Ardalan, Shahed2013-11-072013-11-0720072007Source: Masters Abstracts International, Volume: 46-03, page: 1398.http://hdl.handle.net/10393/27441http://dx.doi.org/10.20381/ruor-18709Trichomonas vaginalis is the cause of human trichomoniasis. Although acquisition of iron by binding to host hemoglobin through distinct receptor(s) has been described in this parasite, no specific hemoglobin-binding site has been reported. Our hypotheses were: (1) hemolytic activity of T. vaginalis isolates correlates with the virulence, and (2) T. vaginalis binds hemoglobin through a specific surface receptor. The in vitro hemolytic activities of four T. vaginalis strains were examined. No correlation between hemolytic activity and virulence in different isolates was found. Using hemoglobin-affinity chromatography, two protein bands of approximately 48 and 63 kDa were detected, the former binds preferentially to heme. Mass spectral analysis indicated that the 48- and 63-kDa proteins had significant homology with the subunits of two T. vaginalis adhesins: AP51 and AP65, respectively. This study confirms the existence of multifunctional proteins in T. vaginalis, which enable the parasite to survive in a constantly changing environment like human vagina.93 p.enBiology, Microbiology.Chemistry, Biochemistry.Thesis