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The specificity of the interaction between Treponema pallidum and fibronectin was demonstrated. Treatment of host cells with only antifibronectin sera and not anticollagen or antilaminin sera, inhibited treponemal cytadsorption. Incubation of fibronectin-coated coverslips with monoclonal antibody to the cell-binding domain of fibronectin reduced treponemal(More)
Specific receptor-mediated binding by Trichomonas vaginalis of human erythrocytes was demonstrated. The ability of live parasites to internalize erythrocytes was also documented. In vitro growth assays during lipid-free and iron-limiting conditions that do not support the survival of T. vaginalis organisms showed that purified erythrocyte lipids and(More)
Three putative Treponema pallidum ligands (P1, P2, and P3) that bind host fibronectin were characterized by peptide mapping. Papain digestion of each protein yielded a comigrating peptide of approximately 12,000 molecular weight. An antibody to this protein fragment inhibited T. pallidum host cytadherence, indicating that this peptide may be the functional(More)
Adherence to host target cells is a critical step in establishing infection with the sexually transmitted pathogen Trichomonas vaginalis. Four parasite surface proteins mediating attachment to vaginal epithelial cells have been identified. One surface protein, termed AP33, was characterized further to identify domains interactive with previously generated(More)
BACKGROUND AP65 is a prominent adhesin of Trichomonas vaginalis that mediates binding of parasites to host vaginal epithelial cells (VECs). AP65 with no secretion signal sequence, membrane targeting peptide, and anchoring motif was recently found to be secreted. RESULTS We first wanted to demonstrate surface association of AP65 to the parasite followed by(More)
The syphilis bacterium, Treponema pallidum, parasitizes host cells through recognition of fibronectin (Fn) on cell surfaces. The active site of the Fn molecule has been identified as a four-amino acid sequence, arg-gly-asp-ser (RGDS), located on each monomer of the cell-binding domain. The synthetic heptapeptide gly-arg-gly-asp-ser-pro-cys (GRGDSPC), with(More)
Levels of adherence of Trichomonas vaginalis to epithelial cells was found to be modulated by iron. Cytoadherence values were greater than or equal to twofold higher for trichomonads grown in a complex cultivation medium supplemented with iron. This increase in adherence levels was specifically mediated by iron; parasites cultured in a low-iron medium in(More)
Trichomonosis, a sexually transmitted infection (STI) caused by the protist Trichomonas vaginalis, has significant public health relevance. The annual incidence is ,8 million women in the United States and 170 million worldwide, with an equal number of infected male partners [1]. Both men and women infected with T. vaginalis are at increased risk for human(More)
Trichomonas vaginalis is a protozoan parasite that causes a widely distributed sexually transmitted disease (STD). Since immunoglobulin G (IgG) antibodies to specific trichomonad immunogens are found in serum and vaginal washes (VWs) from patients with trichomoniasis, a potential mechanism of immune evasion by this parasite might be the ability of T.(More)
Trichomonas vaginalis isolates were examined for the presence of viral double-stranded RNA (dsRNA) and the property of phenotypic variation. Only the heterogeneous isolates composed of mAb-reactive and -nonreactive organisms, as determined by indirect immunofluorescence and flow cytofluorometry, and capable of phenotypic variation possessed the dsRNA. Both(More)