Peter D Kwong, PhD

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.