Peter D Kwong

Summary

Affiliation: National Institutes of Health
Country: USA

Publications

  1. Cheng C, Pancera M, Bossert A, Schmidt S, Chen R, Chen X, et al. Immunogenicity of a Prefusion HIV-1 Envelope Trimer in Complex with a Quaternary-Structure-Specific Antibody. J Virol. 2015;90:2740-55 pubmed publisher
    ..Our findings demonstrate the potential to reduce "off-target" immunogenicity while maintaining the capacity to generate autologous NAbs. ..
  2. Wibmer C, Gorman J, Anthony C, Mkhize N, Druz A, York T, et al. Structure of an N276-Dependent HIV-1 Neutralizing Antibody Targeting a Rare V5 Glycan Hole Adjacent to the CD4 Binding Site. J Virol. 2016;90:10220-10235 pubmed publisher
    ..These data highlight how glycan holes can play a role in the elicitation of B-cell lineages targeting the CD4 binding site. ..
  3. Kong R, Xu K, Zhou T, Acharya P, Lemmin T, Liu K, et al. Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody. Science. 2016;352:828-33 pubmed publisher
    ..These results reveal the fusion peptide to be a neutralizing antibody epitope and thus a target for vaccine design. ..
  4. Krebs S, Kwon Y, Schramm C, Law W, Donofrio G, Zhou K, et al. Longitudinal Analysis Reveals Early Development of Three MPER-Directed Neutralizing Antibody Lineages from an HIV-1-Infected Individual. Immunity. 2019;50:677-691.e13 pubmed publisher
    ..These features suggest that VRC42 may be a promising template for lineage-based vaccine design. ..
  5. Lai Y, Wang T, O Dell S, Louder M, SchOn A, Cheung C, et al. Lattice engineering enables definition of molecular features allowing for potent small-molecule inhibition of HIV-1 entry. Nat Commun. 2019;10:47 pubmed publisher
    ..The improved diffraction reveals BMS-818251 to utilize functional groups that interact with gp120 residues from the conserved β20-β21 hairpin to improve potency. ..
  6. Chuang G, Zhou J, Acharya P, Rawi R, Shen C, Sheng Z, et al. Structural Survey of Broadly Neutralizing Antibodies Targeting the HIV-1 Env Trimer Delineates Epitope Categories and Characteristics of Recognition. Structure. 2019;27:196-206.e6 pubmed publisher
    ..0005). The unusual characteristics of epitope and paratope delineated here are likely to reflect respectively virus-immune evasion and antibody-recognition solutions that allow effective neutralization of HIV-1. ..
  7. Xu K, Acharya P, Kong R, Cheng C, Chuang G, Liu K, et al. Epitope-based vaccine design yields fusion peptide-directed antibodies that neutralize diverse strains of HIV-1. Nat Med. 2018;24:857-867 pubmed publisher
    ..The N terminus of the HIV-1 fusion peptide is thus a promising target of vaccine efforts aimed at eliciting broadly neutralizing antibodies. ..
  8. Kwong P, Mascola J. HIV-1 Vaccines Based on Antibody Identification, B Cell Ontogeny, and Epitope Structure. Immunity. 2018;48:855-871 pubmed publisher
    ..Both epitope-based and antibody lineage-based HIV-1 vaccine approaches are being readied for human clinical trials. ..
  9. Sastry M, Bewley C, Kwong P. Effective isotope labeling of proteins in a mammalian expression system. Methods Enzymol. 2015;565:289-307 pubmed publisher
    ..These methods should allow NMR spectroscopic analysis of the structure and function of posttranslationally modified and secreted, cytoplasmic, or membrane-bound proteins. ..

More Information

Publications25

  1. Zhou T, Zheng A, Baxa U, Chuang G, Georgiev I, Kong R, et al. A Neutralizing Antibody Recognizing Primarily N-Linked Glycan Targets the Silent Face of the HIV Envelope. Immunity. 2018;48:500-513.e6 pubmed publisher
  2. Zhou T, Lynch R, Chen L, Acharya P, Wu X, Doria Rose N, et al. Structural Repertoire of HIV-1-Neutralizing Antibodies Targeting the CD4 Supersite in 14 Donors. Cell. 2015;161:1280-92 pubmed publisher
  3. Georgiev I, Joyce M, Yang Y, Sastry M, Zhang B, Baxa U, et al. Single-Chain Soluble BG505.SOSIP gp140 Trimers as Structural and Antigenic Mimics of Mature Closed HIV-1 Env. J Virol. 2015;89:5318-29 pubmed publisher
    ..SOSIP, as they would not require furin cleavage to achieve mimicry of mature Env spikes on virions. ..
  4. Kwong P, Mascola J. Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogenies. Immunity. 2012;37:412-25 pubmed publisher
    ..The human immune system is capable of developing antibodies that broadly neutralize HIV-1--and an increasingly detailed view is accumulating for how effective immunity against HIV-1 can be generated. ..
  5. Rutten L, Lai Y, Blokland S, Truan D, Bisschop I, Strokappe N, et al. A Universal Approach to Optimize the Folding and Stability of Prefusion-Closed HIV-1 Envelope Trimers. Cell Rep. 2018;23:584-595 pubmed publisher
    ..Our approach provides a means to produce prefusion-closed Env trimers from diverse HIV-1 strains, a substantial advance for vaccine development. ..
  6. Cale E, Gorman J, Radakovich N, Crooks E, Osawa K, Tong T, et al. Virus-like Particles Identify an HIV V1V2 Apex-Binding Neutralizing Antibody that Lacks a Protruding Loop. Immunity. 2017;46:777-791.e10 pubmed publisher
    ..The N90-VRC38 lineage thus identifies a solution for V1V2-apex binding that provides a more conventional B cell pathway for vaccine design. ..
  7. Kwon Y, Chuang G, Zhang B, Bailer R, Doria Rose N, Gindin T, et al. Surface-Matrix Screening Identifies Semi-specific Interactions that Improve Potency of a Near Pan-reactive HIV-1-Neutralizing Antibody. Cell Rep. 2018;22:1798-1809 pubmed publisher
    ..We propose surface-matrix screening as a general method to improve antibodies, with improved semi-specific interactions between antibody and antigen enabling increased potency without compromising breadth. ..
  8. Wu X, Zhang Z, Schramm C, Joyce M, Kwon Y, Zhou T, et al. Maturation and Diversity of the VRC01-Antibody Lineage over 15 Years of Chronic HIV-1 Infection. Cell. 2015;161:470-485 pubmed publisher
    ..This high rate of antibody evolution provides a mechanism by which antibody lineages can achieve extraordinary diversity and, over years of chronic infection, develop effective HIV-1 neutralization. ..
  9. Zhou T, Doria Rose N, Cheng C, Stewart Jones G, Chuang G, Chambers M, et al. Quantification of the Impact of the HIV-1-Glycan Shield on Antibody Elicitation. Cell Rep. 2017;19:719-732 pubmed publisher
    ..Based on these high titers and exponential relationship, we propose site-selective deglycosylated trimers as priming immunogens to increase the frequency of site-targeting antibodies. ..
  10. Kwong P, Wilson I. HIV-1 and influenza antibodies: seeing antigens in new ways. Nat Immunol. 2009;10:573-8 pubmed publisher
    ..We outline how each of these different modes of antibody recognition is particularly suited to overcoming a specific viral evasion tactic and assess potential routes of re-elicitation in vaccine settings. ..
  11. Joyce M, Wheatley A, Thomas P, Chuang G, Soto C, Bailer R, et al. Vaccine-Induced Antibodies that Neutralize Group 1 and Group 2 Influenza A Viruses. Cell. 2016;166:609-623 pubmed publisher
    ..We propose the sequence signature-quantified prevalence of these B cells as a metric to guide universal influenza A immunization strategies. ..
  12. Stewart Jones G, Soto C, Lemmin T, Chuang G, Druz A, Kong R, et al. Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G. Cell. 2016;165:813-26 pubmed publisher
  13. Bonsignori M, Zhou T, Sheng Z, Chen L, Gao F, Joyce M, et al. Maturation Pathway from Germline to Broad HIV-1 Neutralizer of a CD4-Mimic Antibody. Cell. 2016;165:449-63 pubmed publisher
    ..We integrated our CH235-lineage findings with a second broadly neutralizing lineage and HIV-1 co-evolution to suggest a vaccination strategy for inducing both lineages. ..
  14. Joyce M, Georgiev I, Yang Y, Druz A, Geng H, Chuang G, et al. Soluble Prefusion Closed DS-SOSIP.664-Env Trimers of Diverse HIV-1 Strains. Cell Rep. 2017;21:2992-3002 pubmed publisher
    ..Structure-based design thus enables the production of prefusion closed HIV-1-Env trimers from dozens of diverse strains. ..
  15. Lemmin T, Soto C, Stuckey J, Kwong P. Microsecond Dynamics and Network Analysis of the HIV-1 SOSIP Env Trimer Reveal Collective Behavior and Conserved Microdomains of the Glycan Shield. Structure. 2017;25:1631-1639.e2 pubmed publisher
    ..Overall, our results provide a microsecond-based understanding of the Env glycan shield. ..
  16. request reprint
    Kwong P, Doyle M, Casper D, Cicala C, Leavitt S, Majeed S, et al. HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites. Nature. 2002;420:678-82 pubmed
    ..Because this solution is available for cell-surface receptors but not for most antibodies, conformational masking enables HIV-1 to maintain receptor binding and simultaneously to resist neutralization. ..