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用PCR扩增间日疟原虫海南分离株基因组DNA中乳酸脱氢酶(LDH)全长基因,命名为PvLDH/HN(GenBank登录号为FJ527750)。生物信息学分析表明,PvLDH/HN全长951bp,编码316个氨基酸残基,与间日疟原虫SalvadorI株、Belem株LDH等分离株核苷酸序列同源性均为99.89%(950/951),氨基酸序列同源性均为100%(316/316)。拓扑结构分析显示,该蛋白具有2个α螺旋跨膜区域,可能是膜蛋白。三级结构模型显示主要抗原表位82～95aa位于蛋白表面,构成特异性底物结合环,提示该位点是可能的药物作用靶点及免疫诊断抗原表位。
The full length gene of lactate dehydrogenase (LDH) in the genomic DNA of Plasmodium vivax in Hainan was amplified by PCR and named PvLDH / HN (GenBank accession number FJ527750). Bioinformatics analysis showed that the full length of PvLDH / HN was 951bp and encoded 316 amino acid residues, which shared 99.89% (950/951) homology with the isolates of SalvadorI and Belem of Plasmodium vivax, , The amino acid sequence homology is 100% (316/316). Topological analysis shows that the protein has two α-helical transmembrane regions, which may be membrane proteins. The tertiary structure model shows that the major epitopes 82-95aa are located on the protein surface and constitute a specific substrate binding loop, suggesting that this site is a potential drug target and an immunodiagnostic epitope.