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首页> 外文期刊>Infection and immunity >Natural variation within the principal adhesion domain of the Plasmodium vivax duffy binding protein.
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Natural variation within the principal adhesion domain of the Plasmodium vivax duffy binding protein.

机译：间日疟原虫达菲结合蛋白的主要粘附域内的自然变化。

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The blood-stage development of malaria parasites is initiated by the invasion of merozoites into susceptible erythrocytes. Specific receptor-ligand interactions must occur for the merozoites to first attach to and then invade erythrocytes. Because the invasion process is essential for the parasite's survival and the merozoite adhesion molecules are exposed on the merozoite surface during invasion, these adhesion molecules are candidates for antibody-dependent malaria vaccines. The Duffy binding protein of Plasmodium vivax belongs to a family of erythrocyte-binding proteins that contain functionally conserved cysteine-rich regions. The amino cysteine-rich regions of these homologous erythrocyte-binding proteins were recently identified for P. vivax, Plasmodium knowlesi, and Plasmodium falciparum as the principal erythrocyte-binding domains (C. Chitnis and L. H. Miller, J. Exp. Med. 180:497-506, 1994, and B. K. L. Sim, C. E. Chitnis, K. Wasniowska, T. J. Hadley, and L. H. Miller, Science 264:1941-1944, 1994). We report that amino acids in this critical ligand domain of the P. vivax Duffy binding protein are hypervariable, but this variability is limited. Hypervariability of the erythrocyte-binding domain suggests that this domain is the target of an effective immune response, but conservation of amino acid substitutions indicates that functional constraints limit this variation. In addition, the amino cysteine-rich region and part of the hydrophilic region immediately following it were the site of repeated homologous recombinations as represented by tandem repeat sequence polymorphisms. Similar polymorphisms have been identified in the same region of the homologous genes of P. falciparum and P. knowlesi, suggesting that there is a common mechanism of recombination or gene conversion that occurs in these Plasmodium genes.
机译：疟原虫的血液阶段发展是由裂殖子侵入易感红细胞引起的。裂殖子必须先发生特定的受体-配体相互作用，然后才能与红细胞结合。因为入侵过程对于寄生虫的生存至关重要，并且裂殖子粘附分子在入侵过程中暴露于裂殖子表面，所以这些粘附分子是抗体依赖性疟疾疫苗的候选者。间日疟原虫的达菲结合蛋白属于红细胞结合蛋白家族，其含有功能上保守的富含半胱氨酸的区域。这些同源红细胞结合蛋白的富含氨基半胱氨酸的区域最近被鉴定为间日疟原虫，诺氏疟原虫和恶性疟原虫为主要的红细胞结合域（C.Chitnis和LH Miller，J.Exp.Med.180： 1994年，第497-506页，以及BKL Sim，CE Chitnis，K.Wasniowska，TJ Hadley和LH Miller，Science 264：1941-1944，1994）。我们报告说，间日疟原虫达菲结合蛋白的这个关键配体域中的氨基酸是高变的，但是这种可变性是有限的。红细胞结合结构域的高变性表明该结构域是有效免疫反应的靶标，但是氨基酸取代的保守性表明功能限制限制了这种变化。另外，如串联重复序列多态性所代表的，富含氨基半胱氨酸的区域和紧随其后的部分亲水区域是重复同源重组的位点。在恶性疟原虫和诺氏疟原虫的同源基因的相同区域中已鉴定出相似的多态性，这表明在这些疟原虫基因中存在重组或基因转化的共同机制。

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