Isolation and characterization of a receptor for type 1 fimbriae of Escherichia coli from guinea pig erythrocytes

J Biol Chem. 1988 Apr 15;263(11):5362-7.


The adhesion of Escherichia coli to eukaryotic cells is mediated by proteinaceous surface appendages called fimbriae and complementary receptors on host cells. Although type 1 fimbriae, which contain a D-mannose-reactive lectin, have been well studied little is known about the binding mechanism of isolated fimbriae to individual cell receptors. This report describes the isolation and purification of a guinea pig erythrocyte receptor for type 1 fimbriae. Erythrocyte membranes were dissolved in 0.5% Triton X-100 and the receptor isolated and purified by affinity chromatography using type 1 fimbriae immobilized on Sepharose. The 65-kDa receptor, which inhibits the agglutination of guinea pig erythrocytes by type 1 fimbriated E. coli, has a pI of 8.5-8.7, and binds concanavalin A and type 1 fimbriae in a dose-dependent and saturable manner. The fimbrial binding activity of the receptor was reduced when treated with sodium metaperiodate, endoglycosidase H, trypsin, and V8 protease, suggesting the isolated receptor is a glycoprotein with N-linked carbohydrate units. Isolated type 1 fimbriae inhibited the binding of fimbriated E. coli to purified receptor in a dose- and time-related fashion. The calculated binding affinity was 6 X 10(6) M-1, a value consistent with the low binding affinity expected from previous studies of the agglutination of guinea pig erythrocytes by isolated type 1 fimbriae.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Bacterial Adhesion*
  • Chemical Phenomena
  • Chemistry, Physical
  • Dose-Response Relationship, Drug
  • Erythrocytes / analysis*
  • Escherichia coli / physiology*
  • Fimbriae, Bacterial / metabolism
  • Guinea Pigs
  • Hemagglutination / drug effects
  • Hexosaminidases / metabolism
  • Membrane Proteins / analysis
  • Receptors, Immunologic / isolation & purification*
  • Receptors, Immunologic / metabolism
  • Solubility


  • Membrane Proteins
  • Receptors, Immunologic
  • pili, bacterial receptor
  • Hexosaminidases