Structural Immunology


Research Interests

Structural biology of immune recognition, molecular mimicry and allergy

Description of Research

Understanding the physiological processes of self-nonself discrimination in terms of physicochemical 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. We have analyzed how the 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 selfreactive 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.

Recent Publications

Kaur, H., Salunke, D.M. 2015. Antibody promiscuity: Understanding the paradigm shift in antigen recognition.IUBMB Life 67, 498 PubMed link

Khan, T., Salunke, D.M. 2014. Adjustable locks and flexible keys: plasticity of epitope-paratope interactions in germline antibodies. J Immunol 192, 5398 PubMed link

Bhowmick, A., Salunke, D.M. 2013. Limited conformational flexibility in the paratope may be responsible for degenerate specificity of HIV epitope recognition. IntImmunol 25, 77 PubMed link

Lomash, S., Nagpal, S., Salunke, D.M. 2010. An antibody as surrogate receptor reveals determinants of activity of an innate immune peptide antibiotic. J BiolChem 285, 35750 PubMed link

Gaur, V., Qureshi, I.A., Singh, A., Chanana, V., Salunke, D.M. 2010. Crystal structure and functional insights of hemopexin fold protein from grass pea. Plant Physiol 152,1842 PubMed link