RECEPTOR AFFINITY PURIFICATION OF A LIPID-BINDING ADHESIN FROM HELICOBACTER-PYLORI

Our previous work has shown that Helicobacter pylori specifically reco gnizes gangliotetraosyleeramide, gangliotriaosylceramide, and phosphat idylethanolamine in vitro. This binding specificity is shared by exoen zyme S from Pseudomonas aeruginosa, and monoclonal antibodies against this adhesin prevent the attachment of H. pylori to its lipid receptor s. We now report the use of a novel, versatile affinity matrix to puri fy a 63-kDa exoenzyme S-like adhesin from H. pylori which is responsib le for the lipid-binding specificity of this organism.