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Niti Kumar, Ph.D.

Principal Scientist, Division Of Molecular Microbiology and Immunology

Stress biology lab

Our lab is interested in the quality control processes adopted by a cell during stress and infection. We are using different biological systems to understand critical pathway(s) involved in genome and proteome maintenance that help in restoration of cellular homeostasis.

Understanding the protein folding and degradation machinery of human host and malaria parasite

Dysregulation in protein folding or degradation machinery results in accumulation of misfolded protein in different cellular organelles which eventually manifests into cardiovascular and neurodegenerative, metabolic diseases and dysregulation in protein trafficking. Further, host cellular protein folding capacity gets affected during microbe infection. Though, some components of protein folding and degradation machinery are conserved, while few other are highly diverged. We are looking into the components of protein folding and degradation machinery in the host-parasite context. We are specifically interested to understand how human malaria parasite is able to keep its aggregation-prone proteome in soluble and functional state. We are specifically looking at the role of heat-shock proteins and E3 ligases in Plasmodium falciparum and how they provide survival advantage to the parasite.

In addition, we are also using mammalian cells to assess the protein folding capacity of different cellular organelles and their response to different stress conditions. We are also screening for molecules which can increase the protein folding capacity of cellular organelles and rescue the cell from protein conformational diseases.

Probing into telomere dynamics in human malaria parasite

The replicative capacity of human malaria parasite is maintained by its unsually large telomerase. Plasmodial telomerase is 2.5 times bigger than the human telomerase and its RNA component is 3 times bigger than the human counterpart. Besides, the large size of parasite telomerase, its individual domains (TEN, TRBD, RT and CTE) exhibits remarkable sequence divergence from the human ortholog. In addition to this, the proteins binding to telomeric/sub-telomeric regions are also highly diverged and many of yeast and human orthologues are absent in parasite. We have adopted two-pronged approach wherein (i) we are trying pharmacological targeting of non-canonical nucleic acid structures in telomeres of malaria parasite and (ii) exploring the role of telomere binding proteins.

Investigating the extra-ribosomal functions of ribosomal proteins during stress and infection.

Ribosomal proteins (RPs) are the important component of the protein translation machinery. Emerging observations suggest that apart from their primary role in protein synthesis, ribosomal proteins play important extra-ribosomal roles in maintenance of cellular homeostasis. They have critical roles in translational fidelity, cell signaling, growth and development. However, the mechanistic insights into these processes are not well understood. Specific goals of this project are to understand the (i) cellular quality control mechanisms adopted by ribosomal proteins during stress, and (ii) role of ribosomal proteins in host-pathogen interaction.

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