Dr. Dinakar M. Salunke

    
 

Present Position
Scientist, National Institute of Immunology, New Delhi

Educational Qualifications
Ph D (1983) Indian Institute of Science, Bangalore

Primary Research Interests
Structural Biology of Immune Recognition, Molecular Mimicry and Allergy

Email: dinakar@nii.res.in

  

   

Awards/Honours
National Bioscience Award (1999); Shanti Swarup Bhatnagar Prize for Biological Sciences (2000); Ranbaxy Research Award for Basic Research in Medical Sciences (2002); Outstanding Scientific Achievements, National Institute of Immunology (2000 & 2001); Prof RC Shah Memorial Award (2000); Dr CR Krishnamurthi Oration Award (2004); Dr AT Varute Oration Award (2005); JC Bose National Fellowship Award (2007)

Fellowship / Membership of Professional Bodies
Fellow, National Academy of Sciences (India) (1995); Fellow, Indian Academy of Sciences (2001); Fellow, Indian National Science Academy (2004); Member, Molecular Immunology Forum (1996); Member, Guha Research Conference (1993)

Membership of Editorial Boards
International Archives of Bioscience (2001-to date); Resonance - A Science Education Journal (2006- to date); Proceedings of the Indian National Science Academy (2006-todate)

Highlights of the Most Significant Research Contributions

             Understanding the physiological processes of self-nonself discrimination in terms of physico-chemical principles of molecular interactions has been a major focus of our research. Our work on the pluripotency of primary immune response led to discovering new ways of antibody degeneracy and has impacted the evolving paradigm shift in immune recognition and generation of antibody repertoire [Immunity (2006) 24:359]. We have analyzed how immune system reacts when encountered with the antigens that keep changing shape and showed that the restricted paratope conformational repertoire on binding of an antigen to multiple independent antibodies may be relevant for minimizing possibility of self-reactive antibodies.  
             Molecular insights into the functional mimicry in the context of immune response were addressed using structural, immunological and thermodynamic approaches. We have demonstrated how paratope plasticity facilitates molecular mimicry of otherwise unrelated antigens. While our analyses of carbohydrate-peptide mimicry provided important conceptual leads towards design and development of new generation of vaccines, the analyses involving carbohydrate-porphyrin mimicry provided possible mechanistic understanding of the molecular pathology of porphyria. Structural issues pertaining to innate immunity and food allergies are also being addressed.
 

Selected Recent Publications

  1. Krishnan L, Sahni G, Kaur KJ, Salunke DM (2008) Role of antibody paratope conformational flexibility in the manifestation of molecular mimicry. Biophys J 94:1367

  2. Krishnan L, Lomash S, Raj BPJ, Kaur KJ and Salunke DM (2007) Paratope Plasticity in Diverse Modes Facilitates Molecular Mimicry in Antibody Response. J Immunol 178:7923

  3. Sethi DK, Agarwal A, Manivel V, Rao KVS and Salunke DM (2006) Differential epitope positioning within the germline antibody paratope enhances promiscuity in the primary immune response. Immunity 24:429    

  4. Goel M, Krishnan L, Kaur S, Kaur KJ and Salunke DM (2004) Plasticity within the antigen combining site may manifest as molecular mimicry in the humoral immune response J Immunol 173:7358

  5.  Nair DT, Kaur KJ, Singh K, Mukherjee P, Rajagopal D, George A, Bal V, Rath S, Rao KVS and Salunke DM (2003) Mimicry of native peptide antigens by the corresponding retro-inverso analogs is dependent on their intrinsic structure and interaction propensities J Immunol 170:1362

  6. Nair DT, Singh K, Siddiqui Z, Nayak BP, Rao KVS and Salunke DM (2002) Epitope Recognition by diverse antibodies suggests conformational convergence in an antibody response. J Immunol 168:2371

  7. Jain D, Nair DT, Swaminathan GJ, Abraham EG, Nagaraju J, and Salunke DM (2001) Structure of the induced antibacterial protein from tasar silkworm, Antheraea mylitta: Implications to molecular evolution. J Biol Chem 276:41377

  8. Goel M, Jain D, Kaur K, Kenoth R, Maiya BG, Swamy MJ and Salunke DM (2001) Functional equality in the absence of structural similarity: an added dimension to molecular mimicry. J Biol Chem 276: 39277

  9. Nair DT, Singh K, Sahu N, Rao KVS and Salunke DM (2000) Crystal structure of an antibody bound to an immunodominant peptide epitope: Novel features in peptide -antibody recognition. J Immunol 165:6949

  10. Jain D, Kaur KJ, Sundaravadivel B and Salunke DM (2000) Structural and functional consequences of peptide-carbohydrate mimicry: crystal structure of a carbohydrate-mimicking peptide bound to concanavalin A. J Biol Chem 275:16098