Cloning, sequence and expression of the lactate dehydrogenase gene from the human malaria parasite, Plasmodium vivax

Dilek Turgut-Balik, Ekrem Akbulut, Debbie K. Shoemark, Venhar Celik, Kathleen M. Moreton, Richard B. Sessions, J. John Holbrook, R. Leo Brady

Research output: Contribution to journalArticle (Academic Journal)

Abstract

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.
Original languageEnglish
Pages (from-to)1051-1055
Number of pages5
JournalBiotechnology Letters
Volume26
Issue number13
DOIs
Publication statusPublished - 1 Jul 2004

Keywords

  • anti-malarial
  • gene cloning
  • homology model
  • lactate dehydrogenase
  • Plasmodium vivax

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