Iqbal J, Siddique A B, Ahlborg N, Perlmann P, Berzins K
Department of Immunology, Stockholm University, Sweden.
Parasitology. 1995 Jun;110 ( Pt 5):503-11. doi: 10.1017/s0031182000065215.
Cytoadherence of Plasmodium falciparum-infected erythrocytes plays an important role in the pathogenesis of cerebral malaria. The identity of cell surface molecules on parasitized erythrocytes involved in cytoadherence is of great interest to understand the molecular basis of this mechanism. Peptide sequences derived from exofacial loops of the erythrocyte antigen band 3 from parasitized erythrocytes have previously been shown to inhibit cytoadherence. We now report that a non-repeated region of Pf155/RESA (residues 213-218) contains a hexapeptide motif being highly homologous to cytoadherence inhibitory sequences from band 3. Synthetic peptides containing the hexapeptide motif of Pf155/RESA inhibited the binding of P. falciparum-infected erythrocytes to melanoma cells in vitro. Furthermore, individuals residing in malaria-endemic areas have antibodies reactive with epitopes involving these motifs in band 3 and in Pf155/RESA.
恶性疟原虫感染的红细胞的细胞黏附在脑型疟疾的发病机制中起重要作用。参与细胞黏附的被寄生红细胞表面分子的身份对于理解这一机制的分子基础非常重要。先前已表明，源自被寄生红细胞的红细胞抗原带3胞外环的肽序列可抑制细胞黏附。我们现在报告，Pf155/RESA的一个非重复区域（第213 - 218位氨基酸残基）包含一个六肽基序，该基序与带3的细胞黏附抑制序列高度同源。含有Pf155/RESA六肽基序的合成肽在体外抑制了恶性疟原虫感染的红细胞与黑色素瘤细胞的结合。此外，居住在疟疾流行地区的个体具有与涉及带3和Pf155/RESA中这些基序的表位反应的抗体。
