Ocampo Marisol, Curtidor Hernando, Vera Ricardo, Valbuena John J, Rodríguez Luis E, Puentes Alvaro, López Ramses, García Javier E, Tovar Diana, Pacheco Paola, Navarro Miguel A, Patarroyo Manuel E
Fundación Instituto de Inmunologia de Colombia, Universidad Nacional de Colombia, Avda. Calle 26 No. 50-00, Bogotá, Colombia.
Biochem Biophys Res Commun. 2004 Mar 5;315(2):319-29. doi: 10.1016/j.bbrc.2004.01.050.
MAEBL is an erythrocyte binding protein located in the rhoptries and on the surface of mature merozoites, being expressed at the beginning of schizogony. The structure of MAEBL originally isolated from rodent malaria parasites suggested a molecule likely to be involved in invasion. We thus became interested in identifying possible MAEBL functional regions. Synthetic peptides spanning the MAEBL sequence were tested in erythrocyte binding assays to identify such possible MAEBL functional regions. Nine high activity binding peptides (HABPs) were identified: two were found in the M1 domain, one was found between the M1 and M2 regions, five in the erythrocyte binding domain (M2), and one in the protein's repeat region. The results showed that peptide binding was saturable; some HABPs inhibited in vitro merozoite invasion and specifically bound to a 33kDa protein on red blood cell membrane. HABPs' possible function in merozoite invasion of erythrocytes is also discussed.
MAEBL是一种红细胞结合蛋白，位于棒状体和成熟裂殖子表面，在裂体增殖开始时表达。最初从啮齿动物疟原虫中分离出的MAEBL结构表明，该分子可能参与入侵过程。因此，我们开始对确定MAEBL可能的功能区域感兴趣。在红细胞结合试验中测试了跨越MAEBL序列的合成肽，以确定此类可能的MAEBL功能区域。鉴定出九个高活性结合肽（HABP）：两个位于M1结构域，一个位于M1和M2区域之间，五个位于红细胞结合结构域（M2），一个位于蛋白质的重复区域。结果表明，肽结合是可饱和的；一些HABP抑制体外裂殖子入侵，并特异性结合红细胞膜上的一种33kDa蛋白。还讨论了HABP在裂殖子入侵红细胞中的可能功能。
