Indications That the Erythrocyte Receptor Involved in Enterotoxigenic Escherichia Coli Attachment is a Sialoglycoconjugate

Overview

Journal J Clin Microbiol

Specialty Microbiology

Date 1985 Jun 1

PMID 2861212

Citations 10

Authors

H Bartus

P Actor

E Snipes

D Sedlock

I Zajac

Affiliations

Soon will be listed here.

Abstract

A reverse hemagglutination assay was used to study adherence to human erythrocytes by Escherichia coli H10407, which possesses colonization factor antigen I. Pretreatment of erythrocytes with trypsin, chymotrypsin, papain, protease, and neuraminidase completely abolished attachment reactivity. In addition, the hemagglutination reaction was prevented by the presence of urea and guanidine. In contrast, the lipases, nucleotide hydrolases, exoglycosidases, and reagents affecting disulfide or sulfhydryl moieties did not alter receptor reactivity. Glycoconjugates containing sialic acid inhibited the hemagglutination reaction. Furthermore, a sialoglycoprotein isolated from the erythrocyte membrane inhibited the hemagglutination reaction. Collectively, these data indicate that the erythrocyte receptor responsible for attachment by E. coli possessing colonization factor antigen I is a sialoglycoconjugate.

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