Reinhart H, Obedeanu N, Merzbach D, Sobel J D
Division of Infectious Diseases, Wayne State University, Detroit, Michigan.
J Infect Dis. 1991 Aug;164(2):404-6. doi: 10.1093/infdis/164.2.404.
Mannose residues on the outer membranes of polymorphonuclear leukocytes (PMNL) are capable of binding mannose-sensitive Escherichia coli. Tamm-Horsfall protein, a major urinary glycoprotein, has also been shown to bind mannose-sensitive E. coli via mannose-containing side chains. The effect of Tamm-Horsfall protein on the interaction between PMNL and mannose-sensitive E. coli was studied by measuring luminol-dependent chemoluminescence after bacterial stimulation. In the presence of 0.475, 4.75, 47.5, and 475 mg/l Tamm-Horsfall protein, chemoluminescence responses were reduced in a dose-dependent fashion by 8.7%, 38.1%, 60.3%, and 96.1%, respectively. Addition of 0.003 units/ml alpha-mannosidase reversed the effect of increasing concentrations significantly. Thus, urinary Tamm-Horsfall protein seems to compete with PMNL for mannose-sensitive E. coli in a mannose-sensitive fashion, thereby significantly reducing the role of PMNL as a defense mechanism in the urine of patients with urinary tract infection.