Our research approach is to understand the virulence of Trichomonas vaginalis through the identification and biochemical characterization of membrane immunogens with important biological properties or functions. Four major areas of research are emphasized: i) immunochemical membrane analysis of numerous long-term grown and fresh isolates targeting key antigens as molecules governing heterogeneity; ii) assessment and identification of (membrane) antigens shed or secreted by pathogenic trichomonads; iii) parasite cytadsorption to host cells; and finally iv) continued examination of the interaction between specific host macromolecules and T. vaginalis. Numerous methodologies will be employed which include standard radiolabeling procedures, chromatographic and electrophoretic methods, centrifugation-gradient procedures, antibody reagents, sensitive and specific radio-immunoprecipitation assays, and fluorescence-Nemarski-electron microscopy. Our overall objective is to identify highly immunogenic membrane antigens of T. vaginalis which possess key biologic functions, such as ligands involved in host cytadherence or receptors of specific host proteins, both processes essential for infection of human hosts. Studies in our laboratory presented in the Preliminary Results section continue to show the progress and feasibility of our plan at understanding this host-parasite relationship and using the pathogenic human trichomonads as models.

National Institute of Health (NIH)
National Institute of Allergy and Infectious Diseases (NIAID)
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Tropical Medicine and Parasitology Study Section (TMP)
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University of Texas Health Science Center San Antonio
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San Antonio
United States
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Engbring, J A; Alderete, J F (1998) Three genes encode distinct AP33 proteins involved in Trichomonas vaginalis cytoadherence. Mol Microbiol 28:305-13
Alderete, J F; Engbring, J; Lauriano, C M et al. (1998) Only two of the Trichomonas vaginalis triplet AP51 adhesins are regulated by iron. Microb Pathog 24:1-16
Provenzano, D; Khoshnan, A; Alderete, J F (1997) Involvement of dsRNA virus in the protein composition and growth kinetics of host Trichomonas vaginalis. Arch Virol 142:939-52
Engbring, J A; O'Brien, J L; Alderete, J F (1996) Trichomonas vaginalis adhesin proteins display molecular mimicry to metabolic enzymes. Adv Exp Med Biol 408:207-23
Alderete, J F; Provenzano, D; Lehker, M W (1995) Iron mediates Trichomonas vaginalis resistance to complement lysis. Microb Pathog 19:93-103
Provenzano, D; Alderete, J F (1995) Analysis of human immunoglobulin-degrading cysteine proteinases of Trichomonas vaginalis. Infect Immun 63:3388-95
Arroyo, R; Alderete, J F (1995) Two Trichomonas vaginalis surface proteinases bind to host epithelial cells and are related to levels of cytoadherence and cytotoxicity. Arch Med Res 26:279-85
Alderete, J F; Arroyo, R; Lehker, M W (1995) Analysis for adhesins and specific cytoadhesion of Trichomonas vaginalis. Methods Enzymol 253:407-14
Khoshnan, A; Alderete, J F (1995) Characterization of double-stranded RNA satellites associated with the Trichomonas vaginalis virus. J Virol 69:6892-7
Alderete, J F; O'Brien, J L; Arroyo, R et al. (1995) Cloning and molecular characterization of two genes encoding adhesion proteins involved in Trichomonas vaginalis cytoadherence. Mol Microbiol 17:69-83

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