Turgut-Balik Dilek, Akbulut Ekrem, Shoemark Debbie K, Celik Venhar, Moreton Kathleen M, Sessions Richard B, Holbrook J John, Brady R Leo
University of Firat, Faculty of Arts and Sciences, Department of Biology, 23169 Elazig, Turkey.
Biotechnol Lett. 2004 Jul;26(13):1051-5. doi: 10.1023/B:BILE.0000032958.78158.10.
Increased drug resistance to anti-malarials highlights the need for the development of new therapeutics for the treatment of malaria. To this end, the lactate dehydrogenase (LDH) gene was cloned and sequenced from genomic DNA of Plasmodium vivax ( PvLDH) Belem strain. The 316 amino acid protein-coding region of the PvLDH gene was inserted into the prokaryotic expression vector pKK223-3 and a 34 kDa protein with LDH activity was expressed in E. coli. Structural differences between human LDHs and PfLDH make the latter an attractive target for inhibitors leading to novel anti-malarial drugs. The sequence similarity between PvLDH and PfLDH (90% residue identity and no insertions or deletions) indicate that the same approach could be applied to Plasmodium vivax, the most common human malaria parasite in the world.
对抗疟疾药物的耐药性增加凸显了开发治疗疟疾新疗法的必要性。为此，从间日疟原虫（PvLDH）贝伦株的基因组DNA中克隆并测序了乳酸脱氢酶（LDH）基因。将PvLDH基因的316个氨基酸的蛋白质编码区域插入原核表达载体pKK223-3中，并在大肠杆菌中表达出具有LDH活性的34 kDa蛋白质。人类LDH与PfLDH之间的结构差异使后者成为新型抗疟疾药物抑制剂的有吸引力的靶点。PvLDH与PfLDH之间的序列相似性（90%的残基同一性且无插入或缺失）表明，相同的方法可应用于间日疟原虫，这是世界上最常见的人类疟原虫。
