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Infect. Immun., Jul 1996, 2643-2648, Vol 64, No. 7
M Huesca, S Borgia, P Hoffman and CA Lingwood
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 treatment at low pH. We have previously shown
that heat shock proteins (hsps) bind to sulfatide, and the suspicion that
this was a stress-induced response is supported by the fact that a similar
change in H. pylori binding specificity was observed if the organisms were
briefly exposed to heat shock treatment. Following the stress stimulus, the
change in glycolipid binding specificity was prevented by the inclusion of
inhibitors of protein synthesis or by incubation with anti-hsp antibodies.
Expression of hsps in the surface extract and surface reactivity with
anti-hsp antibodies correlated with the change in glycolipid binding
specificity. Despite the presence of high levels of H. pylori cell surface
urease activity which may neutralize the microenvironmental pH, the
acid-induced change in binding specificity was enhanced in the presence of
urea. These studies suggest that cell surface hsps mediate sulfatide
recognition by this organism under stress conditions. A binary receptor
model is proposed for gastric colonization by H. pylori.
Copyright © 1996, American Society for Microbiology
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
Department of Microbiology, Research Institute, The Hospital for Sick Children, Toronto, Ontario, Canada.
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