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Sulfatide recognition by colonization factor antigen CS6 from enterotoxigenic Escherichia coli.

Journal article
Authors Lena Jansson
Joshua Tobias
Catharina Jarefjäll
Michael Lebens
Ann-Mari Svennerholm
Susann Teneberg
Published in PloS one
Volume 4
Issue 2
Pages e4487
ISSN 1932-6203
Publication year 2009
Published at Institute of Biomedicine, Department of Microbiology and Immunology
Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages e4487
Language en
Links dx.doi.org/10.1371/journal.pone.000...
Keywords Antigens, Bacterial, metabolism, Bacterial Adhesion, Enterotoxigenic Escherichia coli, pathogenicity, Escherichia coli Proteins, metabolism, Fimbriae Proteins, metabolism, Glycosphingolipids, metabolism, Humans, Intestine, Small, chemistry, microbiology, Mice, Protein Binding, Protein Subunits, metabolism, Rabbits, Sulfoglycosphingolipids, analysis, metabolism, Virulence
Subject categories Microbiology in the medical area, Chemistry

Abstract

The first step in the pathogenesis of enterotoxigenic Escherichia coli (ETEC) infections is adhesion of the bacterium to the small intestinal epithelium. Adhesion of ETEC is mediated by a number of antigenically distinct colonization factors, and among these, one of the most commonly detected is the non-fimbrial adhesin coli surface antigen 6 (CS6). The potential carbohydrate recognition by CS6 was investigated by binding of recombinant CS6-expressing E. coli and purified CS6 protein to a large number of variant glycosphingolipids separated on thin-layer chromatograms. Thereby, a highly specific binding of the CS6-expressing E. coli, and the purified CS6 protein, to sulfatide (SO(3)-3Galbeta1Cer) was obtained. The binding of the CS6 protein and CS6-expressing bacteria to sulfatide was inhibited by dextran sulfate, but not by dextran, heparin, galactose 4-sulfate or galactose 6-sulfate. When using recombinantly expressed and purified CssA and CssB subunits of the CS6 complex, sulfatide binding was obtained with the CssB subunit, demonstrating that the glycosphingolipid binding capacity of CS6 resides within this subunit. CS6-binding sulfatide was present in the small intestine of species susceptible to CS6-mediated infection, e.g. humans and rabbits, but lacking in species not affected by CS6 ETEC, e.g. mice. The ability of CS6-expressing ETEC to adhere to sulfatide in target small intestinal epithelium may thus contribute to virulence.

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