Evidence map›Paper›PMID 33084569›Full record

ArticleeLife2020

A broadly neutralizing macaque monoclonal antibody against the HIV-1 V3-Glycan patch.

Zijun Wang, Christopher O Barnes, Rajeev Gautam, Julio C Cetrulo Lorenzi, Christian T Mayer, Thiago Y Oliveira, Victor Ramos, Melissa Cipolla, Kristie M Gordon, Harry B Gristick and 9 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. 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
1.5field-weighted citation impact, top 18% 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, 18 citations in OpenAlex.

  1. Article
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  5. Article
  6. Gene Editing of Primary Rhesus Macaque B Cells.Journal of visualized experiments : JoVE · 2023
    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

19 authors at 5 institutions in 1 country.

Zijun Wang *Laboratory of Molecular Immunology, The Rockefeller University, New York, United States.
Christopher O Barnes *Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
Rajeev Gautam *Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, United States.
Julio C Cetrulo LorenziLaboratory of Molecular Immunology, The Rockefeller University, New York, United States.
Christian T MayerLaboratory of Molecular Immunology, The Rockefeller University, New York, United States.
Thiago Y OliveiraLaboratory of Molecular Immunology, The Rockefeller University, New York, United States.
Victor RamosLaboratory of Molecular Immunology, The Rockefeller University, New York, United States.ORCID 0000-0001-7353-3420
Melissa CipollaLaboratory of Molecular Immunology, The Rockefeller University, New York, United States.
Kristie M GordonLaboratory of Molecular Immunology, The Rockefeller University, New York, United States.
Harry B GristickDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
Anthony P WestDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
Yoshiaki NishimuraLaboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, United States.
Henna RainaLaboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, United States.
Michael S SeamanCenter for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Boston, United States.
Anna GazumyanLaboratory of Molecular Immunology, The Rockefeller University, New York, United States.
Malcolm MartinLaboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, United States.
Pamela J BjorkmanDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.ORCID 0000-0002-2277-3990
Michel C NussenzweigLaboratory of Molecular Immunology, The Rockefeller University, New York, United States.
Amelia EscolanoLaboratory of Molecular Immunology, The Rockefeller University, New York, United States.ORCID 0000-0002-1945-2440
Rockefeller University · USCalifornia Institute of Technology · USNational Institutes of Health · USBeth Israel Deaconess Medical Center · USHoward Hughes Medical Institute · US

Funding

Support Component D/Vaccine Discovery, Concept to ClinicUM1AI100663 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI BAROUCH, DAN H. · 2012 to 2018
$131.5M
Virus & Reservoirs CoreP30AI045008 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI ROBERT GROSS · 1999 to 2026
$78.6M
Stuctural basis of bNab activityP01AI100148 · NIAID · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI Pamela J Bjorkman · 2013 to 2026
$43.3M
NIAID NIH HHS P01 AI100148NIAID NIH HHS P30 AI045008NIAID NIH HHS UM1 AI100663
6 · The paper itself

Abstract

A small fraction of HIV-1- infected humans develop broadly neutralizing antibodies (bNAbs) against HIV-1 that protect macaques from simian immunodeficiency HIV chimeric virus (SHIV). Similarly, a small number of macaques infected with SHIVs develop broadly neutralizing serologic activity, but less is known about the nature of simian antibodies. Here, we report on a monoclonal antibody, Ab1485, isolated from a macaque infected with SHIVAD8 that developed broadly neutralizing serologic activity targeting the V3-glycan region of HIV-1 Env. Ab1485 neutralizes 38.1% of HIV-1 isolates in a 42-pseudovirus panel with a geometric mean IC50 of 0.055 µg/mLl and SHIVAD8 with an IC50 of 0.028 µg/mLl. Ab1485 binds the V3-glycan epitope in a glycan-dependent manner. A 3.5 Å cryo-electron microscopy structure of Ab1485 in complex with a native-like SOSIP Env trimer showed conserved contacts with the N332gp120 glycan and gp120 GDIR peptide motif, but in a distinct Env-binding orientation relative to human V3/N332gp120 glycan-targeting bNAbs. Intravenous infusion of Ab1485 protected macaques from a high dose challenge with SHIVAD8. We conclude that macaques can develop bNAbs against the V3-glycan patch that resemble human V3-glycan bNAbs.

Indexed as

AIDS VaccinesAnimalsAntibodies, MonoclonalBroadly Neutralizing AntibodiesFemaleHIV-1HIV Envelope Protein gp120HIV InfectionsMacaca mulattaPeptide FragmentsPolysaccharidesAIDS VaccinesAntibodies, MonoclonalBroadly Neutralizing AntibodiesHIV Envelope Protein gp120HIV envelope protein gp120 (305-321)Peptide FragmentsPolysaccharidesantibodyanti hiv-1broadly neutralizingimmunologyinfectious diseaseinflammationmicrobiologypatch antibodyrhesus macaquev3 glycan

Identifiers

PMID33084569
PMCPMC7577740
OpenAlexW3094063449

What OpenQuestion holds

Textmetadata
LicenceCC0
Read underepoch 390

Registered trials

None linked

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.