Premium
Salmonella enterica serotype Typhimurium Std fimbriae bind terminal α(1,2)fucose residues in the cecal mucosa
Author(s) -
Chessa Daniela,
Winter Maria G.,
Jakomin Marcello,
Bäumler Andreas J.
Publication year - 2009
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2008.06566.x
Subject(s) - fimbria , biology , salmonella enterica , microbiology and biotechnology , bacterial adhesin , fucosylation , fucose , neuraminidase , virulence factor , serotype , intestinal mucosa , enterobacteriaceae , salmonella , lectin , virulence , virology , escherichia coli , glycoprotein , bacteria , biochemistry , virus , medicine , genetics , gene
Summary The std operon encodes a fimbrial adhesin of Salmonella enterica serotype Typhimurium that is required for attachment to intestinal epithelial cells and for cecal colonization in the mouse. To study the mechanism by which this virulence factor contributes to colonization we characterized its binding specificity. Std‐mediated binding to human colonic epithelial (Caco‐2) cells could be abrogated by removing N‐linked glycans. Adherence of Std fimbriated S. Typhimurium to Caco‐2 cells could be blocked by co‐incubation with H type 2 oligosaccharide (Fucα1‐2Galβ1‐4GlcNAc) or by pretreatment of cells with α1‐2 fucosidase. In contrast, pretreatment of Caco‐2 cells with neuraminidase or co‐incubation with the type 2 disaccharide precursor (Galβ1‐4GlcNAc) did not reduce adherence of Std fimbriated S. Typhimurium. Binding of purified Std fimbriae to Fucα1‐2Galβ1‐4GlcNAc in a solid phase binding assay was competitively inhibited by Ulex europaeus agglutinin‐I (UEA‐I), a lectin specific for Fucα1‐2 moieties. Purified Std fimbriae and UEA both bound to a receptor localized in the mucus layer of the murine cecum. These data suggest that the std operon encodes an adhesin that binds an α1‐2 fucosylated receptor(s) present in the cecal mucosa.