ArticleNature2014
Broad and potent HIV-1 neutralization by a human antibody that binds the gp41-gp120 interface.
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In one paragraph
Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 318 papers, 1 of them a synthesis that pooled it.
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318citing papers in PubMed, 1 pooled it
30.0field-weighted citation impact, top 1% of its field
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The trial behind it
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Who cites it
318 citing papers in PubMed, 1 synthesis or guideline pooled it, 431 citations in OpenAlex.
- Employing Broadly Neutralizing Antibodies as a Human Immunodeficiency Virus Prophylactic & Therapeutic Application.Frontiers in immunology · 2021Pooled it
- Detection and activation of HIV broadly neutralizing antibody precursor B cells using anti-idiotypes.The Journal of experimental medicine · 2019Trial
- Cross Type Neutralizing Antibodies Detected in a Unique HIV-2 Infected Individual From India.Frontiers in immunology · 2018Trial
- Broad and potent cross clade neutralizing antibodies with multiple specificities in the plasma of HIV-1 subtype C infected individuals.Scientific reports · 2017Trial
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- Non-integrase mechanisms for dolutegravir resistance.Retrovirology · 2026Review
- N-Glycans modulate tilting of HIV-1 envelope glycoprotein.Nature communications · 2026Article
- Vaccine elicitation of HIV-1 neutralizing antibodies against both V2 apex and fusion peptide in rhesus macaques.Cell reports · 2026Article
- Conformational landscape of HIV-1 Env from closed to fully open.Nature communications · 2026Article
- Virus glycoprotein nanodisc platform for vaccine analytics.Nature communications · 2026Article
- Functional Convergence of Genetically Diverse B-Cell Receptors in Simian-HIV Infected Rhesus Macaques.bioRxiv : the preprint server for biology · 2026Article
- The HIV-1 envelope glycoprotein: structure, function and interactions with neutralizing antibodies.Nature reviews. Microbiology · 2025Review
- Vaccine Elicitation of HIV-1 Neutralizing Antibodies Against Both V2 Apex and Fusion Peptide in Rhesus Macaques.bioRxiv : the preprint server for biology · 2025Article
- Parallel evolution of the elite neutralizer phenotype in divergent HIV-1 clades.Journal of virology · 2025Article
- A comprehensive engineering strategy improves potency and manufacturability of a near pan-neutralizing antibody against HIV.Structure (London, England : 1993) · 2025Article
- Identification and characterization of a broadly neutralizing and protective nanobody against the HA1 domain of H5 avian influenza virus hemagglutinin.Journal of virology · 2025Article
- Afucosylated broadly neutralizing antibodies targeting the HIV envelope elicit enhanced NK-cell-mediated cytotoxicity against HIV-infected CD4+ T-cell and macrophage targets.Journal of leukocyte biology · 2025Article
- Incompletely closed HIV-1Npj viruses · 2025Article
258 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
29 authors at 8 institutions in 2 countries.
Jinghe HuangLaboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
Byong H KangLaboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
Marie PanceraVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
Jeong Hyun Lee1] The Scripps Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, The Scripps Research Institute, La Jolla, California 92037, USA [2] International AIDS Vaccine Initiative (IAVI) Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, California 92037, USA.
Tommy TongSan Diego Biomedical Research Institute, San Diego, California 92121, USA.
Yu FengInternational AIDS Vaccine Initiative (IAVI) Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, California 92037, USA.
Hiromi ImamichiLaboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
Ivelin S GeorgievVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
Gwo-Yu ChuangVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
Aliaksandr DruzVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
Nicole A Doria-RoseVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
Leo LaubLaboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
Kwinten SliepenDepartment of Medical Microbiology, Academic Medical Center, University of Amsterdam, Amsterdam 1100 DD, The Netherlands.
Marit J van GilsDepartment of Medical Microbiology, Academic Medical Center, University of Amsterdam, Amsterdam 1100 DD, The Netherlands.
Alba Torrents de la PeñaDepartment of Medical Microbiology, Academic Medical Center, University of Amsterdam, Amsterdam 1100 DD, The Netherlands.
Ronald DerkingDepartment of Medical Microbiology, Academic Medical Center, University of Amsterdam, Amsterdam 1100 DD, The Netherlands.
Per-Johan KlasseDepartment of Microbiology and Immunology, Weill Medical College of Cornell University, New York, New York 10065, USA.
Stephen A MiguelesLaboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
Robert T BailerVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
Munir AlamDuke Human Vaccine Institute, Duke University, Durham, North Carolina 27710, USA.
Pavel PugachDepartment of Microbiology and Immunology, Weill Medical College of Cornell University, New York, New York 10065, USA.
Barton F HaynesDuke Human Vaccine Institute, Duke University, Durham, North Carolina 27710, USA.
Richard T Wyatt1] The Scripps Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, The Scripps Research Institute, La Jolla, California 92037, USA [2] International AIDS Vaccine Initiative (IAVI) Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, California 92037, USA.
Rogier W Sanders1] Department of Medical Microbiology, Academic Medical Center, University of Amsterdam, Amsterdam 1100 DD, The Netherlands [2] Department of Microbiology and Immunology, Weill Medical College of Cornell University, New York, New York 10065, USA.
James M BinleySan Diego Biomedical Research Institute, San Diego, California 92121, USA.
Andrew B Ward1] The Scripps Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, The Scripps Research Institute, La Jolla, California 92037, USA [2] International AIDS Vaccine Initiative (IAVI) Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, California 92037, USA.
John R MascolaVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
Peter D KwongVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
Mark ConnorsLaboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
National Institute of Allergy and Infectious Diseases · USNational Institutes of Health · USScripps Research Institute · USUniversity of Amsterdam · NLAcademic Medical Center · NLCornell University · USDuke University · USSan Diego Biomedical Research Institute · US
Funding
Virus biology scientific research support componentUM1AI100645 · NIAID · DUKE UNIVERSITY · PI HAYNES, BARTON F. · 2012 to 2018
$204.7MSupport Component D/Vaccine Discovery, Concept to ClinicUM1AI100663 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI BAROUCH, DAN H. · 2012 to 2018
$131.5MNeutralization Mechanisms Of Anti-HIV-1 Monoclonal AntibodiesZIAAI005022 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI ZHOU, TONGQING · 2009 to 2025
$24.6MMechanisms Of Immune Mediated Restriction Of HIV Replication In LTNPZIAAI000855 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI CONNORS, MARK · 2009 to 2025
$20.0MMechanisms Of Humoral EvasionZIAAI005023 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI ZHOU, TONGQING · 2009 to 2025
$18.6MTrimer Production and Immunogenicity TestingP01AI082362 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI MOORE, JOHN P · 2009 to 2014
$16.0MMechanisms of Effective Humoral Immune Responses to HIV-1ZIAAI001090 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI CONNORS, MARK · 2009 to 2025
$14.8MPure and Authentic HIV-1 Env ImmunogensR01AI093278 · NIAID · TORREY PINES INST FOR MOLECULAR STUDIES · PI BINLEY, JAMES M · 2011 to 2024
$11.6MDetermination of the Neutralization Specificity in Broadly Neutralizing HIV SeraZIAAI005089 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI MASCOLA, JOHN · 2009 to 2018
$9.6MDesign of Antigenically-Specific Probes for Sera Analysis and MAb IsolationZICAI005111 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI ZHOU, TONGQING · 2010 to 2025
$4.3MRescue of broadly neutralizing mAbs using native trimerR01AI100790 · NIAID · TORREY PINES INST FOR MOLECULAR STUDIES · PI BINLEY, JAMES M · 2012 to 2016
$2.3MStabilizing HIV-1 Trimers by Linking gp120 SubunitsR33AI084714 · NIAID · TORREY PINES INST FOR MOLECULAR STUDIES · PI BINLEY, JAMES M · 2012 to 2014
$957kEuropean Research Council 280829Intramural NIH HHS ZIA AI000855Intramural NIH HHS ZIA AI001090NIAID NIH HHS AI84714NIAID NIH HHS AI93278NIAID NIH HHS P01 AI082362NIAID NIH HHS R01 AI093278NIAID NIH HHS R01 AI100790NIAID NIH HHS R21 AI084714NIAID NIH HHS R33 AI084714NIAID NIH HHS UM1 AI100645NIAID NIH HHS UM1 AI100663
Abstract
The isolation of human monoclonal antibodies is providing important insights into the specificities that underlie broad neutralization of HIV-1 (reviewed in ref. 1). Here we report a broad and extremely potent HIV-specific monoclonal antibody, termed 35O22, which binds a novel HIV-1 envelope glycoprotein (Env) epitope. 35O22 neutralized 62% of 181 pseudoviruses with a half-maximum inhibitory concentration (IC50) <50 μg ml(-1). The median IC50 of neutralized viruses was 0.033 μg ml(-1), among the most potent thus far described. 35O22 did not bind monomeric forms of Env tested, but did bind the trimeric BG505 SOSIP.664. Mutagenesis and a reconstruction by negative-stain electron microscopy of the Fab in complex with trimer revealed that it bound to a conserved epitope, which stretched across gp120 and gp41. The specificity of 35O22 represents a novel site of vulnerability on HIV Env, which serum analysis indicates to be commonly elicited by natural infection. Binding to this new site of vulnerability may thus be an important complement to current monoclonal-antibody-based approaches to immunotherapies, prophylaxis and vaccine design.
Indexed as
Antibody AffinityAIDS VaccinesAntibodies, MonoclonalAntibodies, NeutralizingAntibody SpecificityCD4 AntigensCell LineCell MembraneConserved SequenceEpitope MappingEpitopesHIV-1HIV AntibodiesHIV Envelope Protein gp120HIV Envelope Protein gp41HumansAIDS VaccinesAntibodies, MonoclonalAntibodies, NeutralizingCD4 AntigensEpitopesHIV AntibodiesHIV Envelope Protein gp120HIV Envelope Protein gp41Immunoglobulin Fab FragmentsReceptors, CCR5
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.