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Biography

Ramasare Prasad has completed his graduation in Chemistry and Doctorate in Molecular Biology from Jawaharlal Nehru University, New Delhi, India. He has then joined Professor Wilmont, Parasite Molecular Biology Unit at University of Georgia, USA, as a Post-doctoral Fellow. He has been working as an Assistant Professor and Associate Professor in Department of Biotechnology, Indian Institute of Technology Roorkee, India, since 1997 and as Professor since 2012 and was also the Head of Department. Presently he is the Professor and Leader of the of Molecular Biology and Proteomics Unit and has published 60 papers in reputed journals and has been serving as an Editorial Board Member of various journals of repute. He has nearly 30 years of research and teaching experience and executed several sponsored projects from DST, DBT, CSIR, UGC, etc.

Abstract

In recent years, there has been sudden increase in bacterial and fungal infections mainly due to infection caused by opportunistic and drug-resistant pathogens particularly in immunocompromised host and patients who has gone for transplant surgery. A therapeutic molecule with inherent properties of both antimicrobial as well as immunomodulatory activity will be more effective in controlling and treating the antimicrobial infections in general and in immunocompromised hosts in particular. Such novel molecules will have dual action; the fi rst is by killing the pathogen and secondly by boosting the immune system of the host. But fi nding such molecules is a diffi cult task. However, the observation that several antimicrobial proteins/peptides besides their antimicrobial action also found to have imunomodulatory eff ects provide strong basis that such proteins do exist in nature. Keeping this fact in mind, an attempt has been made in the present study to search for such a novel protein from Euphorbia hirta a well-known medicinal plant. A novel protein with antimicrobial and immunomodulatory activities has been isolated and purifi ed from Euphorbia hirta leaves. Characterization of purifi ed protein by diff erent biochemical methods (SDS PAGE and HPLC) and biophysical methods (N-terminal sequencing and mass spectrometric technique, revealed that it is 53kDa monomeric proteins. It found to have potent antimicrobial and immunomodulatory activities as confi rmed by various standard assays, TEM and SEM and in vitro and in vivo studies. Attempt was made to identify the protein using bioinformatics tools.