Abstract

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

(Seeinstructions):

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Program Projects (P01)
Project #
5P01AI082274-05
Application #
8513894
Study Section
Special Emphasis Panel (ZAI1-EC-A)
Project Start
Project End
Budget Start
2013-08-01
Budget End
2014-07-31
Support Year
5
Fiscal Year
2013
Total Cost
$220,559
Indirect Cost
$46,094

  Institution

Name
University of Massachusetts Medical School Worcester
Department
Type
DUNS #
603847393
City
Worcester
State
MA
Country
United States
Zip Code
01655

  Publications

Esteves, Pedro J; Abrantes, Joana; Baldauf, Hanna-Mari et al. (2018) The wide utility of rabbits as models of human diseases. Exp Mol Med 50:66
Chan, Kun-Wei; Pan, Ruimin; Costa, Matthew et al. (2018) Structural Comparison of Human Anti-HIV-1 gp120 V3 Monoclonal Antibodies of the Same Gene Usage Induced by Vaccination and Chronic Infection. J Virol 92:
Gonzalez-Perez, Maria Paz; Peters, Paul J; O'Connell, Olivia et al. (2017) Identification of Emerging Macrophage-Tropic HIV-1 R5 Variants in Brain Tissue of AIDS Patients without Severe Neurological Complications. J Virol 91:
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
Farfán-Arribas, Diego J; Liu, Shuying; Wang, Shixia et al. (2017) The dynamics of immunoglobulin V-gene usage and clonotype expansion in mice after prime and boost immunizations as analyzed by NGS. Hum Vaccin Immunother 13:2987-2995
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
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
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
Liu, Shuying; Wang, Shixia; Lu, Shan (2016) DNA immunization as a technology platform for monoclonal antibody induction. Emerg Microbes Infect 5:e33
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

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