Bozner P
Department of Pathology, University of South Alabama Medical Center, Mobile 36617, USA.
J Parasitol. 1997 Apr;83(2):224-9.
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.
通过与大肠杆菌DnaK的交叉反应多克隆抗体、棉铃虫Hsp60的多克隆抗体以及蓝细菌GroEL/Hsp60的多克隆抗体，检测到阴道毛滴虫中分别属于Hsp70和Hsp60家族、分子量分别为72 kDa和58 kDa的热休克蛋白（Hsp）同源物。用光镜观察发现，在用抗DnaK处理的寄生虫4微米冷冻切片上，阴道毛滴虫呈现弥漫性且细颗粒状的细胞内染色。免疫电子显微镜显示，该抗体还识别主要存在于高尔基体、内质网和氢化酶体中的阴道毛滴虫抗原。两种针对Hsp60变体的抗体在光镜下的颗粒中定位了一种同源抗原，该颗粒对应于阴道毛滴虫的氢化酶体。
