Medina-Acosta E, Karess R E, Schwartz H, Russell D G
Department of Pathology, NYU Medical Center, New York 10016.
Mol Biochem Parasitol. 1989 Dec;37(2):263-73. doi: 10.1016/0166-6851(89)90158-8.
The expression, processing and localization of the promastigote surface glycoprotein, gp63, in the amastigote form of Leishmania mexicana was examined. Metabolically labeled protein was immunoprecipitated from promastigotes and amastigotes. The isolated proteins were subjected to deglycosylation and partial peptide mapping. The cleavage products generated migrated similarly in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, indicating that the proteins were closely related. The majority of gp63 in amastigotes was inaccessible to surface-labeling procedures, and lacked the phosphatidylinositol membrane anchor. Immunolocalization of this subpopulation of gp63 revealed it to be present within the parasite's flagellar pocket. Despite the relative paucity of 'membrane-form' gp63, isolation and analysis of surface proteins from lesion amastigotes indicated that gp63 was the most abundant protein on the amastigote surface.
对墨西哥利什曼原虫无鞭毛体形式前鞭毛体表面糖蛋白gp63的表达、加工和定位进行了研究。从前鞭毛体和无鞭毛体中免疫沉淀代谢标记的蛋白质。对分离出的蛋白质进行去糖基化和部分肽图谱分析。产生的裂解产物在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳中迁移情况相似，表明这些蛋白质密切相关。无鞭毛体中的大多数gp63无法通过表面标记程序检测到，并且缺乏磷脂酰肌醇膜锚定。对这一亚群gp63的免疫定位显示它存在于寄生虫的鞭毛袋内。尽管“膜形式”gp63相对较少，但从病变无鞭毛体中分离和分析表面蛋白表明，gp63是无鞭毛体表面最丰富的蛋白质。
