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. 1993 Jun;61(6):2474–2478. doi: 10.1128/iai.61.6.2474-2478.1993

Receptor affinity purification of a lipid-binding adhesin from Helicobacter pylori.

C A Lingwood 1, G Wasfy 1, H Han 1, M Huesca 1
PMCID: PMC280871  PMID: 8500882

Abstract

Our previous work has shown that Helicobacter pylori specifically recognizes gangliotetraosylceramide, gangliotriaosylceramide, and phosphatidylethanolamine in vitro. This binding specificity is shared by exoenzyme S from Pseudomonas aeruginosa, and monoclonal antibodies against this adhesin prevent the attachment of H. pylori to its lipid receptors. We now report the use of a novel, versatile affinity matrix to purify a 63-kDa exoenzyme S-like adhesin from H. pylori which is responsible for the lipid-binding specificity of this organism.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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