Evidence map›Paper›PMID 37436899›Full record

ArticleCell reports2023

HIV-1 neutralizing antibodies elicited in humans by a prefusion-stabilized envelope trimer form a reproducible class targeting fusion peptide.

Shuishu Wang, Flavio Matassoli, Baoshan Zhang, Tracy Liu, Chen-Hsiang Shen, Tatsiana Bylund, Timothy Johnston, Amy R Henry, I-Ting Teng, Prabhanshu Tripathi and 26 more

Open access · goldAbstract readClinical Trial, Phase I
In one paragraph

Article in Cell reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.4field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 17 citations in OpenAlex.

  1. Trial
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  4. Review
  5. Article
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  8. Review
  9. Ultrapotent Broadly Neutralizing Human-llama Bispecific Antibodies against HIV-1.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  10. Article
  11. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

36 authors at 3 institutions in 1 country.

Shuishu WangVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Flavio MatassoliVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Baoshan ZhangVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Tracy LiuVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Chen-Hsiang ShenVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Tatsiana BylundVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Timothy JohnstonVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Amy R HenryVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
I-Ting TengVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Prabhanshu TripathiVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Jordan E BeckerZuckerman Mind Brain Behavior Institute, Columbia University, New York, NY 10027, USA; Department of Biochemistry and Molecular Biophysics, Columbia University Vagelos College of Physicians and Surgeons, New York, NY 10032, USA.
Anita ChangelaVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Ridhi ChaudharyVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Cheng ChengVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Martin GaudinskiVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Jason GormanVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Darcy R HarrisVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Myungjin LeeVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Nicholas C MoranoZuckerman Mind Brain Behavior Institute, Columbia University, New York, NY 10027, USA; Department of Biochemistry and Molecular Biophysics, Columbia University Vagelos College of Physicians and Surgeons, New York, NY 10032, USA.
Laura NovikVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Sijy O'DellVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Adam S OliaVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Danealle K ParchmentVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Reda RawiVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Jesmine Roberts-TorresVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Tyler StephensElectron Microscopy Laboratory, Cancer Research Technology Program, Frederick National Laboratory for Cancer Research, Frederick, MD 21701, USA.
Yaroslav TsybovskyElectron Microscopy Laboratory, Cancer Research Technology Program, Frederick National Laboratory for Cancer Research, Frederick, MD 21701, USA.
Danyi WangVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
David J Van WazerVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Tongqing ZhouVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Nicole A Doria-RoseVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Richard A KoupVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Lawrence ShapiroZuckerman Mind Brain Behavior Institute, Columbia University, New York, NY 10027, USA; Department of Biochemistry and Molecular Biophysics, Columbia University Vagelos College of Physicians and Surgeons, New York, NY 10032, USA.
Daniel C DouekVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Adrian B McDermottVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.
Peter D KwongVaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA; Department of Biochemistry and Molecular Biophysics, Columbia University Vagelos College of Physicians and Surgeons, New York, NY 10032, USA. Electronic address: pdkwong@nih.gov.
National Institutes of Health · USColumbia University · USFrederick National Laboratory for Cancer Research · US

Funding

Vaccine Immunology ProgramZIAAI005143 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI KOUP, RICHARD A · 2019 to 2025
$51.8M
Neutralization Mechanisms Of Anti-HIV-1 Monoclonal AntibodiesZIAAI005022 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI ZHOU, TONGQING · 2009 to 2025
$24.6M
HIV/AIDS Vaccine and Antibody DevelopmentZICAI005002 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI CHENG, CHENG · 2019 to 2025
$17.6M
The Genome Analysis CoreZICAI005133 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI DOUEK, DANIEL CESAR · 2019 to 2025
$16.9M
Design of Antigenically-Specific Probes for Sera Analysis and MAb IsolationZICAI005111 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI ZHOU, TONGQING · 2010 to 2025
$4.3M
Computational Tools for Structural AnalysisZICAI005112 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI RAWI, REDA · 2010 to 2025
$4.1M
CCR NIH HHS HHSN261200800001CIntramural NIH HHS ZIA AI005022NCI NIH HHS HHSN261200800001E
6 · The paper itself

Abstract

Elicitation of antibodies that neutralize the tier-2 neutralization-resistant isolates that typify HIV-1 transmission has been a long-sought goal. Success with prefusion-stabilized envelope trimers eliciting autologous neutralizing antibodies has been reported in multiple vaccine-test species, though not in humans. To investigate elicitation of HIV-1 neutralizing antibodies in humans, here, we analyze B cells from a phase I clinical trial of the "DS-SOSIP"-stabilized envelope trimer from strain BG505, identifying two antibodies, N751-2C06.01 and N751-2C09.01 (named for donor-lineage.clone), that neutralize the autologous tier-2 strain, BG505. Though derived from distinct lineages, these antibodies form a reproducible antibody class that targets the HIV-1 fusion peptide. Both antibodies are highly strain specific, which we attribute to their partial recognition of a BG505-specific glycan hole and to their binding requirements for a few BG505-specific residues. Prefusion-stabilized envelope trimers can thus elicit autologous tier-2 neutralizing antibodies in humans, with initially identified neutralizing antibodies recognizing the fusion-peptide site of vulnerability.

Indexed as

AIDS VaccinesHIV-1HIV InfectionsHIV SeropositivityAntibodies, Neutralizingenv Gene Products, Human Immunodeficiency VirusHIV AntibodiesHumansPeptidesAIDS VaccinesAntibodies, Neutralizingenv Gene Products, Human Immunodeficiency VirusHIV AntibodiesPeptidesantibody-antigen bindingCP: Immunologycryo-EM structureenvelope trimerfusion peptideglycan holeHIV vaccineimmunogen designreproducible antibody classsite of vulnerability

Identifiers

PMID37436899
PMCPMC10491024
OpenAlexW4383912798

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LicenceCC BY
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Registered trials

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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.