Frommel T O, Button L L, Fujikura Y, McMaster W R
Department of Medical Genetics, University of British Columbia, Vancouver, Canada.
Mol Biochem Parasitol. 1990 Jan 1;38(1):25-32. doi: 10.1016/0166-6851(90)90201-v.
Leishmania exist as extracellular promastigotes which multiply in the gut of the sandfly insect vector and as intracellular amastigotes which divide in the phagolysosome of mononuclear phagocytic cells of the mammalian host. Promastigotes express a major surface glycoprotein of 63 kDa, referred to as GP63. The expression of GP63 in both Leishmania life stages was studied using rabbit antibodies against native GP63 as well as rabbit antibodies against recombinant GP63 that was synthesized in an Escherichia coli expression system. Immunofluorescence staining detected GP63 in intracellular amastigotes contained within a macrophage cell line and within freshly isolated lesion amastigotes. Western blot analysis using anti-recombinant GP63 antibodies also demonstrated that amastigotes synthesize GP63 which may undergo differential post-translational processing as compared to promastigote GP63.
利什曼原虫以细胞外前鞭毛体的形式存在，它们在白蛉昆虫媒介的肠道中繁殖；同时也以细胞内无鞭毛体的形式存在，在哺乳动物宿主的单核吞噬细胞的吞噬溶酶体中分裂。前鞭毛体表达一种63 kDa的主要表面糖蛋白，称为GP63。利用针对天然GP63的兔抗体以及针对在大肠杆菌表达系统中合成的重组GP63的兔抗体，研究了GP63在利什曼原虫两个生活阶段的表达情况。免疫荧光染色在巨噬细胞系内的细胞内无鞭毛体以及新鲜分离的病灶无鞭毛体中检测到了GP63。使用抗重组GP63抗体的蛋白质印迹分析也表明，无鞭毛体合成GP63，与前鞭毛体GP63相比，它可能经历不同的翻译后加工。
