Fab-Independent Antiadhesion Effects of Secretory Immunoglobulin A on S-Fimbriated Escherichia coli Are Mediated by Sialyloligosaccharides

Author:

Schroten Horst1,Stapper Christoph1,Plogmann Ricarda1,Köhler Henrik1,Hacker Jörg2,Hanisch Franz-Georg3

Affiliation:

1. Zentrum für Kinderheilkunde der Heinrich-Heine-Universität, Düsseldorf,1

2. Institut für Molekulare Infektionsbiologie der Universität Würzburg, Würzburg,2 and

3. Institut für Biochemie II der Universität zu Köln, Köln,3 Germany

Abstract

ABSTRACT S-fimbriated Escherichia coli strains cause sepsis and meningitis in newborns and are known to recognize the carbohydrate sequence sialyl-(α2-3)-galactoside. We show that adhesion of cloned S-fimbriated E. coli to human epithelial cells is inhibited Fab independently by sialyloligosaccharides on secretory immunoglobulin A (s-IgA). This indicates an anti-infective function of s-IgA (Fc), particularly in early human milk.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

Reference18 articles.

1. Nonimmune binding of human immunoglobulin A to type II group B streptococci

2. Structure of the carbohydrate units of IgA1 immunoglobulin. I. Composition, glycopeptide isolation, and structure of the asparagine-linked oligosaccharide units;Baenziger J.;J. Biol. Chem.,1974

3. Glycopeptides of heavy chains from human IgA myeloma proteins;Despont J. P. J.;J. Immunol.,1974

4. Goldman A. S. Goldblum R. M. Immunologic system in human milk Textbook of gastroenterology and nutrition in infancy 2nd ed. Lebenthal E. 1989 135 142 Raven Press New York N.Y

5. Specificity of S fimbriae on recombinant Escherichia coli: preferential binding to gangliosides expressing NeuGc alpha (2-3)Gal and NeuAc alpha (2-8)NeuAc

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