Overview
Dr. Kwong received his PhD from Columbia University in 1995 and continued as a postdoc with Wayne A. Hendrickson until 2000, when left Columbia to found and lead the Structural Biology Section at the Vaccine Research Center (VRC) at the National Institutes of Health. In 2023, he was recruited back to Columbia University to be Co-Director of the Aaron Diamond AIDS Research Center. Since 2016, Kwong has also been an Adjunct Professor in the Department of Biochemistry and Molecular Biophysics at Columbia University. Kwong is internationally recognized for his work defining structural aspects of the HIV-1 envelope glycoproteins and their interactions with antibodies. His awards include the Presidential Early Career Award for Scientists and Engineers (2003), the Norman P. Salzman Award in Virology (2012), election to the American Academy of Microbiology (2014), and multiple NIAID Merit and NIH Director’s Awards. For the last several years, he has focused on applying the atomic-level tools of structural biology to the development of effective vaccines against HIV-1 and other viral pathogens. At Columbia University, his efforts initially focused on Antibodyomics, the informatics of antibody recognition, development, and improvement. Since formally returning to Columbia University in 2023, he has been working on structural vaccinology.
Academic Appointments
- Professor of Medical Sciences (in Medicine)
Administrative Titles
- Co-director, Aaron Diamond AIDS Research Center
Languages
- English
Gender
- Male
Credentials & Experience
Education & Training
- BA, 1985 Chemistry & Physics, University of Chicago
- MS, 1985 Biochemistry & Molecular Biology, University of Chicago
- PhM, 1989 Columbia University
- PhD, 1995 Columbia University
Honors & Awards
- 1987 National Science Foundation Graduate Fellowship
- 1998 Burroughs Wellcome Fund Career Award in Biomedical Sciences
- 2003 Presidential Early Career Award for Scientists and Engineers
- 2004 Fellow of the American Society of Microbiology
- 2007 Director’s Award, National Institutes of Health
- 2010 NIAID Merit Award
- 2011 NIAID Merit Award
- 2012 SER-CAT Outstanding Science Award
- 2012 Norman P. Salzman Award in Virology
- 2012 NIAID Merit Award
- 2013 Director’s Award, National Institutes of Health
- 2013 NIAID Merit Award
- 2014 Fellow of the American Academy of Microbiology
- 2014 NIAID Merit Award
- 2018 NIAID Merit Award
- 2019 NIAID Merit Award
- 2020 NIAID Merit Award
- 2022 Director’s Award, National Institutes of Health
Research
Kwong solved the structure of the HIV-1 gp120 envelope glycoprotein in complex with CD4 receptor and a neutralizing antibody (featured on the covers of both Nature and Science in June 1998), while a postdoc in Wayne Hendrickson’s lab at Columbia University, then founded and lead the Structural Biology Section of the Vaccine Research Center, National Institute of Allergy and Infectious Disease, NIH, from 2000-2023, before returning to the Columbia University in December 2023. While at the NIH, Kwong showed conformational masking to shield HIV-1 envelope from immune recognition (2002, Nature), and showed that conformational stabilization could induce the elicitation of broad CD4-induced antibodies. Further, such conformational stabilization proved crucial in the elicitation of high titer responses against respiratory syncytial virus (RSV), with the DS-Cav1 immunogen Kwong designed (2013, Science) providing the basis for the approved GSK vaccine AREXVY. Kwong defined domain structures for almost all of HIV-1 gp120 envelope (1998, Nature; 2005, Science; 2009, PNAS; 2011, Nature), the prefusion-closed structure of HIV-1 envelope trimer (2014, Nature), as well as the fully glycosylated envelope trimer from three clades (2016, Cell). Kwong has also used an antibody-guided vaccine approach to elicit broadly neutralizing antibodies against HIV, particularly at the fusion peptide site of vulnerability (2018, Nature Med; 2019, Cell). While vaccine-elicited antibodies can be potent and broadly neutralizing, they tend to be of low titer; recent experiments with SHIV demonstrate the boosting these titers to achieve serum neutralization of over 50% breadth on a 208-strain panel at a 1:100 ID50 (2024, Cell). Kwong has published over 400 peer-reviewed papers, including more than 50 in Nature, Science and Cell. He has mentored over 25 postdoctoral fellows, of which more than a dozen have gone on to head independent research groups.
Selected Publications
- Kwong PD, Wyatt R, Robinson J, Sweet RW, Sodroski J and Hendrickson WA. (1998). Structure of an HIV gp120 Envelope Glycoprotein in Complex with the CD4 Receptor and a Neutralizing Human Antibody. Nature 393, 648-659.
(First atomic-level structure of HIV-1 core gp120 glycoprotein) - Kwong PD, Doyle ML, Casper DJ, Cicala C, Leavitt SA, Majeed S, Steenbeke TD, Venturi M, Chaiken I, Fung M, Katinger H, Parren PWI, Robinson J, Van Ryk D, Wang L, Burton DR, Freire E, Wyatt R, Sodroski J, Hendrickson WA and Arthos J. (2002). HIV-1 Evades Antibody-mediated Neutralization through Conformational Masking of Receptor-binding Sites. Nature 420, 678-682.
(Defined viral evasion mechanism of conformational masking) - Wei X, Decker JM, Wang S, Hui H, Kappes JC, Wu X, Salazar-Gonzalez JF, Salazar MG, Kilby JM, Saag MS, Komarova NL, Nowak MA, Hahn BH, Kwong PD and Shaw GM. (2003). Antibody Neutralization and Escape by HIV-1. Nature 422, 307-312.
(Defined viral evasion mechanism of glycan shielding) - Zhou T, Ling X, Dey B, Hessell A, Van Ryk D, Xiang SH, Yang X, Zhang MY, Zwick M, Arthos J, Burton D, Dimitrov D, Sodroski J, Wyatt R, Nabel G, Kwong PD. (2007) Structural definition of a conserved neutralization epitope on HIV-1 gp120. Nature 445, 732-736.
(Revealed how broadly neutralizing antibody recognition overlaps with receptor binding site.) - Zhou T, Georgiev I, Wu X, Yang ZY, Dai K, Finzi A, Kwon YD, Scheid J, Shi W, Xu L, Yang Y, Zhu J, Nussenzweig MC, Sodroski J, Shapiro L, Nabel GJ, Mascola JR, Kwong PD. (2010) Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 329, 811-817.
(Revealed how heavy chain mimicry of the CD4 receptor enables neutralization of 90% of HIIV-1) - McLellan JS, Chen M, Joyce MG, Sastry M, Stewart-Jones GBE, Yang Y, Zhang B, Chen L, Srivatsan S, Zheng A, Zhou T, Graepel KW, Kumar A, Moin S, Boyington JC, Chuang GY, Soto C, Baxa U, Bakker AQ, Spits H, Beaumont T, Zheng Z, Xia N, Ko SY, Todd JP, Rao S, Graham BS, Kwong PD (2013) Structure-based design of a fusion glycoprotein vaccine for respiratory syncytial virus. Science 342, 592-598.
(“First” structure-based designed vaccine selected as “runner up” of the year by Science in 2013.) - Pancera M, Zhou T, Druz A, Georgiev IS, Soto C, Gorman J, Huang J, Acharya P, Chuang GY, Ofek G, Stewart-Jones GBE, Stuckey J, Bailer RT, Joyce MG, Louder MK, Tumba N, Yang Y, Zhang B, Cohen MS, Haynes BF, Mascola JR, Morris L, Munro JB, Blanchard SC, Mothes W, Connors M, Kwong PD (2014) Structure and immune recognition of trimeric prefusion HIV-1 Env. Nature 514, 455-461.
(First atomic-level structure of HIV-1 envelope trimer – defining both gp120 and gp41) - Stewart-Jones GB, Soto C, Lemmin T, Chuang GY, Druz A, Kong R, Thomas PV, Wagh K, Zhou T, Behrens AJ, Bylund T, Choi CW, Davison JR, Georgiev IS, Joyce MG, Kwon YD, Pancera M, Taft J, Yang Y, Zhang B, Shivatare SS, Shivatare VS, Lee CD, Wu CY, Bewley CA, Burton DR, Koff WC, Connors M, Crispin M, Baxa U, Korber BT, Wong CH, Mascola JR, Kwong PD. (2016) Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G. Cell 165, 813-826.
(Frist atomic-level structure of the HIV-1 glycan shield) - Xu K, Acharya P, Kong R, Cheng C, Chuang GY, Liu K, Louder MK, O'Dell S, Rawi R, Sastry M, Shen CH, Zhang B, Zhou T, Asokan M, Bailer RT, Chambers M, Chen X, Choi CW, Dandey VP, Doria-Rose NA, Druz A, Eng ET, Farney SK, Foulds KE, Geng H, Georgiev IS, Gorman J, Hill KR, Jafari AJ, Kwon YD, Lai YT, Lemmin T, McKee K, Ohr TY, Ou L, Peng D, Rowshan AP, Sheng Z, Todd JP, Tsybovsky Y, Viox EG, Wang Y, Wei H, Yang Y, Zhou AF, Chen R, Yang L, Scorpio DG, McDermott AB, Shapiro L, Carragher B, Potter CS, Mascola JR, Kwong PD. (2018) Epitope-based vaccine design yields fusion peptide-directed antibodies that neutralize diverse strains of HIV-1. Nat Med. 24, 857-867.
(Demonstrates in mice, guinea pigs. and NHP the ability of fusion-peptide priming coupled to Env-trimer boosting to elicit cross-clade neutralizing responses against a target site of vulnerability) - Kong R, Duan H, Sheng Z, Xu K, Acharya P, Chen X, Cheng C, Dingens AS, Gorman J, Sastry M, Shen CH, Zhang B, Zhou T, Chuang GY, Chao CW, Gu Y, Jafari AJ, Louder MK, O'Dell S, Rowshan AP, Viox EG, Wang Y, Choi CW, Corcoran MM, Corrigan AR, Dandey VP, Eng ET, Geng H, Foulds KE, Guo Y, Kwon YD, Lin B, Liu K, Mason RD, Nason MC, Ohr TY, Ou L, Rawi R, Sarfo EK, Schön A, Todd JP, Wang S, Wei H, Wu W; NISC Comparative Sequencing Program, Mullikin JC, Bailer RT, Doria-Rose NA, Karlsson Hedestam GB, Scorpio DG, Overbaugh J, Bloom JD, Carragher B, Potter CS, Shapiro L, Kwong PD, Mascola JR. (2019) Antibody Lineages with Vaccine-Induced Antigen-Binding Hotspots Develop Broad HIV Neutralization. Cell 178, 567-584.
(Demonstrates in NHP the elicitation of antibodies capable of neutralizing over 50% of HIV-1 – and also reveals the molecular mechanism of epitope-focused SHM by which this occurs)
For a complete list of publications, please visit PubMed.gov