Biosynthesis and processing of a Plasmodium falciparum schizont antigen recognized by immune serum and a monoclonal antibody.
Biosynthesis and processing of a Plasmodium falciparum schizont antigen recognized by immune serum and a monoclonal antibody.
复制标题
由免疫血清和单克隆抗体识别的恶性疟原虫的生物合成和加工。
DOI：
10.1084/jem.156.5.1528
复制
发表时间：
1982-11-01
影响因子：
15.3
通讯作者：
Freeman, R R
中科院分区：
文献类型：
--
作者：
Holder, A A;Freeman, R R
阶段特异性的蛋白质合成的红细胞形式的恶性疟原虫的疟疾寄生虫进行了研究，脉冲标记同步寄生虫培养物与[35 S]蛋氨酸在6小时的时间间隔，在一个完整的48小时的发展周期。约有40种标记的寄生虫蛋白可以与人免疫血清免疫沉淀，其中大部分与发育的前体阶段有关。特别地，一种抗体蛋白是195，000-mol wt种类，针对其产生鼠单克隆抗体。在间接免疫荧光试验中，该单克隆抗体89.1可与裂殖子中的寄生虫膜反应，也可与游离裂殖子表面反应。除了195，000-mol wt蛋白质之外，抗体89.1从标记的异步恶性疟原虫寄生虫培养物的提取物中免疫沉淀一系列低分子量多肽。通过肽图谱显示这些与195，000-mol wt蛋白相关。同步培养物的脉冲追踪标记和用抗体89.1的免疫沉淀显示，195，000-mol wt多肽特异性加工成低分子量产物伴随着鞭毛体成熟和裂殖子释放。这表明，这种恶性疟原虫蛋白质可能类似于啮齿动物疟疾寄生虫约氏疟原虫的类似处理的230，000-mol wt保护性抗原。
Stage-specific protein synthesis by the erythrocytic forms of the malaria parasite Plasmodium falciparum was investigated by pulse labeling synchronous parasite cultures with [35S]methionine at 6-h intervals during a complete 48-h developmental cycle. About 40 labeled parasite proteins could be immunoprecipitated with human immune serum, and most of these were associated with the schizont stage of development. In particular, one schizont protein was a 195,000-mol wt species against which a murine monoclonal antibody was produced. This monoclonal antibody, 89.1 reacted with the parasite membrane in schizonts and also with the surface of free merozoites in the indirect immunofluorescence test. In addition to the 195,000-mol wt protein, antibody 89.1 immunoprecipitated a series of lower-molecular weight polypeptides from extracts of labeled asynchronous P. falciparum parasite cultures. These were shown to be related to the 195,000-mol wt protein by peptide mapping. Pulse-chase labeling of synchronized cultures, and immunoprecipitation with antibody 89.1, showed that specific processing of the 195,000-mol wt polypeptide to the lower- molecular-weight products in concomitant with schizont maturation and merozoite release. It is suggested that this P. falciparum protein may be analogous to a similarly processed 230,000-mol wt protective antigen of the rodent malaria parasite, P. yoelii.