PMID: 8580681Jan 1, 1995Paper

Two Trichomonas vaginalis surface proteinases bind to host epithelial cells and are related to levels of cytoadherence and cytotoxicity

Archives of Medical Research
Rossana Arroyo, J F Alderete

Abstract

Recent reports strongly suggest that cytoadherence and cytotoxicity by Trichomonas vaginalis require cysteine proteinase activity. Because of the large number of cysteine proteinases synthesized by T. vaginalis, a ligand assay was used to identify specific proteinases which may selectively target host cells. Two cysteine proteinases from trichomonal extracts with relative molecular masses (Mr) of 65,000 daltons (65-kDa) and 30-kDa were found to avidly bind to HeLa cell and vaginal epithelial cell surfaces. The two proteinases were distinguished by differential inhibition with leupeptin and N-alpha-p-tosyl-L-lysine chloromethyl ketone (TLCK). Leupeptin pretreatment of live organisms inhibited the 30-kDa proteinase, which concomitantly reduced or eliminated cytoadherence. The T. vaginalis isolates with low levels of cytoadherence also had diminished or no detectable 30-kDa proteinase activity. On the other hand, TLCK pretreatment inhibited both the 30-kDa and 65-kDa proteinases, which resulted in decreased levels of cytoadherence and totally abolished contact-dependent cytotoxicity. Furthermore, isolates capable of attachment but with little or no cytotoxicity toward HeLa cells had no detectable host cell-bound 65-kDa proteinase....Continue Reading

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