Instituto de Inmunología del Valle, Universidad del Valle, Cali, Colombia.
Am J Trop Med Hyg. 2011 Feb;84(2 Suppl):64-70. doi: 10.4269/ajtmh.2011.09-0517.
Merozoite surface protein 1 (MSP-1) is a polymorphic malaria protein with functional domains involved in parasite erythrocyte interaction. Plasmodium vivax MSP-1 has a fragment (Pv200L) that has been identified as a potential subunit vaccine because it is highly immunogenic and induces partial protection against infectious parasite challenge in vaccinated monkeys. To determine the extent of genetic polymorphism and its effect on the translated protein, we sequenced the Pv200L coding region from isolates of 26 P. vivax-infected patients in a malaria-endemic area of Colombia. The extent of nucleotide diversity (π) in these isolates (0.061 ± 0.004) was significantly lower (P ≤ 0.001) than that observed in Thai and Brazilian isolates; 0.083 ± 0.006 and 0.090 ± 0.006, respectively. We found two new alleles and several previously unidentified dimorphic substitutions and significant size polymorphism. The presence of highly conserved blocks in this fragment has important implications for the development of Pv200L as a subunit vaccine candidate.
裂殖子表面蛋白 1（MSP-1）是一种具有功能结构域的多态性疟原虫蛋白，参与寄生虫与红细胞的相互作用。间日疟原虫 MSP-1 有一个片段（Pv200L），已被鉴定为一种潜在的亚单位疫苗，因为它具有高度的免疫原性，并能诱导接种猴子对感染性寄生虫攻击产生部分保护作用。为了确定遗传多态性的程度及其对翻译蛋白的影响，我们对哥伦比亚疟疾流行地区 26 名间日疟原虫感染患者的分离株进行了 Pv200L 编码区的测序。这些分离株的核苷酸多样性（π）程度（0.061 ± 0.004）明显低于泰国和巴西分离株（分别为 0.083 ± 0.006 和 0.090 ± 0.006）（P ≤ 0.001）。我们发现了两个新的等位基因和几个以前未识别的二态替换以及显著的大小多态性。该片段中存在高度保守的块具有重要意义，这对于开发 Pv200L 作为亚单位疫苗候选物具有重要意义。
