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Fucosylation and protein glycosylation create functional receptors for cholera toxin.

Journal article
Authors Amberlyn M Wands
Akiko Fujita
Janet E McCombs
Jakob Cervin
Benjamin Dedic
Andrea C Rodriguez
Nicole Nischan
Michelle R Bond
Marcel Mettlen
David C Trudgian
Andrew Lemoff
Marianne Quiding-Järbrink
Bengt Gustavsson
Catharina Steentoft
Henrik Clausen
Hamid Mirzaei
Susann Teneberg
Ulf Yrlid
Jennifer J Kohler
Published in eLife
Volume 4
Pages e09545
ISSN 2050-084X
Publication year 2015
Published at Institute of Clinical Sciences, Department of Surgery
Institute of Biomedicine
Institute of Biomedicine, Department of Microbiology and Immunology
Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages e09545
Language en
Subject categories Microbiology


Cholera toxin (CT) enters and intoxicates host cells after binding cell surface receptors using its B subunit (CTB). The ganglioside (glycolipid) GM1 is thought to be the sole CT receptor; however, the mechanism by which CTB binding to GM1 mediates internalization of CT remains enigmatic. Here we report that CTB binds cell surface glycoproteins. Relative contributions of gangliosides and glycoproteins to CTB binding depend on cell type, and CTB binds primarily to glycoproteins in colonic epithelial cell lines. Using a metabolically incorporated photocrosslinking sugar, we identified one CTB-binding glycoprotein and demonstrated that the glycan portion of the molecule, not the protein, provides the CTB interaction motif. We further show that fucosylated structures promote CTB entry into a colonic epithelial cell line and subsequent host cell intoxication. CTB-binding fucosylated glycoproteins are present in normal human intestinal epithelia and could play a role in cholera.

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