Quantitation of Tamm-Horsfall protein binding to uropathogenic Escherichia coli and lectins

J Infect Dis. 1990 Dec;162(6):1335-40. doi: 10.1093/infdis/162.6.1335.


In quantitative experiments using ELISA, binding of Tamm-Horsfall protein (THP) to uropathogenic Escherichia coli was studied with monoclonal antibody to THP. Adherence to E. coli bearing type 1 fimbriae was proportional to THP concentration and size of the bacterial inoculum. Type 1 fimbriae-bearing E. coli bound 50 times more THP than did non-type 1-fimbriated or P-fimbriated strains. Concanavalin A and wheat germ agglutinin bound THP in a dose-dependent fashion, whereas pokeweed mitogen and Vicia villosa B4 isolectin did not. Addition of mannose and N-acetylglucosamine reduced adherence of THP to concanavalin A and wheat germ agglutinin by 50%-80%. Sugar inhibition studies suggested that the fimbrial receptor site for THP has lectin-like properties and that THP binds to fimbriae via its mannose side chains. This quantitative assay is useful for studying the interaction between THP, uroepithelial cells, and bacteria in vitro.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agglutination Tests
  • Bacterial Adhesion / drug effects
  • Carbohydrates / pharmacology
  • Concanavalin A / metabolism
  • Enzyme-Linked Immunosorbent Assay
  • Escherichia coli / drug effects
  • Escherichia coli / metabolism*
  • Escherichia coli / ultrastructure
  • Escherichia coli Infections / microbiology*
  • Fimbriae, Bacterial / metabolism
  • Humans
  • Lectins / metabolism*
  • Mucoproteins / metabolism*
  • Urinary Tract Infections / microbiology*
  • Uromodulin
  • Wheat Germ Agglutinins / metabolism


  • Carbohydrates
  • Lectins
  • Mucoproteins
  • UMOD protein, human
  • Uromodulin
  • Wheat Germ Agglutinins
  • Concanavalin A