Parasite Biology

INFECTIOUS DISEASES / Parasitic Diseases

Research Interests

Malaria parasite, parasite biology, nucleic acid metabolism, translation, protein translocation, unwinding.

Description of Research

In order to understand the basic biology of the malaria parasite we are working on the enzymes (helicases) involved in nucleic acid metabolic pathways.  Helicases catalyze the unwinding of duplex nucleic acids in an ATP-dependent manner. We have reported that these are feasible novel drug targets for malaria control. We have reported the genome wide analysis of helicases from Plasmodium falciparum and their comparison with human host. This analysis revealed presence of some parasite specific helicases. Recently we have reported the purification and detailed characterization of a novel factor involved in mismatch repair (MMR) from P. falciparum. Our results indicate that this factor PfMLH is a homologue of MLH and it is an ATPase and it can incise covalently closed circular DNA. Using immunofluorescence assay we report that the peak expression of MLH in both 3D7 and Dd2 strains of P. falciparum is mainly in the schizont stages of the intraerythrocytic development, where DNA replication is active. We have also reported recently the biochemical characterization of recombinant PfRuvB3, a novel protein from P. falciparum. Using the truncated derivatives we show that Walker motif A is essential for the enzymatic activity of PfRuvB3. The endogenous P. falciparum RuvB3 contains the characteristic ATPase and some DNA helicase activities. The confocal microscopy analysis showed that this protein is mainly expressed during intraerythrocytic schizont stages of the parasite and is localized to the nuclear region. The co-localization studies with a nucleolar marker PfNop1 further suggested that in P. falciparum RuvB3 localizes into a discrete nuclear compartment. Using bioinformatics analysis we have shown the existence of the parasite specific UvrD helicase in the P. falciparum genome and this enzyme is not present in the human host. This helicase is a component of MMR complex. Further work on the characterization of this interesting enzyme and the other components of MMR complex is in progress.  

Recent Publications

Panchal, M., Rawat, K., Kumar, G., Kibria, K.M., Singh, S., Kalamuddin, M., Mohmmed, A., Malhotra, P., Tuteja R. 2014. Plasmodium falciparum signal recognition particle components and anti-parasitic effect of ivermectin in blocking nucleo-cytoplasmic shuttling of SRP. Cell Death and Disease Cell Death Dis 16, e994. doi: 10.1038/cddis.2013.521

Tuteja R. 2014. Insight into the biochemically characterized Plasmodium falciparum helicases. Encyclopedia of Malaria In press

Tuteja, R. 2014. Transport of mRNA through the nuclear pore in Plasmodium falciparum. Encyclopedia of Malaria In press

Ahmad, M., Tuteja, R. 2013. Plasmodium falciparum RuvB2 translocates in 5′-3′ direction, relocalizes during schizont stage and its enzymatic activities are up regulated by RuvB3 of the same complex. BBA – Proteins and Proteomics, 1834, 2795-811. doi: 10.1016/j.bbapap.2013 PubMed link

Ahmad, M., Afrin, F., Tuteja, R. 2013. Identification of R2TP complex of Leishmania donovani and Plasmodium falciparum using genome wide in-silico analysis. Communicative & Integrative Biology 6, 6, e26005 PubMed link

Tarique, M., Ahmad, M., Ansari, A., Tuteja, R. 2013. Plasmodium falciparum DOZI, an RNA helicase interacts with eIF4E. Gene 522, 46–59 PubMed link