Dr. Xiangpeng Kong's group at NYU School of Medicine will serve as the Structural Biology Core (SBC) for a Program Project entitled """"""""Neutralizing antibodies targeting the CD4 binding region of HIV-1 ENV"""""""" in response to NIAID program announcement PAR-06-285, HIVVaccine Research and Design (HIVRAD). The team of this P01 includes, in addition to Dr. Kong's group, Drs. Shan Lu (PI, University of Massachusetts Medical School);Paul Clapham (University of Massachusetts Medical School);and Shiu-Lok Hu (University of Washington). Our SBC team is highly experienced in protein crystallography, cryo-electron microscopy and other biophysical techniques, and we will provide services for the P01 team in 3 areas: (i) using protein crystallographic methods to characterize a recombinant protein that mimics the CD4 binding site of HIV-1 gp120, and structural characterization of monoclonal antibodies generated by the P01 team;(ii)using surface plasma resonance (SPR) method to characterize the interactions between HIV-1 gp120 and its mutants with its receptor CD4 as well as antibodies against the HIV-1 surface protein;(iii)using computation method to characterize the structural dynamics of gp120 and its mutants. The structural information generated from our SBC will help the POTs aim in designing a vaccine against HIV-1.

Public Health Relevance


National Institute of Health (NIH)
National Institute of Allergy and Infectious Diseases (NIAID)
Research Program Projects (P01)
Project #
Application #
Study Section
Special Emphasis Panel (ZAI1-EC-A)
Project Start
Project End
Budget Start
Budget End
Support Year
Fiscal Year
Total Cost
Indirect Cost
University of Massachusetts Medical School Worcester
United States
Zip Code
Li, Xiaoyan; Grant, Oliver C; Ito, Keigo et al. (2017) Structural Analysis of the Glycosylated Intact HIV-1 gp120-b12 Antibody Complex Using Hydroxyl Radical Protein Footprinting. Biochemistry 56:957-970
Marty-Roix, Robyn; Vladimer, Gregory I; Pouliot, Kimberly et al. (2016) Identification of QS-21 as an Inflammasome-activating Molecular Component of Saponin Adjuvants. J Biol Chem 291:1123-36
Costa, Matthew R; Pollara, Justin; Edwards, Regina Whitney et al. (2016) Fc Receptor-Mediated Activities of Env-Specific Human Monoclonal Antibodies Generated from Volunteers Receiving the DNA Prime-Protein Boost HIV Vaccine DP6-001. J Virol 90:10362-10378
Suschak, John J; Wang, Shixia; Fitzgerald, Katherine A et al. (2016) A cGAS-Independent STING/IRF7 Pathway Mediates the Immunogenicity of DNA Vaccines. J Immunol 196:310-6
Townsley, Samantha; Li, Yun; Kozyrev, Yury et al. (2016) Conserved Role of an N-Linked Glycan on the Surface Antigen of Human Immunodeficiency Virus Type 1 Modulating Virus Sensitivity to Broadly Neutralizing Antibodies against the Receptor and Coreceptor Binding Sites. J Virol 90:829-41
Liu, Shuying; Wang, Shixia; Lu, Shan (2016) DNA immunization as a technology platform for monoclonal antibody induction. Emerg Microbes Infect 5:e33
Townsley, Samantha; Mohamed, Zeinab; Guo, Wenjin et al. (2016) Induction of Heterologous Tier 2 HIV-1-Neutralizing and Cross-Reactive V1/V2-Specific Antibodies in Rabbits by Prime-Boost Immunization. J Virol 90:8644-60
Musich, Thomas; O'Connell, Olivia; Gonzalez-Perez, Maria Paz et al. (2015) HIV-1 non-macrophage-tropic R5 envelope glycoproteins are not more tropic for entry into primary CD4+ T-cells than envelopes highly adapted for macrophages. Retrovirology 12:25
Suschak, John J; Wang, Shixia; Fitzgerald, Katherine A et al. (2015) Identification of Aim2 as a sensor for DNA vaccines. J Immunol 194:630-6
Kumar, Rajnish; Pan, Ruimin; Upadhyay, Chitra et al. (2015) Functional and Structural Characterization of Human V3-Specific Monoclonal Antibody 2424 with Neutralizing Activity against HIV-1 JRFL. J Virol 89:9090-102

Showing the most recent 10 out of 43 publications