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Binding specificities of wild-type and cloned Escherichia coli strains that recognize globo-A.


ABSTRACT: In this study we compared the specificity for the globoseries of glycolipids of Escherichia coli expressing the O-negative, A-positive (ONAP) adhesin and clones transformed with the pap-like (prs or pap-2) gene cluster. Receptor-active glycolipids were identified by the ability of radiolabeled bacteria to bind to the glycolipids on thin-layer chromatogram plates. The ONAP adhesin and pap-like clones bound with high affinity to the globo-A and Forssman glycolipids. The ONAP strains did not recognize other glycolipids of the globoseries. In contrast, the pap-like clones also showed weak binding to globotriaosylceramide and reacted weakly with Gal alpha 1----4 Gal beta-latex beads. We suggest that the pap-like and ONAP adhesins recognize an epitope shared by the globo-A and Forssman structures, e.g., terminal GalNAc alpha 1----3 bound to Gal alpha 1----4Gal beta-containing glycolipids.

SUBMITTER: Lindstedt R 

PROVIDER: S-EPMC259831 | biostudies-literature | 1989 Nov

REPOSITORIES: biostudies-literature

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Binding specificities of wild-type and cloned Escherichia coli strains that recognize globo-A.

Lindstedt R R   Baker N N   Falk P P   Hull R R   Hull S S   Karr J J   Leffler H H   Svanborg Edén C C   Larson G G  

Infection and immunity 19891101 11


In this study we compared the specificity for the globoseries of glycolipids of Escherichia coli expressing the O-negative, A-positive (ONAP) adhesin and clones transformed with the pap-like (prs or pap-2) gene cluster. Receptor-active glycolipids were identified by the ability of radiolabeled bacteria to bind to the glycolipids on thin-layer chromatogram plates. The ONAP adhesin and pap-like clones bound with high affinity to the globo-A and Forssman glycolipids. The ONAP strains did not recogn  ...[more]

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