pylori: structure-activity and inhibitory activity against BabA, SabA, HpaA and a fibronectin-binding adhesin.

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METHODS Identification of anti-adhesive peptides against Helicobacter pylori obtained by enzymatic hydrolysis of seed proteins from Pisum sativum L. (Fabaceae). RESULTS Bioassay-guided fractionation of protein tryptic digest by ultrafiltration, size exclusion chromatography (SEC) and reversed phase

Helicobacter pylori induces beta3GnT5 in human gastric cell lines, modulating expression of the SabA ligand sialyl-Lewis x.

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Chronic Helicobacter pylori infection is recognized as a cause of gastric cancer. H. pylori adhesion to gastric cells is mediated by bacterial adhesins such as sialic acid-binding adhesin (SabA), which binds the carbohydrate structure sialyl-Lewis x. Sialyl-Lewis x expression in the gastric
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