Relatedness of structures of a major immunogen in Trichomonas vaginalis isolates.

AUTOR(ES)

Alderete, J. F.

RESUMO

Solubilization of live Trichomonas vaginalis organisms with detergent caused the release of cysteine proteinases in the detergent extract which were inhibitable with N-alpha-p-tosyl-L-lysine chloromethyl ketone. The detergent extracts of all isolates tested possessed similar cysteine proteinase activities. These parasite proteinases rapidly degraded a prominent immunogen whose surface disposition undergoes phenotypic variation in some isolates. The relatedness of the forms of this immunogen among all isolates tested was confirmed by identical immunoblot patterns of autolysed immunogen, and data suggest the presence of repeating units or at least equidistant sites for proteinase cleavage within the immunogen molecule.

Documentos Relacionados

• Monoclonal antibody to a major surface glycoprotein immunogen differentiates isolates and subpopulations of Trichomonas vaginalis.
• Analysis of the proteinases of representative Trichomonas vaginalis isolates.
• Monoclonal antibody to a major glycoprotein immunogen mediates differential complement-independent lysis of Trichomonas vaginalis.
• Biological variability in clinical isolates of Trichomonas vaginalis
• Concordance between genetic relatedness and phenotypic similarities of Trichomonas vaginalis strains