Curtidor Hernando, Rodríguez Luis E, Ocampo Marisol, López Ramses, García Javier E, Valbuena John, Vera Ricardo, Puentes Alvaro, Vanegas Magnolia, Patarroyo Manuel E
Fundación Instituto de Inmunología de Colombia, Carrera 50 No. 26-00, Bogotá, Colombia.
Protein Sci. 2005 Feb;14(2):464-73. doi: 10.1110/ps.041084305.
Erythrocyte binding ligand 1 (EBL-1) is a member of the ebl multigene family involved in Plasmodium falciparum invasion of erythrocytes. We found that five EBL-1 high-activity binding peptides (HABPs) bound specifically to erythrocytes: 29895 ((41)HKKKSGELNNNKSGILRSTY(60)), 29903 ((201)LYECGK-KIKEMKWICTDNQF(220)), 29923 ((601)CNAILGSYADIGDIVRGLDV(620)), 29924((621)WRDINTNKLSEK-FQKIFMGGY(640)), and 30018 ((2481)LEDIINLSKKKKKSINDTSFY(2500)). We also show that binding was saturable, not sialic acid-dependent, and that all peptides specifically bound to a 36-kDa protein on the erythrocyte membrane. The five HABPs inhibited in vitro merozoite invasion depending on the peptide concentration used, suggesting their possible role in the invasion process.
红细胞结合配体1(EBL-1)是参与恶性疟原虫入侵红细胞的ebl多基因家族成员。我们发现五个EBL-1高活性结合肽(HABP)能特异性结合红细胞:29895((41)HKKKSGELNNNKSGILRSTY(60))、29903((201)LYECGK-KIKEMKWICTDNQF(220))、29923((601)CNAILGSYADIGDIVRGLDV(620))、29924((621)WRDINTNKLSEK-FQKIFMGGY(640))和30018((2481)LEDIINLSKKKKKSINDTSFY(2500))。我们还表明这种结合是可饱和的,不依赖于唾液酸,并且所有肽都能特异性结合红细胞膜上的一种36 kDa蛋白。这五个HABP根据所用肽的浓度在体外抑制裂殖子入侵,表明它们在入侵过程中可能发挥的作用。