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.

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National Institute of Health (NIH)
National Institute of Allergy and Infectious Diseases (NIAID)
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Special Emphasis Panel (ZAI1-EC-A)
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University of Massachusetts Medical School Worcester
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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
Pouliot, Kimberly; Buglione-Corbett, Rachel; Marty-Roix, Robyn et al. (2014) Contribution of TLR4 and MyD88 for adjuvant monophosphoryl lipid A (MPLA) activity in a DNA prime-protein boost HIV-1 vaccine. Vaccine 32:5049-56
Chen, Yuxin; Vaine, Michael; Wallace, Aaron et al. (2013) A novel rabbit monoclonal antibody platform to dissect the diverse repertoire of antibody epitopes for HIV-1 Env immunogen design. J Virol 87:10232-43
Buglione-Corbett, Rachel; Pouliot, Kimberly; Marty-Roix, Robyn et al. (2013) Serum cytokine profiles associated with specific adjuvants used in a DNA prime-protein boost vaccination strategy. PLoS One 8:e74820
Pan, Ruimin; Sampson, Jared M; Chen, Yuxin et al. (2013) Rabbit anti-HIV-1 monoclonal antibodies raised by immunization can mimic the antigen-binding modes of antibodies derived from HIV-1-infected humans. J Virol 87:10221-31
Murphy, Megan K; Yue, Ling; Pan, Ruimin et al. (2013) Viral escape from neutralizing antibodies in early subtype A HIV-1 infection drives an increase in autologous neutralization breadth. PLoS Pathog 9:e1003173
O'Connell, Olivia; Repik, Alexander; Reeves, Jacqueline D et al. (2013) Efficiency of bridging-sheet recruitment explains HIV-1 R5 envelope glycoprotein sensitivity to soluble CD4 and macrophage tropism. J Virol 87:187-98
Peters, Paul J; Richards, Kathryn; Clapham, Paul (2013) Human immunodeficiency viruses: propagation, quantification, and storage. Curr Protoc Microbiol Chapter 15:Unit 15J.1
Gonzalez-Perez, Maria Paz; O'Connell, Olivia; Lin, Rongheng et al. (2012) Independent evolution of macrophage-tropism and increased charge between HIV-1 R5 envelopes present in brain and immune tissue. Retrovirology 9:20
Duenas-Decamp, Maria J; O'Connell, Olivia J; Corti, Davide et al. (2012) The W100 pocket on HIV-1 gp120 penetrated by b12 is not a target for other CD4bs monoclonal antibodies. Retrovirology 9:9

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