Research Topics
| Peter D KwongSummaryAffiliation: National Institutes of Health Country: USA Publications
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Detail Information
Publications
Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritinXinzhen 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...
Human immunodeficiency virus: refolding the envelopePeter D Kwong
Nature 433:815-6. 2005
Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogeniesPeter 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...
Structural basis for broad detection of genogroup II noroviruses by a monoclonal antibody that binds to a site occluded in the viral particleGrant 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...
HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sitesPeter 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...
HIV-1 and influenza antibodies: seeing antigens in new waysPeter 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...
Vaccine design reaches the atomic levelPeter 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...
Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1Xueling 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...
Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120Lei 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...
Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01Tongqing 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...
Structure-based stabilization of HIV-1 gp120 enhances humoral immune responses to the induced co-receptor binding siteBarna 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...
Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4Chih 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....
Structure of a V3-containing HIV-1 gp120 coreChih 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...
Crystal structure of PG16 and chimeric dissection with somatically related PG9: structure-function analysis of two quaternary-specific antibodies that effectively neutralize HIV-1Marie 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...
Tyrosine-sulfate isosteres of CCR5 N-terminus as tools for studying HIV-1 entrySon 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....
Characterization of human immunodeficiency virus type 1 monomeric and trimeric gp120 glycoproteins stabilized in the CD4-bound state: antigenicity, biophysics, and immunogenicityBarna 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...
Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9Jason 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...
Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencingXueling Wu
Vaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA
Science 333:1593-602. 2011....
Enhanced exposure of the CD4-binding site to neutralizing antibodies by structural design of a membrane-anchored human immunodeficiency virus type 1 gp120 domainLan 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...
Structural basis for norovirus inhibition and fucose mimicry by citrateGrant 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...
Local conformational stability of HIV-1 gp120 in unliganded and CD4-bound states as defined by amide hydrogen/deuterium exchangeLeopold 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...
Structure of a major antigenic site on the respiratory syncytial virus fusion glycoprotein in complex with neutralizing antibody 101FJason 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...
Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobilityMarie 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....
Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loopsYoung 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...
Structural definition of a conserved neutralization epitope on HIV-1 gp120Tongqing 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...
Immunotypes of a quaternary site of HIV-1 vulnerability and their recognition by antibodiesXueling 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...
Relationship between antibody 2F5 neutralization of HIV-1 and hydrophobicity of its heavy chain third complementarity-determining regionGilad 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...
Mechanism of human immunodeficiency virus type 1 resistance to monoclonal antibody B12 that effectively targets the site of CD4 attachmentXueling Wu
Vaccine Research Center, NIAID, NIH, 40 Convent Dr, Bethesda, MD 20892, USA
J Virol 83:10892-907. 2009....
Crystal structure of human antibody 2909 reveals conserved features of quaternary structure-specific antibodies that potently neutralize HIV-1Anita Changela
Vaccine Research Center, NIAID NIH, 40 Convent Drive, Building 40, Room 4508, Bethesda, MD 20892 3027, USA
J Virol 85:2524-35. 2011....
Structure-Based Stabilization of HIV-1 gp120 Enhances Humoral Immune Responses to the Induced Co-Receptor Binding SiteBarna 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...
Peptides from second extracellular loop of C-C chemokine receptor type 5 (CCR5) inhibit diverse strains of HIV-1Cajetan 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...
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 vulnerabilityGrant 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...
Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitopeGilad 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...
Scorpion-toxin mimics of CD4 in complex with human immunodeficiency virus gp120 crystal structures, molecular mimicry, and neutralization breadthChih Chin Huang
Vaccine Research Center, National Institutes of Health, Bethesda, Maryland 20892, USA
Structure 13:755-68. 2005....
Design and characterization of epitope-scaffold immunogens that present the motavizumab epitope from respiratory syncytial virusJason 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....
Progress in the rational design of an AIDS vaccineGary 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....
Elicitation of structure-specific antibodies by epitope scaffoldsGilad 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...
Structure of respiratory syncytial virus fusion glycoprotein in the postfusion conformation reveals preservation of neutralizing epitopesJason 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...
A short segment of the HIV-1 gp120 V1/V2 region is a major determinant of resistance to V1/V2 neutralizing antibodiesNicole 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....
Broad and potent neutralization of HIV-1 by a gp41-specific human antibodyJinghe 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...
Structural basis of respiratory syncytial virus neutralization by motavizumabJason 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...
Heterologous epitope-scaffold prime:boosting immuno-focuses B cell responses to the HIV-1 gp41 2F5 neutralization determinantJavier 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...
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 analysisMarie 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...
Structural basis of tyrosine sulfation and VH-gene usage in antibodies that recognize the HIV type 1 coreceptor-binding site on gp120Chih-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...
Somatic Populations of PGT135-137 HIV-1-Neutralizing Antibodies Identified by 454 Pyrosequencing and BioinformaticsJiang 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...
Mining the B cell repertoire for broadly neutralizing monoclonal antibodies to HIV-1Peter D Kwong
Vaccine Research Center, NIAID, National Institutes of Health, Bethesda, MD 20892, USA
Cell Host Microbe 6:292-4. 2009....
The changing face of HIV vaccine researchPeter 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...
Computational prediction of N-linked glycosylation incorporating structural properties and patternsGwo 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...
Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopyMallika 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....
Structure-based identification and neutralization mechanism of tyrosine sulfate mimetics that inhibit HIV-1 entryPriyamvada 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....
The rational design of an AIDS vaccineDaniel 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...
Interfacial metal and antibody recognitionTongqing 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...
Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: implications for viral entry and immunogenicityChantelle 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...
Mammalian expression of isotopically labeled proteins for NMR spectroscopyMallika 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...
Rational design of vaccines to elicit broadly neutralizing antibodies to HIV-1Peter 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....
Rational design of vaccines to elicit broadly neutralizing antibodies to HIV-1Peter 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....
Rational design of vaccines to elicit broadly neutralizing antibodies to HIV-1Peter 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....
Rational design of vaccines to elicit broadly neutralizing antibodies to HIV-1Peter 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....
Enhancing protein crystallization through precipitant synergyShahzad 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...
The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120Rogier W Sanders
Dept of Microbiology and Immunology, Weill Medical College of Cornell University, New York, NY 10021, USA
J Virol 76:7293-305. 2002....
Replication-competent variants of human immunodeficiency virus type 2 lacking the V3 loop exhibit resistance to chemokine receptor antagonistsGeorge 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...
Antigenic conservation and immunogenicity of the HIV coreceptor binding siteJulie 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...
Structure-activity relationships in the binding of chemically derivatized CD4 to gp120 from human immunodeficiency virusHui 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...
Combinatorial optimization of a CD4-mimetic miniprotein and cocrystal structures with HIV-1 gp120 envelope glycoproteinFrancois Stricher
CEA, iBiTecS, SIMOPRO, Gif Sur Yvette F 91191, France
J Mol Biol 382:510-24. 2008....
Mutagenic stabilization and/or disruption of a CD4-bound state reveals distinct conformations of the human immunodeficiency virus type 1 gp120 envelope glycoproteinShi 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...
Antibody neutralization and escape by HIV-1Xiping 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...
Epitope mapping and characterization of a novel CD4-induced human monoclonal antibody capable of neutralizing primary HIV-1 strainsShi 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...
Tyrosine sulfation of human antibodies contributes to recognition of the CCR5 binding region of HIV-1 gp120Hyeryun 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...
Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognitionMarkus 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...
HIV vaccine design and the neutralizing antibody problemDennis R Burton
Departments of Immunology and Molecular Biology, Scripps Research Institute, La Jolla, California, USA
Nat Immunol 5:233-6. 2004
Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1Aran 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...
The 447-52D antibody: hitting HIV-1 where its armor is thickestPeter D Kwong
Structure 12:173-4. 2004
