TARGET ANTIGENS OF MALARIA TRANSMISSION BLOCKING IMMUNITY EXIST AS A STABLE MEMBRANE-BOUND COMPLEX
TARGET ANTIGENS OF MALARIA TRANSMISSION BLOCKING IMMUNITY EXIST AS A STABLE MEMBRANE-BOUND COMPLEX
复制标题
DOI：
10.1111/j.1365-3024.1987.tb00511.x
复制
发表时间：
1987-05-01
影响因子：
2.2
通讯作者：
KUMAR, N
中科院分区：
文献类型：
--
作者：
KUMAR, N
通过阻断蚊子中肠中的雄配子对雌配子的受精来阻断疟疾传播的单克隆抗体（MoAb）免疫沉淀三种多肽（表观非还原摩尔比为1：1）。230，000、48，000、45，000重量）。早期的研究表明，与单克隆抗体反应的表位仅存在于分子上。wt 230，000多肽在鸡原卟啉单胞菌和48，000/45，000 mol.恶性疟原虫中的wt抗原（Kumar 1985，Vermeulen等1985）。在凝胶渗透色谱中，发现所有三种多肽共洗脱。使用交联试剂交联完整细胞上和可溶性提取物中的蛋白质。单克隆抗体免疫沉淀的交联产物显示出近似的mol. wt %至300，000，表明高摩尔比和低摩尔比之间的化学计量为1：1。wt多肽。也有证据表明存在48，000/45，000摩尔的亚群。wt多肽，其不与230，000 mol. wt多肽。这些数据表明，230，000多肽与48，000和45，000多肽物理结合;高分子量和低分子量多肽似乎存在于稳定的膜结合复合物中。
Monoclonal antibodies (MoAbs) blocking transmisison of malaria by blocking fertilization of female gametes by male gametes in the mosquito midgut immunoprecipitate three polypeptides (apparent non-reduced mol. wt of 230,000, 48,000, 45,000) from the surface of gametes and zygotes of Plasmodium gallinaceum and P. falciparum. Earlier studies have shown that the epitopes with which the MoAbs react are present only on the mol. wt 230,000 polypeptide in P. gallinaceum and the 48,000/45,000 mol. wt antigens in P. falciparum (Kumar 1985, Vermeulen et al. 1985). In gel permeation chromatography all three polypeptides were found to be co-eluted. Cross-linking reagents were used to cross-link proteins on the intact cells and in the soluble extracts. The cross-linked product immunoprecipitated by the MoAbs showed an approximate mol. wt of 290,000 to 300,000, suggesting a stoichiometry of 1:1 between the high and low mol. wt polypeptides. Evidence was also obtained for the existence of a subpopulation of the 48,000/45,000 mol. wt polypeptides which is not complexed with the 230,000 mol. wt polypeptide. These data indicate that the 230,000 polypeptide is physically associated with the 48,000 and 45,000 polypeptides; the high and low molecular weight polypeptides appear to exist in a stable membrane bound complex.