H. S. Savithri

Professor
Department of Biochemistry
Research Areas: 
Structure and function of viral proteins, PLP-dependent enzymes
Research Highlights: 

Professor Savithri's lab works on the architecture, genome organisation and expression of plant viral proteins. In particular, viruses such as Physalis mottle virus (PhMV), Sesbania mosaic virus (SeMV), Pepper vein banding virus (PVBV), Tomato leaf curl Bangalore virus (ToLCBV), Cotton leaf curl virus (CLCuV) and Peanut bud necrosis virus (PBNV) are being investigated. The complete genomic sequences of PhMV, SeMV, PVBV, CLCuV and ToLCV have been determined and PhMV, SeMV and PVBV are shown to be new members of their respective genera. Using these viruses, research in this group also includes using virus-like particles (VLPs) to identify pathways of virus assembly and to develop them as biodegradable nano-carriers for biomedical application. Further studies on the in vivo functions of the SeMV, PVBV and PBNV encoded proteins and their intermediates with special emphasis on polyprotein processing are in progress. In this context, her laboratory is currently focussed on projects that involve: (1) The determination of genomic sequences of new gemini and poty viruses and their strains from India to establish the genetic variability and diversity in the viral genomic sequences. (2) Structure-function relationship of structural and non-structural proteins of viruses through protein engineering. (3) Identification of host factors interacting with viral proteins/genomes and their functional characterization. (4) Protein engineering to evolve enzymes with altered substrate and reaction specificities. Prof. Saithri's research group also works on Pyridoxal phosphate (PLP) dependent enzymes which are invaiable multimeric and exhibit unique features of substrate and reaction specificity. Structure-function relationship of Serine hydroxymethyltransferase (SHMT) and Di amino propionate ammonia lyase(DAP lyase) are being investigated to establish the role of specific amino acid residues in substrate and reaction specificities, cofactor binding ,catalysis and in the maintenance of oligomeric structure.

Phone: 
91-80-22932310