Receptor Structure for F1C Fimbriae of Uropathogenic Escherichia coli

• DOI: 10.1128/iai.68.6.3541-3547.2000
• Publication Date: 2002-07-27T09:58:18Z
• Authors: A. Salam Khan; Bernhard Kniep; Tobias A. Oelschl...; Irma Van Die; Timo Korhonen; Jörg Hacker
• Keywords: Lactosylceramide; Globotriaosylceramide

ABSTRACT F1C fimbriae are correlated with uropathogenic Escherichia coli strains. Although mediate binding to kidney tubular cells, their receptor is not known. In this paper, we demonstrate for the first time specific carbohydrate residues as structure F1C-fimbria-expressing E. . The of fimbriated recombinant strain HB101(pPIL110-54) and purified reference glycolipids different compositions was evaluated by using thin-layer chromatography (TLC) overlay solid-phase assays. TLC fimbrial analysis revealed ability only glucosylceramide (GlcCer), β1-linked galactosylceramide 2 (GalCer2) nonhydroxy fatty acids, lactosylceramide, globotriaosylceramide, paragloboside (nLc 4 Cer), lactotriaosylceramide, gangliotriaosylceramide (asialo-GM [GgO 3 Cer]) gangliotetraosylceramide 1 Cer]). well optimal microtiter plates coated asialo-GM (GgO Cer). bacterial interaction Cer) strongly inhibited disaccharide GalNAcβ1-4Galβ linked bovine serum albumin. We observed no globotetraosylceramide or Forssman antigen (Gb 5 glycosphingolipids sialic-acid-containing gangliosides. It demonstrated that presence a GalCer GlcCer residue alone sufficient binding, additional required high-affinity adherence. Indeed, efficiency bacteria increased 19-fold when sequence in Thus, it suggested which positioned internally epitope