Oquendo P, Hundt E, Lawler J, Seed B
Department of Genetics, Harvard Medical School, Boston, Massachusetts.
Cell. 1989 Jul 14;58(1):95-101. doi: 10.1016/0092-8674(89)90406-6.
Erythrocytes infected with P. falciparum express knob-like adhesion structures that allow the infected cells to cling to the postcapilliary endothelium of characteristic host organs. At present, the mechanism of cytoadherence is not fully understood. While parasitized erythrocytes have been shown to specifically bind to the platelet/matrix molecule thrombospondin, adherence to suitable target cells can also be blocked by monoclonal antibody OKM5, which recognizes a surface molecule expressed by hematopoietic cells and endothelium. In apparent reconciliation of these findings, it has been reported that the OKM5 antigen (CD36) is a receptor for thrombospondin. Here we report that expression of a CD36 cDNA clone in COS cells supports cytoadherence of parasitized erythrocytes but does not support increased binding of purified human thrombospondin.
感染恶性疟原虫的红细胞会表达出瘤状黏附结构，使受感染细胞能够黏附于特定宿主器官的毛细血管后内皮。目前，细胞黏附机制尚未完全明确。虽然已表明被寄生的红细胞能特异性结合血小板/基质分子血小板反应蛋白，但单克隆抗体OKM5也可阻断其与合适靶细胞的黏附，OKM5可识别造血细胞和内皮细胞表达的一种表面分子。为了协调这些明显矛盾的发现，有报道称OKM5抗原（CD36）是血小板反应蛋白的受体。在此我们报告，COS细胞中CD36 cDNA克隆的表达支持被寄生红细胞的细胞黏附，但不支持纯化的人血小板反应蛋白结合增加。
