The HIV Vaccine Translational Research (HVTR) Laboratory at the Translational Health Science and Technology Institute (THSTI) was established as a joint initiative between the Department of Biotechnology, THSTI, and IAVI in 2012. The HVTR laboratory studies the genetic and virological properties of circulating HIV strains in India, and complements the efforts of IAVI’s Neutralizing Antibody Center (NAC) to accelerate the development of broadly neutralizing antibodies (bnAbs) that would be affordable and applicable to low- and middle-income countries. It is part of the Indian government’s effort to create regional centers of scientific excellence to help address the burgeoning disease burden in the country.
The HVTR laboratory comprises an interdisciplinary group of scientists with varied educational backgrounds and experience in virology, protein design and engineering, as well as antibody discovery and characterization. The team’s unique capabilities and multifaceted experience enable it to drive research in some of the most promising areas of antibody discovery and vaccine development. The HVTR laboratory is playing a crucial role in spurring indigenous antibody discovery and preclinical development efforts, promoting industry collaboration on promising prevention products. It has also established strategic partnerships with leading academic and industry partners in India and across the globe.
The laboratory is funded by the Department of Biotechnology, Government of India; Department of Science and Technology, Government of India; Wellcome Trust-DBT India Alliance; Science & Engineering Research Board, Department of Science & Technology, Government of India; Research Council of Norway (GLOBVAC); and USAID via Microbicide and ADVANCE grants.
The HVTR laboratory is based at the THSTI NCR Biotech Science Cluster in Faridabad, Haryana, India. The principal investigators at the HVTR laboratory are:
- Jayanta Bhattacharya, Director, IAVI
- Suprit Deshpande, Research Scientist, THSTI
- Ranajoy Mullick, Manager – Immunobiology, Vaccine R&D Program, IAVI
- Nitin Hingankar, Project Scientist II, THSTI
- Jyoti Sutar, Senior Associate, IAVI
- Sohini Mukherjee, Senior Specialist, IAVI
Selected publications by HVTR investigators and their collaborators:
Evaluation of antiviral T cell responses and TSCM cells in volunteers enrolled in a phase I HIV-1 subtype C prophylactic vaccine trial in India. PLoS One 15(2): e0229461. 2020. (Open access)
Effect of diversity in gp41 membrane proximal external region of primary HIV-1 Indian subtype C sequences on interaction with broadly neutralizing antibodies 4E10 and 10E8. Virus Res. 273: 197763. 2019. (Subscription required)
The chaperone ERp29 is required for tunneling nanotube formation by stabilizing. MSec. J Biol. Chem. May 3;294(18):7177-7193. 2019. (Subscription required)
Characterization of the membrane-bound form of the chimeric, B/C recombinant HIV-1 Env, LT5.J4b12C. J Gen. Virol 99 (10): 1438-1443. 2018. (Open access)
Envelope proteins of two HIV-1 clades induced different epitope-specific antibody response. Vaccine. 2018 Mar 14;36(12):1627-1636. 2018. (Subscription required)
Cell surface ectodomain integrity of a subset of functional HIV-1 envelopes is dependent on a conserved hydrophilic domain containing region in their C-terminal tail. Retrovirology. 2018 Jul 20;15(1):50. 2018. (Open Access)
Characterization of a stable HIV-1 B/C recombinant, soluble and trimeric envelope glycoprotein (Env) highly resistant to CD4-induced conformational changes. Journal of Biological Chemistry. 292 (38): 15849-15858. 2017. (Open Access)
Stabilization of a soluble, native-like trimeric form of an efficiently cleaved Indian HIV-1 clade C envelope glycoprotein. J Biol Chem. 292(20):8236-8243. 2017. (Open Access)
Dual immunity concomitantly suppresses HIV-1 progression. Trends in Microbiol. 25 (5): 334-335. 2017. (Subscription required)
Association of mutations in V3/C3 domain with enhanced sensitivity of HIV-1 clade C primary envelopes to autologous broadly neutralizing plasma antibodies. Retrovirology 13: 41. 2016. (Open Access)
HIV-1 clade C escapes broadly neutralizing autologous antibodies with N332 glycan specificity by distinct mechanisms. Retrovirology 30;13(1):60. 2016. (Open Access)
Conformational Epitope-Specific Broadly Neutralizing Plasma Antibodies Obtained from an HIV-1 Clade C Infected Elite Neutralizer Mediate Autologous Virus Escape through Novel Mutations in V1 Loop. Journal of Virology 90 (7): 3446-3457. 2016. (Open Access)
Determinants in V2C2 region of HIV-1 clade C primary envelopes conferred altered neutralization susceptibilities to IgG1b12 and PG9 monoclonal antibodies in context dependent manner. Virology 462-463: 266–272. 2014. (Subscription required)