Stanley H A, Reese R T
Proc Natl Acad Sci U S A. 1985 Sep;82(18):6272-5. doi: 10.1073/pnas.82.18.6272.
A system has been developed that allows efficient production of monkey monoclonal antibodies from owl monkeys. Splenocytes or peripheral blood lymphocytes from monkeys immune to the human malarial parasite, Plasmodium falciparum, were fused with P3X63 Ag8.653 mouse myelomas. The resulting hybridomas were screened by an indirect fluorescent antibody test for the production of monkey monoclonal antibodies (mAb) reactive with P. falciparum. Most of the mAb reacted with the P. falciparum merozoites and immunoprecipitated a parasite-derived glycoprotein having a relative molecular weight of 185,000. These mAb gave a minimum of five different immunoprecipitation patterns, thus demonstrating that a large number of polypeptides obtained when parasitized erythrocytes are solubilized share epitopes with this large glycoprotein. In addition, mAb were obtained that reacted with antigens associated with the infected erythrocyte membrane. One of these mAb bound a Mr 95,000 antigen.
已开发出一种系统,可高效生产来自夜猴的猴单克隆抗体。将对人类疟原虫恶性疟原虫免疫的猴子的脾细胞或外周血淋巴细胞与P3X63 Ag8.653小鼠骨髓瘤细胞融合。通过间接荧光抗体试验筛选所得杂交瘤,以检测与恶性疟原虫反应的猴单克隆抗体(mAb)的产生。大多数mAb与恶性疟原虫裂殖子反应,并免疫沉淀出一种相对分子质量为185,000的寄生虫衍生糖蛋白。这些mAb呈现出至少五种不同的免疫沉淀模式,从而表明当被寄生的红细胞溶解时获得的大量多肽与这种大糖蛋白共享表位。此外,还获得了与感染红细胞膜相关抗原反应的mAb。其中一种mAb结合了一种分子量为95,000的抗原。