López Ramsés, Valbuena John, Rodríguez Luis E, Ocampo Marisol, Vera Ricardo, Curtidor Hernando, Puentes Alvaro, García Javier, Ramirez Luis E, Patarroyo Manuel E
Fundación Instituto de Inmunología de Colombia (FIDIC) and Universidad Nacional de Colombia, Colombia.
Peptides. 2006 Jul;27(7):1685-92. doi: 10.1016/j.peptides.2006.02.001. Epub 2006 May 19.
This work shows that Plasmodium falciparum merozoite surface protein-6 (MSP-6) peptides specifically bind to membrane surface receptor on human erythrocytes. Three high activity binding peptides (HABPs) were found: peptides 31175 (41MYNNDKILSKNEVDTNIESN60) and 31178 (101YDIQATYQFPSTSGGNNVIP120) in the amino terminal region and 31191 (361EIDSTINNLVQEMIHLFSNNY380) at the carboxy terminal. Their binding to erythrocytes was saturable. HABPs 31191 and 31178 recognized 56 and 26 kDa receptors on erythrocyte membrane and inhibited in vitro Plasmodium falciparum merozoite invasion of erythrocytes by between 27% and 46% at 200 microg ml(-1) concentration, suggesting that these MSP-6 protein peptides play a possible role in the invasion process.
这项研究表明，恶性疟原虫裂殖子表面蛋白-6（MSP-6）肽可特异性结合人红细胞膜表面受体。发现了三种高活性结合肽（HABP）：氨基末端区域的肽31175（41MYNNDKILSKNEVDTNIESN60）和31178（101YDIQATYQFPSTSGGNNVIP120）以及羧基末端的31191（361EIDSTINNLVQEMIHLFSNNY380）。它们与红细胞的结合是可饱和的。HABP 31191和31178识别红细胞膜上56 kDa和26 kDa的受体，并在200 μg ml(-1)浓度下将体外恶性疟原虫裂殖子对红细胞的侵袭抑制27%至46%，这表明这些MSP-6蛋白肽在侵袭过程中可能发挥作用。
