Interaction of a rat intestinal brush border membrane glycoprotein with type-1 fimbriae of Salmonella typhimurium

Mol Cell Biochem. 1996 May 24;158(2):125-31. doi: 10.1007/BF00225838.

Abstract

Type-1 fimbriated Salmonella typhimurium was found to adhere to rat intestinal brush border membrane in a mannose sensitive manner. The maximum binding of the purified fimbriae observed with the rat illeal enterocytes was inhibited by 69.2% in presence of D-mannose. Brush border membrane from rat illeum was isolated, delipidified, solubilised and fractionated by affinity chromatography on type-1 fimbriae coupled Sepharose CL 4B column. Sodium dodecyl sulphate polyacrylamide gel electrophoresis of the material eluted from the column with D-mannose revealed a single band of molecular weight 60 kDa. The direct binding of this affinity eluted glycoprotein to the purified type-1 fimbriae was demonstrated by a modified Western blot experiment. Our findings suggest that the 60 kDa glycoprotein may serve as a receptor for the type-1 fimbriae in the rat intestinal brush border membrane and thereby may help in mediating bacterial adherence to the host epithelium.

MeSH terms

  • Animals
  • Chromatography, Affinity
  • Chromatography, High Pressure Liquid
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme-Linked Immunosorbent Assay
  • Female
  • Fimbriae, Bacterial / metabolism*
  • Flow Cytometry
  • Intestines / ultrastructure*
  • Male
  • Mannose / pharmacology
  • Membrane Glycoproteins / metabolism*
  • Microvilli / chemistry*
  • Molecular Weight
  • Rats
  • Rats, Wistar
  • Salmonella typhimurium / metabolism*

Substances

  • Membrane Glycoproteins
  • Mannose