Immunological detection and subcellular localization of Hsp70 and Hsp60 homologs in Trichomonas vaginalis.
Heat shock protein (Hsp) homologs of Trichomonas vaginalis belonging to Hsp70 and Hsp60 families with Mr 72 and 58 kDa, respectively, were detected by cross-reacting polyclonal antibody to DnaK of Escherichia coli. polyclonal antibody to Hsp60 of Heliothis virescens, and polyclonal antibody to GroEL/Hsp60 of cyanobacteria. A diffuse and finely granular intracellular staining of T. vaginalis was obtained with anti-DnaK on frozen 4-micron sections of the parasite as revealed by light microscopy. This antibody also recognized T. vaginalis antigen(s) present mainly in the Golgi apparatus, endoplasmic reticulum, and hydrogenosomes, as demonstrated by immunoelectron microscopy. Both antibodies against Hsp60 variants localized a homolog antigen in light microscopic granules, corresponding to hydrogenosomes of T. vaginalis.
Bozner
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Department of Pathology, University of South Alabama Medical Center, Mobile 36617, USA.
D000818:Animals; D015153:Blotting, Western; D018834:Chaperonin 60 / Q000032:analysis* / Q000276:immunology; D003429:Cross Reactions; D018840:HSP70 Heat-Shock Proteins / Q000032:analysis* / Q000276:immunology; D007106:Immune Sera / Q000276:immunology; D007150:Immunohistochemistry; D016253:Microscopy, Immunoelectron; D014246:Trichomonas vaginalis / Q000737:chemistry* / Q000648:ultrastructure
D018834:Chaperonin 60; D018840:HSP70 Heat-Shock Proteins; D007106:Immune Sera