Section 42
Chapter 41,147

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

Reinhart, H.H.; Obedeanu, N.; Sobel, J.D.

Journal of Infectious Diseases 162(6): 1335-1340


ISSN/ISBN: 0022-1899
PMID: 1977810
DOI: 10.1093/infdis/162.6.1335
Accession: 041146801

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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.

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