Peter D Kwong

Summary

Affiliation: National Institutes of Health
Country: USA

Publications

  1. pmc Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin
    Xinzhen Yang
    Department of Cancer Immunology and AIDS, Dana Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA
    J Virol 76:4634-42. 2002
  2. ncbi request reprint Human immunodeficiency virus: refolding the envelope
    Peter D Kwong
    Nature 433:815-6. 2005
  3. pmc Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy
    Mallika Sastry
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892 3027, USA
    J Biomol NMR 50:197-207. 2011
  4. pmc Somatic Populations of PGT135-137 HIV-1-Neutralizing Antibodies Identified by 454 Pyrosequencing and Bioinformatics
    Jiang Zhu
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health Bethesda, MD, USA
    Front Microbiol 3:315. 2012
  5. pmc Crystal structures of HIV-1 gp120 envelope glycoprotein in complex with NBD analogues that target the CD4-binding site
    Young Do Kwon
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, United States of America
    PLoS ONE 9:e85940. 2014
  6. doi request reprint Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogenies
    Peter D Kwong
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Immunity 37:412-25. 2012
  7. pmc Structural basis for broad detection of genogroup II noroviruses by a monoclonal antibody that binds to a site occluded in the viral particle
    Grant S Hansman
    Department of Virology II, National Institute of Infectious Diseases, Tokyo, JapanA
    J Virol 86:3635-46. 2012
  8. ncbi request reprint HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites
    Peter D Kwong
    Vaccine Research Center, National Institutes of Health, Bethesda, Maryland 20892, USA
    Nature 420:678-82. 2002
  9. doi request reprint Vaccine design reaches the atomic level
    Peter D Kwong
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Sci Transl Med 3:91ps29. 2011
  10. pmc HIV-1 and influenza antibodies: seeing antigens in new ways
    Peter D Kwong
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA
    Nat Immunol 10:573-8. 2009

Detail Information

Publications89

  1. pmc Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin
    Xinzhen Yang
    Department of Cancer Immunology and AIDS, Dana Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA
    J Virol 76:4634-42. 2002
    ..The melting temperatures and ligand recognition properties of the GCN4- and fibritin-stabilized soluble gp140 glycoproteins suggest that these molecules assume conformations distinct from that of the fusion-active, six-helix bundle...
  2. ncbi request reprint Human immunodeficiency virus: refolding the envelope
    Peter D Kwong
    Nature 433:815-6. 2005
  3. pmc Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy
    Mallika Sastry
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892 3027, USA
    J Biomol NMR 50:197-207. 2011
    ....
  4. pmc Somatic Populations of PGT135-137 HIV-1-Neutralizing Antibodies Identified by 454 Pyrosequencing and Bioinformatics
    Jiang Zhu
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health Bethesda, MD, USA
    Front Microbiol 3:315. 2012
    ..Our results thus provide an example of how pathogens like HIV-1 are opposed by a varied humoral immune response, derived from intrinsic mechanisms of antibody development, and embodied by somatic populations of diverse antibodies...
  5. pmc Crystal structures of HIV-1 gp120 envelope glycoprotein in complex with NBD analogues that target the CD4-binding site
    Young Do Kwon
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, United States of America
    PLoS ONE 9:e85940. 2014
    ..Herein, six co-crystal structures of NBD-analogues with gp120 provide a structural framework for continued small molecule-entry inhibitor optimization. ..
  6. doi request reprint Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogenies
    Peter D Kwong
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Immunity 37:412-25. 2012
    ..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...
  7. pmc Structural basis for broad detection of genogroup II noroviruses by a monoclonal antibody that binds to a site occluded in the viral particle
    Grant S Hansman
    Department of Virology II, National Institute of Infectious Diseases, Tokyo, JapanA
    J Virol 86:3635-46. 2012
    ..Together, the results provide evidence that the norovirus particle is capable of extreme conformational flexibility, which may allow for antibody recognition of conserved surfaces that would otherwise be buried on intact particles...
  8. ncbi request reprint HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites
    Peter D Kwong
    Vaccine Research Center, National Institutes of Health, Bethesda, Maryland 20892, USA
    Nature 420:678-82. 2002
    ..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...
  9. doi request reprint Vaccine design reaches the atomic level
    Peter D Kwong
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Sci Transl Med 3:91ps29. 2011
    ..This accomplishment provides a glimpse of the power of structure-based vaccine design to create immunogens capable of eliciting protective responses against genetically diverse pathogens...
  10. pmc HIV-1 and influenza antibodies: seeing antigens in new ways
    Peter D Kwong
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA
    Nat Immunol 10:573-8. 2009
    ..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. pmc Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1
    Xueling Wu
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Science 329:856-61. 2010
    ..Exceptionally broad HIV-1 neutralization can be achieved with individual antibodies targeted to the functionally conserved CD4bs of glycoprotein 120, an important insight for future HIV-1 vaccine design...
  12. pmc Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120
    Lei Chen
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Science 326:1123-7. 2009
    ..This incompatibility, the consequence of slight differences in CD4BS recognition, renders HIV-1 resistant to all but the most accurately targeted antibodies...
  13. pmc Structural basis for diverse N-glycan recognition by HIV-1-neutralizing V1-V2-directed antibody PG16
    Marie Pancera
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, US National Institutes of Health, Bethesda, Maryland, USA
    Nat Struct Mol Biol 20:804-13. 2013
    ..Although HIV-1-glycan diversity facilitates evasion, antibody somatic diversity can overcome this and can provide clues to guide the design of modified antibodies with enhanced neutralization. ..
  14. pmc Crystal structure of PG16 and chimeric dissection with somatically related PG9: structure-function analysis of two quaternary-specific antibodies that effectively neutralize HIV-1
    Marie Pancera
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892 3027, USA
    J Virol 84:8098-110. 2010
    ..The structural and functional details of extraordinary CDR H3 and extensive affinity maturation provide insights into the neutralization mechanism of and the elicitation pathway for broadly neutralizing antibodies like PG9 and PG16...
  15. pmc Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4
    Chih Chin Huang
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Science 317:1930-4. 2007
    ....
  16. pmc Structure of a V3-containing HIV-1 gp120 core
    Chih Chin Huang
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892, USA
    Science 310:1025-8. 2005
    ..The extended nature and antibody accessibility of V3 explain its immunodominance. Together, the results provide a structural rationale for the role of V3 in HIV entry and neutralization...
  17. pmc Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01
    Tongqing Zhou
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health NIH, Bethesda, MD 20892, USA
    Science 329:811-7. 2010
    ..Partial receptor mimicry and extensive affinity maturation thus facilitate neutralization of HIV-1 by natural human antibodies...
  18. pmc Enhanced exposure of the CD4-binding site to neutralizing antibodies by structural design of a membrane-anchored human immunodeficiency virus type 1 gp120 domain
    Lan Wu
    Vaccine Research Center, NIAID, National Institutes of Health, Bldg 40, 40 Convent Drive, Bethesda, MD 20892 3005, USA
    J Virol 83:5077-86. 2009
    ..Structurally designed membrane-anchored ODs represent candidate immunogens to elicit or to allow the detection of broadly neutralizing antibodies to the conserved site of CD4 binding on HIV-1 gp120...
  19. pmc Structure-based stabilization of HIV-1 gp120 enhances humoral immune responses to the induced co-receptor binding site
    Barna Dey
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD, USA
    PLoS Pathog 5:e1000445. 2009
    ..These results demonstrate that structure-based approaches can be exploited to stabilize a conformational site in a large functional protein to enhance immunogenic responses specific for that region...
  20. pmc Tyrosine-sulfate isosteres of CCR5 N-terminus as tools for studying HIV-1 entry
    Son N Lam
    Laboratory of Bioorganic Chemistry, National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, DHHS, Bethesda, MD 20892, USA
    Bioorg Med Chem 16:10113-20. 2008
    ....
  21. pmc Structural basis for HIV-1 neutralization by 2F5-like antibodies m66 and m66.6
    Gilad Ofek
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA
    J Virol 88:2426-41. 2014
    ..Antibodies m66, m66.6, and 2F5 thus utilize similar mechanistic elements to recognize a common gp41-MPER epitope and to neutralize HIV-1. ..
  22. pmc Heavy chain-only IgG2b llama antibody effects near-pan HIV-1 neutralization by recognizing a CD4-induced epitope that includes elements of coreceptor- and CD4-binding sites
    Priyamvada Acharya
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA
    J Virol 87:10173-81. 2013
    ....
  23. pmc Characterization of human immunodeficiency virus type 1 monomeric and trimeric gp120 glycoproteins stabilized in the CD4-bound state: antigenicity, biophysics, and immunogenicity
    Barna Dey
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    J Virol 81:5579-93. 2007
    ..Together, the results suggest that conformational stabilization may improve the ability of gp120 to elicit neutralizing antibodies...
  24. pmc Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
    Jason S McLellan
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    Nature 480:336-43. 2011
    ..In addition to structurally defining V1/V2, the results thus identify a paradigm of antibody recognition for highly glycosylated antigens, which-with PG9-involves a site of vulnerability comprising just two glycans and a strand...
  25. pmc Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing
    Xueling Wu
    Vaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA
    Science 333:1593-602. 2011
    ....
  26. pmc Relationship between antibody 2F5 neutralization of HIV-1 and hydrophobicity of its heavy chain third complementarity-determining region
    Gilad Ofek
    Vaccine Research Center, NIAID, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Virol 84:2955-62. 2010
    ..Together, the results provide a more complete understanding of the 2F5 mechanism of HIV-1 neutralization and indicate ways to enhance the potency of MPER-directed antibodies...
  27. doi request reprint Structural basis for highly effective HIV-1 neutralization by CD4-mimetic miniproteins revealed by 1.5 Å cocrystal structure of gp120 and M48U1
    Priyamvada Acharya
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Structure 21:1018-29. 2013
    ..Ligand chemistry, shape complementarity, surface burial, and gp120 conformation act in concert to modulate binding of ligands to the gp120-Phe43 cavity and, when optimized, can effect near-pan-neutralization of HIV-1...
  28. doi request reprint Delineating antibody recognition in polyclonal sera from patterns of HIV-1 isolate neutralization
    Ivelin S Georgiev
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Science 340:751-6. 2013
    ..Patterns of virus-isolate neutralization can thus afford a detailed epitope-specific understanding of neutralizing-antibody responses to viral infection...
  29. pmc Mining the antibodyome for HIV-1-neutralizing antibodies with next-generation sequencing and phylogenetic pairing of heavy/light chains
    Jiang Zhu
    Vaccine Research Center, National Institutes of Health Intramural Sequencing Center, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 110:6470-5. 2013
    ..Altogether, our findings suggest that phylogenetic matching of heavy and light chains can provide a means to approximate natural pairings...
  30. pmc Immunotypes of a quaternary site of HIV-1 vulnerability and their recognition by antibodies
    Xueling Wu
    Vaccine Research Center, NIAID, NIH, 40 Convent Drive, Bethesda, MD 20892, USA
    J Virol 85:4578-85. 2011
    ..Quaternary structure-specific antibodies appear to target antigenic variants of the same epitope, with neutralization breadth determined by the prevalence of recognized variants among circulating isolates...
  31. pmc Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility
    Marie Pancera
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 107:1166-71. 2010
    ..A "layered" gp120 architecture thus allows movement among alternative glycoprotein conformations required for virus entry and immune evasion, whereas a beta-sandwich clamp maintains gp120-gp41 interaction and regulates gp41 transitions...
  32. pmc Residue-level prediction of HIV-1 antibody epitopes based on neutralization of diverse viral strains
    Gwo Yu Chuang
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA
    J Virol 87:10047-58. 2013
    ..Together the results show how knowledge inherent to a neutralization panel and unbound antigen structure can be utilized for residue-level prediction of antibody epitopes. ..
  33. pmc Multidonor analysis reveals structural elements, genetic determinants, and maturation pathway for HIV-1 neutralization by VRC01-class antibodies
    Tongqing Zhou
    Vaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA
    Immunity 39:245-58. 2013
    ..Developmental similarities in multiple donors thus reveal the generation of VRC01-class antibodies to be reproducible in principle, thereby providing a framework for attempts to elicit similar antibodies in the general population. ..
  34. pmc N332-Directed broadly neutralizing antibodies use diverse modes of HIV-1 recognition: inferences from heavy-light chain complementation of function
    Marie Pancera
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, United States of America
    PLoS ONE 8:e55701. 2013
    ..Overall, our results add to the growing body of evidence that the human immune system is capable of recognizing the N332-region of HIV-1 gp120 in diverse ways...
  35. pmc Structural basis for norovirus inhibition and fucose mimicry by citrate
    Grant S Hansman
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Virol 86:284-92. 2012
    ..Importantly, competition STD NMR showed that citrate could compete with HBGA for norovirus binding. Together, the results suggest that citrate and other glycomimetics have the potential to block human noroviruses from binding to HBGAs...
  36. pmc Local conformational stability of HIV-1 gp120 in unliganded and CD4-bound states as defined by amide hydrogen/deuterium exchange
    Leopold Kong
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892 3027, USA
    J Virol 84:10311-21. 2010
    ..The results provide a framework for understanding how local conformational stability influences entropic change, conformational diversity, and structural rearrangements in the gp120-CD4 binding reaction...
  37. pmc Structure of a major antigenic site on the respiratory syncytial virus fusion glycoprotein in complex with neutralizing antibody 101F
    Jason S McLellan
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Virol 84:12236-44. 2010
    ..Collectively, these results provide a structural basis for RSV neutralization by antibodies that target a major antigenic site on the fusion glycoprotein...
  38. pmc Mechanism of human immunodeficiency virus type 1 resistance to monoclonal antibody B12 that effectively targets the site of CD4 attachment
    Xueling Wu
    Vaccine Research Center, NIAID, NIH, 40 Convent Dr, Bethesda, MD 20892, USA
    J Virol 83:10892-907. 2009
    ....
  39. pmc Structural definition of a conserved neutralization epitope on HIV-1 gp120
    Tongqing Zhou
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    Nature 445:732-7. 2007
    ..A site of vulnerability, related to a functional requirement for efficient association with CD4, can therefore be targeted by antibody to neutralize HIV-1...
  40. ncbi request reprint Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies
    Nicole A Doria-Rose
    1 Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA 2
    Nature 509:55-62. 2014
    ..These data provide important insights relevant to HIV-1 vaccine development. ..
  41. doi request reprint Structure-based design of a fusion glycoprotein vaccine for respiratory syncytial virus
    Jason S McLellan
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Science 342:592-8. 2013
    ..Immunization with site Ø-stabilized variants of RSV F in mice and macaques elicited levels of RSV-specific neutralizing activity many times the protective threshold. ..
  42. pmc Outer domain of HIV-1 gp120: antigenic optimization, structural malleability, and crystal structure with antibody VRC-PG04
    M Gordon Joyce
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA
    J Virol 87:2294-306. 2013
    ..2.2 with VRC-PG04 provides atomic-level details for an HIV-1 domain recognized by broadly neutralizing antibodies and insights relevant to the rational design of an immunogen that could elicit such antibodies by vaccination...
  43. pmc Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops
    Young Do Kwon
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 109:5663-8. 2012
    ..g., the CD4-bound state) provides advantages in terms of HIV-1 Env structural diversity and resistance to antibodies and inhibitors, while maintaining elements essential for entry...
  44. doi request reprint Antibodies VRC01 and 10E8 neutralize HIV-1 with high breadth and potency even with Ig-framework regions substantially reverted to germline
    Ivelin S Georgiev
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892
    J Immunol 192:1100-6. 2014
    ..Partial framework revertants of HIV-1 broadly neutralizing Abs may present advantages over their highly mutated counterparts as Ab therapeutics and as targets for immunogen design. ..
  45. ncbi request reprint Scorpion-toxin mimics of CD4 in complex with human immunodeficiency virus gp120 crystal structures, molecular mimicry, and neutralization breadth
    Chih Chin Huang
    Vaccine Research Center, National Institutes of Health, Bethesda, Maryland 20892, USA
    Structure 13:755-68. 2005
    ....
  46. pmc Crystal structure of human antibody 2909 reveals conserved features of quaternary structure-specific antibodies that potently neutralize HIV-1
    Anita Changela
    Vaccine Research Center, NIAID NIH, 40 Convent Drive, Building 40, Room 4508, Bethesda, MD 20892 3027, USA
    J Virol 85:2524-35. 2011
    ....
  47. ncbi request reprint Structure-Based Stabilization of HIV-1 gp120 Enhances Humoral Immune Responses to the Induced Co-Receptor Binding Site
    Barna Dey
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, United States of America
    PLoS Pathog 5:e1000445. 2009
    ..These results demonstrate that structure-based approaches can be exploited to stabilize a conformational site in a large functional protein to enhance immunogenic responses specific for that region...
  48. pmc Soluble mimetics of human immunodeficiency virus type 1 viral spikes produced by replacement of the native trimerization domain with a heterologous trimerization motif: characterization and ligand binding analysis
    Marie Pancera
    Vaccine Research Center, NIH, Bethesda, Bethesda, MD 20892, USA
    J Virol 79:9954-69. 2005
    ..Thus, the gp120-GCN4 trimers demonstrate several properties that are consistent with some of those anticipated for gp120 in the context of the viral spike...
  49. pmc De novo identification of VRC01 class HIV-1-neutralizing antibodies by next-generation sequencing of B-cell transcripts
    Jiang Zhu
    Vaccine Research Center and NIH Intramural Sequencing Center, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD 20892
    Proc Natl Acad Sci U S A 110:E4088-97. 2013
    ..Bioinformatics analysis can thus directly identify functional HIV-1-neutralizing antibodies of the VRC01 class from a sequenced antibody repertoire. ..
  50. pmc Computational prediction of N-linked glycosylation incorporating structural properties and patterns
    Gwo Yu Chuang
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MA 20892, USA
    Bioinformatics 28:2249-55. 2012
    ..None of the currently available servers, however, utilizes protein structural information for the prediction of N-glycan occupancy...
  51. doi request reprint Structure of RSV fusion glycoprotein trimer bound to a prefusion-specific neutralizing antibody
    Jason S McLellan
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Science 340:1113-7. 2013
    ..These studies should enable design of improved vaccine antigens and define new targets for passive prevention of RSV-induced disease...
  52. pmc Peptides from second extracellular loop of C-C chemokine receptor type 5 (CCR5) inhibit diverse strains of HIV-1
    Cajetan Dogo-Isonagie
    Laboratory of Bioorganic Chemistry, NIAID, National Institutes of Health, Bethesda, Maryland 20892, USA
    J Biol Chem 287:15076-86. 2012
    ..These peptides may serve as a starting point for the design of inhibitors with broad spectrum anti-HIV activity...
  53. pmc Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability
    Grant S Hansman
    Structural Biology Section, Vaccine Research Center, National Institute of Allergy and Infectious Diseases, 40 Convent Drive, Building 40, Room 4508, National Institutes of Health, Bethesda, MD 20892, USA
    J Virol 85:6687-701. 2011
    ..Despite this evasion tactic, the HBGA site of viral vulnerability may provide a viable target for small molecule- and antibody-mediated neutralization of GII norovirus...
  54. pmc Structure of respiratory syncytial virus fusion glycoprotein in the postfusion conformation reveals preservation of neutralizing epitopes
    Jason S McLellan
    Vaccine Research Center, NIAID NIH, 40 Convent Drive, Bldg 40, Rm 2613B, Bethesda, MD 20892, USA
    J Virol 85:7788-96. 2011
    ..The structural preservation of neutralizing epitopes in the postfusion state suggests that this conformation can elicit neutralizing antibodies and serve as a useful vaccine antigen...
  55. pmc Design and characterization of epitope-scaffold immunogens that present the motavizumab epitope from respiratory syncytial virus
    Jason S McLellan
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    J Mol Biol 409:853-66. 2011
    ....
  56. pmc Elicitation of structure-specific antibodies by epitope scaffolds
    Gilad Ofek
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 107:17880-7. 2010
    ..Epitope scaffolds thus provide a means to elicit antibodies that recognize a predetermined target shape and sequence, even if that shape is transient in nature, and a means by which to dissect factors influencing such elicitation...
  57. pmc Progress in the rational design of an AIDS vaccine
    Gary J Nabel
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 40 Convent Drive, MSC 3005, Bethesda, MD 20892, USA
    Philos Trans R Soc Lond B Biol Sci 366:2759-65. 2011
    ....
  58. pmc Structure-based identification and neutralization mechanism of tyrosine sulfate mimetics that inhibit HIV-1 entry
    Priyamvada Acharya
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, United States
    ACS Chem Biol 6:1069-77. 2011
    ....
  59. pmc Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope
    Gilad Ofek
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Instiutes of Health, Bethesda, MD 20892, USA
    J Virol 78:10724-37. 2004
    ..Based on these structural and biochemical results, immunization strategies for eliciting 2F5- and 4E10-like broadly neutralizing anti-HIV-1 antibodies are proposed...
  60. pmc Structural basis of tyrosine sulfation and VH-gene usage in antibodies that recognize the HIV type 1 coreceptor-binding site on gp120
    Chih Chin Huang
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 101:2706-11. 2004
    ..When confronted by extraordinary viral defenses, the immune system unveils novel adaptive capabilities, with tyrosine sulfation enhancing the vocabulary of antigen recognition...
  61. pmc Synthetic glycopeptides reveal the glycan specificity of HIV-neutralizing antibodies
    Mohammed N Amin
    Institute of Human Virology, University of Maryland School of Medicine, Baltimore, Maryland, USA
    Nat Chem Biol 9:521-6. 2013
    ..In addition to defining the glycan specificities of PG9 and PG16, the identified synthetic glycopeptides provide a valuable template for HIV-1 vaccine design...
  62. doi request reprint Broad and potent neutralization of HIV-1 by a gp41-specific human antibody
    Jinghe Huang
    HIV Specific Immunity Section, Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    Nature 491:406-12. 2012
    ..The highly conserved MPER is a target of potent, non-self-reactive neutralizing antibodies, suggesting that HIV-1 vaccines should aim to induce antibodies to this region of HIV-1 envelope glycoprotein...
  63. pmc A short segment of the HIV-1 gp120 V1/V2 region is a major determinant of resistance to V1/V2 neutralizing antibodies
    Nicole A Doria-Rose
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA
    J Virol 86:8319-23. 2012
    ....
  64. pmc Structural basis of respiratory syncytial virus neutralization by motavizumab
    Jason S McLellan
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA
    Nat Struct Mol Biol 17:248-50. 2010
    ..Modeling suggests that motavizumab recognizes a different quaternary configuration of the F glycoprotein than that observed in a homologous structure...
  65. pmc Heterologous epitope-scaffold prime:boosting immuno-focuses B cell responses to the HIV-1 gp41 2F5 neutralization determinant
    Javier Guenaga
    Vaccine Research Center, National Institutes of Health, Bethesda, Maryland, United States of America
    PLoS ONE 6:e16074. 2011
    ..Together, these results indicate that heterologous ES prime:boost immunization regimens effectively focus the humoral immune response on the structurally defined and immunogen-conserved HIV-1 2F5 epitope...
  66. ncbi request reprint Mining the B cell repertoire for broadly neutralizing monoclonal antibodies to HIV-1
    Peter D Kwong
    Vaccine Research Center, NIAID, National Institutes of Health, Bethesda, MD 20892, USA
    Cell Host Microbe 6:292-4. 2009
    ....
  67. pmc Rational design of vaccines to elicit broadly neutralizing antibodies to HIV-1
    Peter D Kwong
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892
    Cold Spring Harb Perspect Med 1:a007278. 2011
    ....
  68. pmc The changing face of HIV vaccine research
    Peter D Kwong
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    J Int AIDS Soc 15:17407. 2012
    ..This article summarizes challenges to the development of an HIV-1 vaccine, lessons learned from scientific investigation and completed vaccine trials, and promising developments in HIV-1 vaccine design...
  69. doi request reprint Mammalian expression of isotopically labeled proteins for NMR spectroscopy
    Mallika Sastry
    National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892 3027, USA
    Adv Exp Med Biol 992:197-211. 2012
    ..Selective amino-acid labeling is also described. These developments should reduce barriers to the determination of NMR structures with isotopically labeled proteins from mammalian expression systems...
  70. ncbi request reprint The rational design of an AIDS vaccine
    Daniel C Douek
    Vaccine Research Center, NIAID, National Institutes of Health, Room 4502, Building 40, MSC 3005, 40 Convent Drive, Bethesda, MD 20892, USA
    Cell 124:677-81. 2006
    ..AIDS vaccine design requires a scientifically driven, rational approach that encompasses the latest advances in viral molecular genetics, structural biology, and immunology...
  71. pmc Interfacial metal and antibody recognition
    Tongqing Zhou
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
    Proc Natl Acad Sci U S A 102:14575-80. 2005
    ..5 kcal/mol of binding energy. This energetic contribution, which is greater than that from a typical protein atom, demonstrates how interfacial metal ligation can play a unique role in antigen recognition...
  72. pmc Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: implications for viral entry and immunogenicity
    Chantelle L Hood
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Room 4502, Building 40, MSC 3005, 40 Convent Drive, Bethesda, Maryland 20892 3005, USA
    J Virol 84:2972-82. 2010
    ..Together, these data suggest that CatL cleavage of EBOV GP exposes its receptor-binding domain, thereby facilitating access to a putative cellular receptor in steps that lead to membrane fusion...
  73. ncbi request reprint Rational design of vaccines to elicit broadly neutralizing antibodies to HIV-1
    Peter D Kwong
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    Cold Spring Harb Perspect Biol 3:a007278. 2011
    ....
  74. ncbi request reprint Rational design of vaccines to elicit broadly neutralizing antibodies to HIV-1
    Peter D Kwong
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    Cold Spring Harb Perspect Biol 3:a007278. 2011
    ....
  75. ncbi request reprint Rational design of vaccines to elicit broadly neutralizing antibodies to HIV-1
    Peter D Kwong
    Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
    Cold Spring Harb Perspect Biol 3:a007278. 2011
    ....
  76. ncbi request reprint Enhancing protein crystallization through precipitant synergy
    Shahzad Majeed
    Vaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA
    Structure 11:1061-70. 2003
    ..The results indicate that mechanistically distinct precipitants can synergize, with precipitant combinations adding unique dimensions to protein crystallization...
  77. pmc Structure-activity relationships in the binding of chemically derivatized CD4 to gp120 from human immunodeficiency virus
    Hui Xie
    Department of Pharmacology and Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032, USA
    J Med Chem 50:4898-908. 2007
    ..This first SAR on ligand binding to an interior cavity of gp120 may provide a starting point for structure-based assembly of small molecules targeting gp120-CD4 interaction...
  78. pmc Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1
    Aran F Labrijn
    Department of Immunology, The Scripps Research Institute, La Jolla, California 92037, USA
    J Virol 77:10557-65. 2003
    ..The results identify hurdles in using CD4i epitopes as targets for antibody-mediated neutralization in vaccine design but also indicate that the CD4i regions could be efficiently targeted by small molecule entry inhibitors...
  79. ncbi request reprint Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition
    Markus Koch
    Department of Cancer Immunology and AIDS, Dana Farber Cancer Institute, Boston, MA 02115, USA
    Virology 313:387-400. 2003
    ..Thus, carbohydrates that flank receptor-binding regions on gp120 protect primary HIV-1 isolates from antibody-mediated neutralization...
  80. ncbi request reprint Tyrosine sulfation of human antibodies contributes to recognition of the CCR5 binding region of HIV-1 gp120
    Hyeryun Choe
    Children s Hospital, Department of Pediatrics, Harvard Medical School, Boston, MA 02115, USA
    Cell 114:161-70. 2003
    ..These studies identify a distinct subset of CD4-induced HIV-1 neutralizing antibodies that closely emulate CCR5 and demonstrate that tyrosine sulfation can contribute to the potency and diversity of the human humoral response...
  81. ncbi request reprint Antibody neutralization and escape by HIV-1
    Xiping Wei
    Howard Hughes Medical Institute, University of Alabama at Birmingham, 720 South 20th Street, Kaul 816, Birmingham, Alabama 35294 0024, USA
    Nature 422:307-12. 2003
    ..The evolving glycan shield thus represents a new mechanism contributing to HIV-1 persistence in the face of an evolving antibody repertoire...
  82. pmc Mutagenic stabilization and/or disruption of a CD4-bound state reveals distinct conformations of the human immunodeficiency virus type 1 gp120 envelope glycoprotein
    Shi Hua Xiang
    Department of Cancer Immunology and AIDS, Dana Farber Cancer Institute and Harvard Medical School Boston, Massachusetts 02115, USA
    J Virol 76:9888-99. 2002
    ..These results indicate that CD4BS antibodies recognize conformations of gp120 different from that recognized by CD4 and CD4i antibodies...
  83. ncbi request reprint Epitope mapping and characterization of a novel CD4-induced human monoclonal antibody capable of neutralizing primary HIV-1 strains
    Shi Hua Xiang
    Department of Cancer Immunology and AIDS, Dana Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA
    Virology 315:124-34. 2003
    ..Thus, on primary HIV-1 isolates, this gp120 region, which has been previously implicated in chemokine receptor binding, is accessible to a subset of CD4i antibodies...
  84. ncbi request reprint HIV vaccine design and the neutralizing antibody problem
    Dennis R Burton
    Departments of Immunology and Molecular Biology, Scripps Research Institute, La Jolla, California, USA
    Nat Immunol 5:233-6. 2004
  85. pmc Antigenic conservation and immunogenicity of the HIV coreceptor binding site
    Julie M Decker
    Howard Hughes Institute, Department of Medicine, University of Alabama at Birmingham, Birmingham, AL 35294, USA
    J Exp Med 201:1407-19. 2005
    ..Despite remarkable evolutionary diversity among primate lentiviruses, functional constraints on receptor binding create opportunities for broad humoral immune recognition, which in turn serves to constrain the viral quasispecies...
  86. pmc Combinatorial optimization of a CD4-mimetic miniprotein and cocrystal structures with HIV-1 gp120 envelope glycoprotein
    Francois Stricher
    CEA, iBiTecS, SIMOPRO, Gif Sur Yvette F 91191, France
    J Mol Biol 382:510-24. 2008
    ....
  87. pmc Replication-competent variants of human immunodeficiency virus type 2 lacking the V3 loop exhibit resistance to chemokine receptor antagonists
    George Lin
    Department of Medicine, University of Pennsylvania, 421 Curie Blvd, Philadelphia, PA 19104, USA
    J Virol 81:9956-66. 2007
    ..Such minimized Envs may be useful in understanding Env function, screening for new inhibitors of gp120 core interactions with chemokine receptors, and designing novel immunogens for vaccines...
  88. pmc The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120
    Rogier W Sanders
    Dept of Microbiology and Immunology, Weill Medical College of Cornell University, New York, NY 10021, USA
    J Virol 76:7293-305. 2002
    ....
  89. ncbi request reprint The 447-52D antibody: hitting HIV-1 where its armor is thickest
    Peter D Kwong
    Structure 12:173-4. 2004