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Colonization factor CS30 from enterotoxigenic Escherichia coli binds to sulfatide in human and porcine small intestine

Journal article
Authors Astrid von Mentzer
Dani Zalem
Zofia Chrienova
Susann Teneberg
Published in Virulence
Volume 11
Issue 1
Pages 381-390
ISSN 2150-5594
Publication year 2020
Published at Institute of Biomedicine, Department of Microbiology and Immunology
Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 381-390
Language en
Keywords Enterotoxigenic E, coli, colonization factor CS30, microbial adhesion, carbohydrate binding, glycosphingolipid characterization, sulfatide, factor-antigen-i, glycolipid receptors, helicobacter-pylori, antibody-responses, mass-spectrometry, adhesion, etec, diarrhea, cfa/i, Immunology, Infectious Diseases, Microbiology
Subject categories Microbiology in the medical area, Infectious Medicine


The ability to adhere via colonization factors to specific receptors located on the intestinal mucosa is a key virulence factor in enterotoxigenic Escherichia coli (ETEC) pathogenesis. Here, the potential glycosphingolipid receptors of the novel human ETEC colonization factor CS30 were examined by binding of CS30-expressing bacteria to glycosphingolipids on thin-layer chromatograms. We thereby found a highly specific binding of CS30-expressing bacteria to a fast-migrating acid glycosphingolipid of human and porcine small intestine, while no binding was obtained with a mutant ETEC strain unable to express CS30 fimbriae. The CS30 binding glycosphingolipid from human small intestine was isolated and characterized by mass spectrometry as sulfatide (SO3-3Gal beta 1Cer). Comparative binding studies using sulfatides with different ceramide compositions gave a preferential binding of CS30 to sulfatide with d18:1-h24:0 ceramide. This ceramide species of sulfatide was also isolated from human small intestine and characterized by mass spectrometry and antibody binding. These studies implicate sulfatide as candidate receptor for mediating attachment of CS30-fimbriated ETEC to human and porcine small intestinal cells. Our findings may be a basis for designing receptor saccharide analogues for inhibition of the intestinal adhesion of CS30-expressing E. coli.

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