Relatedness of structures of a major immunogen in Trichomonas vaginalis isolates

J. F. Alderete, K. A. Neale

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

Solubilization of live Trichomonas vaginalis organisms with detergent caused the release of cysteine proteinases in the detergent extract which were inhibitable with N-α-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.

Original languageEnglish (US)
Pages (from-to)1849-1853
Number of pages5
JournalInfection and immunity
Volume57
Issue number6
StatePublished - 1989

ASJC Scopus subject areas

  • Parasitology
  • Microbiology
  • Immunology
  • Infectious Diseases

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