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Abstract

Leishmania donovani is a protozoan parasite which leads to visceral leishmaniasis. Though Leishmaniasis is a dreadful disease the treatment options of it are limited and far from satisfactory. Eukaryotic initiation factor 5A (eIF5A) is a small, essential eukaryotic protein that contains a modified lysine residue, hypusine. The role of eIF5A in cell proliferation was documented in yeast. In HIV it was reported that it is involved in transport of viral mRNA from nucleus to cytoplasm in association with Rev HIV-1 protein. In humans, it induces apoptosis by acting as regulator of p53 and also is involved in translation elongation. In Leishmania, the function of eIF5A protein is not yet documented. This study was carried out to find out the function and localization of eIF5A in Leishmania donovani. To examine the subcellular localization of eIF5A protein, we cloned the gene in GFP vector and transfected in Leishmania donovani. Confirmation of the transfectants was done by fluorescent microscopy. Western-blot analysis using anti-GFP antibody showed expression of the fused eIF5A-GFP protein in total cell lysate and cytosolic fraction. However, this protein was absent in the nuclear fraction. This indicates that eIF5A has functions confined to the cytoplasm. To elucidate the function of eIF5A in parasite proliferation, the gene was cloned in an overexpression vector and transfected in promastigotes of Leishmania donovani. Interestingly, we found that there was decrease in growth of overexpressors when compared with the wild type and vector alone parasites. eIF5A overexpression may be leads to apoptosis as reported in other system.

Biography

S. Rashmi is PhD Scholar in the Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER), S.A.S Nagar, Mohali, India.