Herrera S, Rudin W, Herrera M, Clavijo P, Mancilla L, de Plata C, Matile H, Certa U
Department of Microbiology, School of Health, Universidad del Valle, Cali, Colombia.
EMBO J. 1993 Apr;12(4):1607-14. doi: 10.1002/j.1460-2075.1993.tb05805.x.
The major surface protein MSP-1 of Plasmodium falciparum blood-stage malaria parasites contains notably conserved sequence blocks with unknown function. The recombinant protein 190L, which represents such a block, exhibits a high affinity for red blood cell membranes. We demonstrate that both 190L and native MSP-1 protein bind to the inner red blood cell membrane skeleton protein spectrin. By using overlapping peptides covering the 190L molecule, we show that the spectrin contact site of 190L is included in a linear sequence of 30 amino acid residues. Association of 190L with naturally occurring spectrin deficient red blood cells is drastically reduced. In the same cells parasite invasion is normal, but the intracellular parasite development arrests late in the trophozoite stage. A similar situation arises when synthetic peptides covering the spectrin recognition sequence of 190L are added to P.falciparum cultures. These data and the cellular localization of MSP-1 suggest the possibility that MSP-1 associates with spectrin under natural conditions.
恶性疟原虫血液期疟原虫的主要表面蛋白MSP-1含有明显保守的序列块，其功能未知。代表这样一个序列块的重组蛋白190L对红细胞膜具有高亲和力。我们证明190L和天然MSP-1蛋白都与红细胞内膜骨架蛋白血影蛋白结合。通过使用覆盖190L分子的重叠肽，我们表明190L的血影蛋白接触位点包含在30个氨基酸残基的线性序列中。190L与天然存在的血影蛋白缺陷红细胞的结合显著减少。在相同的细胞中，寄生虫入侵正常，但细胞内寄生虫发育在滋养体阶段后期停滞。当将覆盖190L血影蛋白识别序列的合成肽添加到恶性疟原虫培养物中时，也会出现类似情况。这些数据以及MSP-1的细胞定位表明，在自然条件下MSP-1可能与血影蛋白结合。
