Ogu Salim, Nurhainis and Ahmad Fuad, Fazia Adyani (2016) Cloning and characterisation of Lactate Dehydrogenase Gene from Plasmodium knowlesi in bacterial system. In: Borneo Biotech Symposium, 7- 8 December 2016, Kota Kinabalu, Sabah. (Unpublished)
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Abstract
Glycolysis is essential for Plasmodium survival during its intra-erythrocytic stage in the human host. As a consequence, enzymes in the glycolytic pathway have been proposed as ideal therapeutic targets for malaria pharmaceuticals. Specifically, lactate dehydrogenase, which is the final enzyme in glycolysis, has been validated as a good drug target. We have cloned and characterised recombinant lactate dehydrogenase from Plasmodium knowlesi in a bacterial system. Synthetic P. knowlesi lactate dehydrogenase (Pk-LDH) gene was obtained from GenScript®. Pk-LDH gene was successfully amplified from the pUC57 vector and a PCR product with the size of 951bp was cloned into pEASY-Blunt E1 expression vector. The ligated product was subsequently transformed into Trans1-T1 Phage Resistant Chemically Competent Cell. A sequence alignment analysis, which was conducted to compare the sequence similarity of Pk-LDH to LDH from other human malaria parasites revealed open reading frame of 316 amino acids of Pk-LDH and showed 97.8% homology to P. vivax LDH and 90% homology to P. malariae, P. falciparum, and P. ovale LDHs, respectively. The purified recombinant Pk-LDH will later be utilised for inhibition studies in future antimalarial drug design and discovery research, specifically for P. knowlesi.
Item Type: | Conference or Workshop Item (Other) |
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Subjects: | R Medicine > RA Public aspects of medicine |
Kulliyyahs/Centres/Divisions/Institutes (Can select more than one option. Press CONTROL button): | Kulliyyah of Engineering Kulliyyah of Engineering > Department of Biotechnology Engineering |
Depositing User: | Dr Fazia Adyani Ahmad Fuad |
Date Deposited: | 14 Mar 2022 15:41 |
Last Modified: | 17 Mar 2022 16:45 |
URI: | http://irep.iium.edu.my/id/eprint/97180 |
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