
Ashish Kumar
Assistant Professor
ashish.kumar@mahindrauniversity.edu.in
Dr. Ashish Kumar did his Ph.D. at the National Institute of Immunology, New Delhi, India, in the laboratory of Dr. Dinakar M. Salunke, determining the structural function role of medicinally important plants. Later, he moved to the National Institute of Health, Bethesda, US, for his postdoctoral training under the direction of Dr. Joseph Marcotrigiano, and he determined the first structure of the hepatitis C virus surface glycoprotein E2 with its cognate human receptor, CD81, as a complex (Nature Journal, 2021). Dr. Ashish Kumar published numerous papers in the area of structural virology. From 2022, he became a research associate scientist (RF-FTE). He received the prestigious Salzman Award for the year 2022 from the Foundation of the National Institute of Health and, most recently, was a finalist in the prestigious trans-NIH Earl Stadtman Early Independent Faculty Career Award.
Education
- Ph.D. in Life Science (2008-2014) National Institute of Immunology, Jawaharlal Nehru University, New Delhi, India
- MS in Biotechnology (2006-2008) University of Jammu, Jammu & Kashmir, India
- B.Sc in Life Sciences (Zoology, Botany and Chemistry) (2003-2005) University of Lucknow, Uttar Pradesh, India
Experience
- Research Associate Scientist (RF-FTE) (February 2022- present) National Institute of Allergy and Infectious Diseases (NIAID), National Institute of Health (NIH), Bethesda, Maryland 20892 US
- Visiting Post-Doctoral Fellow (February 2018- January 2022) National Institute of Allergy and Infectious Diseases (NIAID), National Institute of Health (NIH), Bethesda, Maryland 20892 US
- Post-Doctoral Research Fellow (December 2016- January 2018) The Pennsylvania State University, Eberly College of Science, University Park, PA-16802
- Post-Doctoral Research Fellow and Senior Technology Office (December 2014- December 2016) National Institute of Immunology, Jawaharlal Nehru University, New Delhi, India, and Regional Centre for Biotechnology (RCB), Faridabad, Haryana (NCR Delhi), India
Publications
- Sara M Maloney, Teressa M Shaw, Kylie M Nennig, Malorie S Larsen, Aadit Shah, Ashish Kumar, Joseph Marcotrigiano, Joe Grove, Eric J Snijder, Robert N Kirchdoerfer, Adam L Bailey. CD81 is a receptor for equine arteritis virus (family: Arteriviridae). mBio 16:e00623-25. https://doi.org/10.1128/mbio.00623-25
- Mart Reimund, Altaira D. Dearborn, Giorgio Graziano, Haotian Lei, Anthony M. Ciancone, Francis J. O'Reilly, Ashish Kumar, Ronald Holewinski, Edward B. Neufeld, Alan T. Remaley†, Joseph Marcotrigiano†. Structure of apolipoprotein b100 bound to low-density lipoprotein receptor. Nature (August 2024, In press)
- Wei Bu, Ashish Kumar, Nathan L Board, JungHyun Kim, Kennichi Dowdell, Shu Zhang, Yona Lei, Anna Hostal, Tammy Krogmann, Yanmei Wang, Stefania Pittaluga, Joseph Marcotrigiano, Jeffrey I Cohen. Epstein-Barr virus gp42 antibodies reveal sites of vulnerability for receptor binding and fusion to B cells. Immunity, 57(3), 559–573.e6 (2024). https://doi.org/10.1016/j.immuni.2024.02.008
- Jennifer Casiano Matos, Kaneemozhe Harichandran, Jingrong Tang, Denis O Sviri-dov, Giacomo Sidoti Migliore, Motoshi Suzuki, Lisa R Olano, Alvaro Hobbs, Ashish Kumar, Myeisha U Paskel, Mattia Bonsignori, Altaira D Dearborn, Alan T Remaley, Joseph Marcotrigiano. Hepatitis C virus E1 recruits high-density lipoprotein to support infectivity and evade antibody recognition. Journal of Virology 98(1):e0084923 (2024). http://doi:10.1128/jvi.00849-23
- Ashish Kumar, Tiana Rohe, Elizabeth J. Elrod, Abdul G. Khan, Altaira D. Dearborn, Ryan Kissinger, Arash Grakoui, Joseph Marcotrigiano. "Regions of hepatitis C virus E2 required for membrane association. Nature Communications 14, 433 (2023). https://doi.org/10.1038/s41467-023-36183-y
- Ashish Kumar, Reafa A. Hossain, Samantha A. Yost, Wei Bu, Yuanyuan Wang, Altaira D. Dearborn, Arash Grakoui, Jeffrey I. Cohen, and Joseph Marcotrigiano. "Structural insights into hepatitis C virus receptor binding and entry." Nature 598, 521–525 (2021). https://doi.org/10.1038/s41586-021-03913-5
- Abha Jain, Amit Kumar, Meha Shikhi, Ashish Kumar, Deepak. T. Nair, and Dinakar M. Salunke. "The structure of MP-4 from Mucuna pruriens at 2.22 Å resolution." Acta Crystallographica Section F: Structural Biology Communications 76, no. 2 (2020): 47-57. https://doi.org/10.1107/S2053230X20000199
- Sarita Chandan Sharma, Ashish Kumar, Sharad Vashisht, and Dinakar M. Salunke. "High resolution structural and functional analysis of a hemopexin motif protein from Dolichos." Scientific reports 9, no. 1 (2019): 1-13. https://doi.org/10.1038/s41598-019-56257-6
- Ashish Kumar, Harmeet Kaur, Abha Jain, Deepak T. Nair, and Dinakar M. Salunke. "Docking, thermodynamics and molecular dynamics (MD) studies of a non-canonical protease inhibitor, MP-4, from Mucuna pruriens." Scientific reports 8, no. 1 (2018): 1-12. https://doi.org/10.1038/s41598-017-18733-9
- Pidathala RV Shabareesh, Ashish Kumar, Dinakar M. Salunke, and Kanwal J. Kaur. "Structural and functional studies of differentially O‐glycosylated analogs of a thrombin inhibitory peptide–variegin." Journal of Peptide Science 23, no. 12 (2017): 880-888. https://doi.org/10.1002/psc.3052
- Ashish Kumar, Chitra Gupta, Deepak T. Nair, and Dinakar M. Salunke. "MP-4 contributes to snake venom neutralization by Mucuna pruriens seeds through an indirect antibody-mediated mechanism." Journal of Biological Chemistry 291, no. 21 (2016): 11373-11384. https://doi.org/10.1074/jbc.M115.699173
- Abha Jain, Ashish Kumar, and Dinakar M. Salunke. "Crystal structure of the vicilin from Solanum melongena reveals existence of different anionic ligands in structurally similar pockets." Scientific reports 6, no. 1 (2016): 1-11. https://doi.org/10.1038/srep23600
- Sharad Vashisht, Ashish Kumar, Kanwal J. Kaur, and Dinakar M. Salunke. "Antibodies can exploit molecular crowding to bind new antigens at noncanonical paratope positions." ChemistrySelect 1, no. 19 (2016): 6287-6292. https://doi.org/10.1002/slct.201600945
The goal of my research is to perform translational research based on knowledge being acquired through in vitro and in vivo and structural information on RNA viruses, particularly newly emerging and mutating viruses. One of the RNA virus families is flavivirus; it is an old family; however, many members still need attention to develop effective therapeutics. Flaviviruses have been identified as the causative agents of a number of human diseases. It consists of more than 70 small, positive-sense, single-stranded RNA viruses transmitted by arthropods, primarily ticks and mosquitoes. Since the global incidence of flavivirus infections is increasing due to climate change, globalization, and urbanization, there is an increased emphasis on understanding the molecular mechanisms underlying flavivirus infections and pathogenesis. Vaccines continue to be the most effective method for preventing viral infections. However, existing flavivirus vaccines can induce severe adverse effects and have certain limitations. Therefore, systematic and novel approaches to vaccine and drug discovery are required in the field of flavivirus. Mostly flaviviruses enter host cells via receptor-mediated endocytosis; however, flaviviruses utilize diverse receptors and attachment factors in various tissues of their natural hosts. Understanding the molecular mechanism by which flaviviruses use host cell receptors and factors for entry could facilitate the development of novel therapeutics. And, understanding the pathways that are being utilized by these viruses for the pathogenesis could be potential checkpoints for the development of an effective vaccine or drug. We will utilize cutting age techniques such as Cryo-electron microscopy (Cryo-EM), X-ray crystallography, and other biophysical techniques as a basic tool to address the questions in RNA virology.
Major Areas of Research-
- Assembly and entry of RNA viruses
- Understanding the molecular mechanisms of membrane fusion used by RNA viruses
- Humoral immunity to RNA viruses
The development of therapeutics based on structural knowledge using either viral proteins or the whole virus









