Journal article
Acidic pH changes receptor binding specificity of Helicobacter pylori: a binary adhesion model in which surface heat shock (stress) proteins mediate sulfatide recognition in gastric colonization
Abstract
The gastric pathogen helicobacter pylori is one of a number of bacteria which bind specifically to gangliotetraosylceramide, gangliotriaosylceramide, and phosphatidylethanolamine in vitro at neutral pH. Since this organism encounters an acid pH during initial infection of the stomach, we have monitored the effect of pH on receptor binding specificity and found induction of specific binding to sulfoglycolipids (sulfatide) following brief …
Authors
Huesca M; Borgia S; Hoffman P; Lingwood CA
Journal
Infection and Immunity, Vol. 64, No. 7, pp. 2643–2648
Publisher
American Society for Microbiology
Publication Date
July 1996
DOI
10.1128/iai.64.7.2643-2648.1996
ISSN
0019-9567
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Adhesins, BacterialAntibodies, BlockingBacterial AdhesionBacterial ProteinsBinding SitesGastritisGlycolipidsHeat-Shock ProteinsHelicobacter InfectionsHelicobacter pyloriHumansHydrogen-Ion ConcentrationIn Vitro TechniquesMembrane ProteinsModels, BiologicalPeptic UlcerProtein Synthesis InhibitorsStomachSulfoglycosphingolipidsUrea