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

Biotechnology Letters
Dilek Turgut-BalikR Leo Brady

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.

Citations

May 30, 2009·Transactions of the Royal Society of Tropical Medicine and Hygiene·M MeenaS P Kalantri
Jun 12, 2012·Protein Expression and Purification·Vandana SinghNuzhat A Kaushal
Jan 23, 2010·Peptides·Ramona HurdayalJ P Dean Goldring
Sep 21, 2013·Journal of Medical Microbiology·Joel C Mouatcho, J P Dean Goldring
Jul 8, 2020·Proceedings of the National Academy of Sciences of the United States of America·Yee-Wai CheungJulian A Tanner
Dec 3, 2020·Nature Communications·Antonio MinopoliRaffaele Velotta

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