Puentes Alvaro, García Javier, Ocampo Marisol, Rodríguez Luis, Vera Ricardo, Curtidor Hernando, López Ramsés, Suarez Jorge, Valbuena John, Vanegas Magnolia, Guzman Fanny, Tovar Diana, Patarroyo Manuel E
Fundacion Instituto de Inmunología de Colombia and Universidad Nacional de Colombia, Carrera 50 No. 26-00, Bogota, Colombia.
Peptides. 2003 Jul;24(7):1015-23. doi: 10.1016/s0196-9781(03)00185-2.
This work determined Plasmodium falciparum merozoite surface protein-8 (MSP-8) regions specifically binding to membrane surface receptors on human erythrocytes. Five high activity binding peptides (HABPs), whose binding to erythrocytes became saturable and sensitive on being treated with neuraminidase and chymotrypsin were identified from the MSP-8 protein. Those amino acids directly involved in interaction with erythrocytes were also determined for each one of the HABPs. Some of them specifically recognized 28, 46, and 73 kDa erythrocyte membrane proteins. Some HABPs inhibited in vitro P. falciparum merozoite invasion of erythrocytes by up to 98%, suggesting the MSP-8 protein's possible role in the invasion process.
这项研究确定了恶性疟原虫裂殖子表面蛋白8(MSP-8)中与人类红细胞膜表面受体特异性结合的区域。从MSP-8蛋白中鉴定出了5种高活性结合肽(HABP),这些肽与红细胞的结合在用神经氨酸酶和胰凝乳蛋白酶处理后变得具有饱和性且敏感。还确定了每种HABP中直接参与与红细胞相互作用的氨基酸。其中一些肽能特异性识别28 kDa、46 kDa和73 kDa的红细胞膜蛋白。一些HABP在体外可将恶性疟原虫裂殖子对红细胞的侵袭抑制高达98%,这表明MSP-8蛋白在侵袭过程中可能发挥作用。