title: Porcine intestinal glycosphingolipids recognized by F6-fimbriated enterotoxigenic Escherichia coli.
abstract: One important virulence factor of enterotoxigenic Escherichia coli is their ability to adhere via fimbrial adhesins to specific receptors located on the intestinal mucosa. Here, the potential glycosphingolipid receptors of enterotoxigenic F6-fimbriated E. coli were examined by binding of purified F6 fimbriae, and F6-expressing bacteria, to glycosphingolipids on thin-layer chromatograms. When intestinal mucosal non-acid glycosphingolipids from single pigs were assayed for F6 binding capacity, a selective interaction with two glycosphingolipids was observed. The binding-active glycosphingolipids were isolated and characterized as lactotriaosylceramide (GlcNAcβ3Galβ4Glcβ1Cer) and lactotetraosylceramide (Galβ3GlcNAcβ3Galβ4Glcβ1Cer). Further binding assays using a panel of reference glycosphingolipids showed a specific interaction between the F6 fimbriae and a number of neolacto core chain (Galβ4GlcNAc) glycosphingolipids. In addition, an occasional binding of the F6 fimbriae to sulfatide, galactosylceramide, lactosylceramide with phytosphingosine and/or hydroxy fatty acids, isoglobotriaosylceramide, gangliotriaosylceramide, and gangliotetraosylceramide was obtained. From the results we conclude that lactotriaosylceramide and lactotetraosylceramide are major porcine intestinal receptors for F6-fimbriated E. coli.
authors.affiliation: Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology, University of Gothenburg, P.O. Box 440, S-405 30 Göteborg, Sweden.
authors.forename: Miralda
authors.initials: M
authors.lastname: Madar Johansson
authors.affiliation: Laboratory of Veterinary Immunology, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, 9820 Merelbeke, Belgium.
authors.forename: Annelies
authors.initials: A
authors.lastname: Coddens
authors.affiliation: Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology, University of Gothenburg, P.O. Box 440, S-405 30 Göteborg, Sweden.
authors.forename: John
authors.initials: J
authors.lastname: Benktander
authors.affiliation: Laboratory of Veterinary Immunology, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, 9820 Merelbeke, Belgium.
authors.forename: Eric
authors.initials: E
authors.lastname: Cox
authors.affiliation: Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology, University of Gothenburg, P.O. Box 440, S-405 30 Göteborg, Sweden. Electronic address: Susann.Teneberg@medkem.gu.se.
authors.forename: Susann
authors.initials: S
authors.lastname: Teneberg
mesh_terms: D018829:Adhesins, Bacterial / Q000378:metabolism; D000818:Animals; D001422:Bacterial Adhesion; D054307:Enterotoxigenic Escherichia coli / Q000502:physiology*; D036781:Fimbriae Proteins / Q000378:metabolism*; D010861:Fimbriae, Bacterial / Q000378:metabolism*; D006028:Glycosphingolipids / Q000302:isolation & purification / Q000378:metabolism*; D007413:Intestinal Mucosa / Q000737:chemistry*; D013058:Mass Spectrometry; D011485:Protein Binding; D013552:Swine
chemical_list: D018829:Adhesins, Bacterial; D006028:Glycosphingolipids; D036781:Fimbriae Proteins
keywords: F6-fimbriated Escherichia coli; Glycosphingolipid characterization; Mass spectrometry; Microbial adhesion; Porcine intestinal glycosphingolipids