Berendt A R, McDowall A, Craig A G, Bates P A, Sternberg M J, Marsh K, Newbold C I, Hogg N
Molecular Parasitology Group, Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, England.
Cell. 1992 Jan 10;68(1):71-81. doi: 10.1016/0092-8674(92)90207-s.
The intercellular adhesion molecule-1 (ICAM-1, CD54) is one of three putative endothelial receptors that mediate in vitro cytoadherence of P. falciparum-infected erythrocytes. Since cytoadherence to postcapillary venular endothelium is thought to be a major factor in the virulence of P. falciparum malaria, we have examined the interaction between ICAM-1 and the P. falciparum-infected cell, and have compared it with the interaction to the physiological counter receptor, the leukocyte integrin LFA-1. Our results demonstrate that the malaria-binding site resides in the first two domains of the ICAM-1 molecule and overlaps, but is distinct from, the LFA-1 site.
细胞间黏附分子-1(ICAM-1,CD54)是三种推测的内皮受体之一,介导恶性疟原虫感染红细胞的体外细胞黏附。由于对毛细血管后微静脉内皮的细胞黏附被认为是恶性疟原虫疟疾毒力的一个主要因素,我们研究了ICAM-1与恶性疟原虫感染细胞之间的相互作用,并将其与与生理反受体白细胞整合素LFA-1的相互作用进行了比较。我们的结果表明,疟疾结合位点位于ICAM-1分子的前两个结构域,与LFA-1位点重叠但不同。