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Volume 148, Issue 4

Interaction of human Tamm–Horsfall glycoprotein with toxin Free

Abstract

Tamm–Horsfall glycoprotein (THP), which is synthesized by renal tubular cells, is the most abundant protein in normal human urine. Although its physiological function remains unclear, it has been proposed that THP may act as a defence factor against urinary tract infections by inhibiting the binding of S- and P-fimbriated to renal epithelial cells. Because THP-related proteins are also found in the superficial layers of the oral mucosa, the authors investigated the ability of THP to interfere with the cytoadherence of pathogenic bacteria that colonize mucosal surfaces other than those of the urogenital tract. In this report, it is shown that THP binds to virulent and reduces its adherence to both renal and pulmonary epithelial cells. This cytoadherence inhibitory effect was not observed with a mutant lacking the pertussis toxin (PTX) operon, and was dependent on the direct interaction of THP with the S2 subunit within the PTX B oligomer. The authors also show that the glycosylation moiety of THP is crucial for its binding to PTX. The THP–PTX interaction was exploited to develop an affinity chromatography method that allows a one-step purification of active PTX. These observations suggest that besides its anti-adherence activity, THP may also trap toxins produced by pathogenic bacteria that colonize mucosal surfaces.

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Keyword(s): CHO, chinese hamster ovary , cytoadherence , FHA, filamentous haemagglutinin , O-glycosidase, glycopeptide α-N-acetylgalactosaminidase , PTX, pertussis toxin , purification , THP, Tamm–Horsfall glycoprotein and virulence
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2002-04-01
2024-04-18
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Interaction of human Tamm–Horsfall glycoprotein with Bordetella pertussis toxin
Microbiology 148, 1193 (2002); https://doi.org/10.1099/00221287-148-4-1193
/content/journal/micro/10.1099/00221287-148-4-1193
/content/journal/micro/10.1099/00221287-148-4-1193
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