Journal article
Relatedness of structures of a major immunogen in Trichomonas vaginalis isolates
Infection and immunity, Vol.57(6), pp.1849-1853
06/1989
Handle:
https://hdl.handle.net/2376/104256
PMCID: PMC313366
PMID: 2785964
Abstract
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.
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Details
- Title
- Relatedness of structures of a major immunogen in Trichomonas vaginalis isolates
- Creators
- J F Alderete - Department of Microbiology, University of Texas Health Science Center, San Antonio 78284-7758K A Neale
- Publication Details
- Infection and immunity, Vol.57(6), pp.1849-1853
- Academic Unit
- Molecular Biosciences, School of
- Publisher
- United States
- Grant note
- AI-22380 / NIAID NIH HHS K04-AI-00584 / NIAID NIH HHS
- Identifiers
- 99900546558301842
- Language
- English
- Resource Type
- Journal article