Tongqing Zhou, Ph.D.

Stadtman Investigator

Structural Virology and Vaccinology Section

NIAID/VRC

Building 40, Room 3509
40 Convent Drive
Bethesda, MD 20892

301-761-7068

tzhou@mail.nih.gov

Research Topics

Many viral pathogens evade immune recognition through mechanisms such as conformational changes in surface proteins, glycan masking of antigenic sites, and rapid sequence variation. The Structural Virology and Vaccinology Section applies structural biology and artificial intelligence (AI) to study these processes and their consequences for viral infectivity and immune evasion. Using cryogenic electron microscopy (cryo-EM) and X-ray crystallography, we determine high-resolution structures of viral antigens and their complexes with neutralizing antibodies to define key determinants of immune recognition and mechanisms of viral escape. In parallel, we investigate the conformational dynamics and antigenic landscapes of viral surface proteins, and study the structural and immunogenetic basis for how broadly neutralizing antibodies develop, mature, and achieve breadth against diverse viral pathogens.

These insights directly inform the design of vaccines and antibody therapeutics. With a primary focus on retroviruses, including HIV-1 and HTLV-1 (Human T-lymphotropic virus 1), we apply structure- and AI-based approaches to engineer and optimize viral antigens capable of eliciting broadly neutralizing immune responses, and to improve antibody potency and breadth. Our work integrates structural, virological, and immunological data to advance next-generation vaccines and immunotherapies against some of the most challenging infectious diseases facing global health.

Biography

Dr. Tongqing Zhou is an Earl Stadtman Tenure-Track Investigator and Chief of the Structural Virology and Vaccinology Section at the Vaccine Research Center, NIAID. He received his B.S. in Biochemistry from Wuhan University, an M.S. in Electronic and Computer-Controlled Systems from Wayne State University School of Engineering, and a Ph.D. in Cell Biology from the Chinese Academy of Sciences. He completed postdoctoral training in structural biology at Wayne State University School of Medicine, where he developed expertise in determining high-resolution structures of biological macromolecules. In 2001, Dr. Zhou joined the Dale and Betty Bumpers Vaccine Research Center, where he pioneered structure-based design of viral immunogens and advanced the application of structural biology and artificial intelligence to study viral-host interactions, immune evasion, and antibody neutralization. Dr. Zhou's current group at NIAID focuses on structure- and AI-based immunogen design for retroviruses, with the goal of developing next-generation vaccines and antibody therapeutics for infectious diseases. His contributions have earned him multiple NIH Director's Awards and NIAID Merit Awards, and he has been recognized as a Clarivate Analytics Highly Cited Researcher in Microbiology every year since 2014.

Selected Publications

  1. Zhou T, Wang L, Misasi J, Pegu A, Zhang Y, Harris DR, Olia AS, Talana CA, Yang ES, Chen M, Choe M, Shi W, Teng IT, Creanga A, Jenkins C, Leung K, Liu T, Stancofski ED, Stephens T, Zhang B, Tsybovsky Y, Graham BS, Mascola JR, Sullivan NJ, Kwong PD. Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529. Science. 2022;376(6591):eabn8897.
  2. Chen X, Zhou T, Schmidt SD, Duan H, Cheng C, Chuang GY, Gu Y, Louder MK, Lin BC, Shen CH, Sheng Z, Zheng MX, Doria-Rose NA, Joyce MG, Shapiro L, Tian M, Alt FW, Kwong PD, Mascola JR. Vaccination induces maturation in a mouse model of diverse unmutated VRC01-class precursors to HIV-neutralizing antibodies with >50% breadth. Immunity. 2021;54(2):324-339.e8.
  3. Zhou T, Tsybovsky Y, Gorman J, Rapp M, Cerutti G, Chuang GY, Katsamba PS, Sampson JM, Schön A, Bimela J, Boyington JC, Nazzari A, Olia AS, Shi W, Sastry M, Stephens T, Stuckey J, Teng IT, Wang P, Wang S, Zhang B, Friesner RA, Ho DD, Mascola JR, Shapiro L, Kwong PD. Cryo-EM Structures of SARS-CoV-2 Spike without and with ACE2 Reveal a pH-Dependent Switch to Mediate Endosomal Positioning of Receptor-Binding Domains. Cell Host Microbe. 2020;28(6):867-879.e5.
  4. Abu-Shmais AA, Freeman G, Creanga A, Vukovich MJ, Malla T, Mantus GE, Shimberg GD, Gillespie RA, Guerra Canedo V, Dadonaite B, Rodgers MD, Chopde AJ, Bardwil-Lugones E, Bylund T, Henry AR, Roberts-Torres J, Johnston TS, Smith S, Yang ES, Cheng C, Walker EL, Ravichandran M, Gordon IJ, Dittakavi TS, Reed DS, Pierson TC, Dropulic L, Bloom JD, Tsybovsky Y, Boritz EA, Douek DC, Zhou T, Kanekiyo M, Andrews SF. Cross-neutralizing and potent human monoclonal antibodies against historical and emerging H5Nx influenza viruses. Nat Microbiol. 2025;10(11):2903-2918.
  5. Madel Alfajaro M, Keeler EL, Li N, Catanzaro NJ, Teng IT, Zhao Z, Grunst MW, Yount B, Schäfer A, Wang D, Kim AS, Synowiec A, Peña-Hernández MA, Zepeda S, Arinola R, Kaur R, Menasche BL, Wei J, Russell GA, Huck J, Song J, Ring A, Iwasaki A, Jangra RK, Lee S, Martinez DR, Mothes W, Uchil PD, Doench JG, Spaulding AB, Baric RS, Serebryannyy L, Tsybovsky Y, Zhou T, Douek DC, Wilen CB. HKU5 bat merbecoviruses engage bat and mink ACE2 as entry receptors. Nat Commun. 2025;16(1):6822.

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This page was last updated on Wednesday, June 10, 2026