Evidence map›Paper›PMID 34373853›Full record

ArticlebioRxiv : the preprint server for biology2021

Structural Basis and Mode of Action for Two Broadly Neutralizing Antibodies Against SARS-CoV-2 Emerging Variants of Concern.

Wenwei Li, Yaozong Chen, Jérémie Prévost, Irfan Ullah, Maolin Lu, Shang Yu Gong, Alexandra Tauzin, Romain Gasser, Dani Vézina, Sai Priya Anand and 20 more

Open access · greenAbstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed, 22 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

30 authors at 6 institutions in 2 countries.

Wenwei Li *Department of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT, USA.
Yaozong Chen *Infectious Disease Division, Department of Medicine, Uniformed Services University of the Health Sciences, Bethesda, MD 20814-4712, USA.
Jérémie Prévost *Centre de Recherche du CHUM (CRCHUM), Montreal, QC H2X 0A9, Canada.
Irfan UllahDepartment of Internal Medicine, Section of Infectious Diseases, Yale University School of Medicine, New Haven, CT 06520.
Maolin LuDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT, USA.
Shang Yu GongCentre de Recherche du CHUM (CRCHUM), Montreal, QC H2X 0A9, Canada.
Alexandra TauzinCentre de Recherche du CHUM (CRCHUM), Montreal, QC H2X 0A9, Canada.
Romain GasserCentre de Recherche du CHUM (CRCHUM), Montreal, QC H2X 0A9, Canada.
Dani VézinaCentre de Recherche du CHUM (CRCHUM), Montreal, QC H2X 0A9, Canada.
Sai Priya AnandCentre de Recherche du CHUM (CRCHUM), Montreal, QC H2X 0A9, Canada.
Guillaume GoyetteCentre de Recherche du CHUM (CRCHUM), Montreal, QC H2X 0A9, Canada.
Debashree ChaterjeeCentre de Recherche du CHUM (CRCHUM), Montreal, QC H2X 0A9, Canada.
Shilei DingCentre de Recherche du CHUM (CRCHUM), Montreal, QC H2X 0A9, Canada.
William D TolbertInfectious Disease Division, Department of Medicine, Uniformed Services University of the Health Sciences, Bethesda, MD 20814-4712, USA.
Michael W GrunstDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT, USA.
Yuxia BoDepartment of Biochemistry, Microbiology and Immunology, and Center for Infection, Immunity, and Inflammation, University of Ottawa, Ottawa, ON K1H 8M5, Canada.
Shijian ZhangDepartment of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Boston, MA, USA.
Jonathan RichardCentre de Recherche du CHUM (CRCHUM), Montreal, QC H2X 0A9, Canada.
Fei ZhouLaboratory of Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Rick K HuangLaboratory of Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Lothar EsserLaboratory of Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Allison ZeherLaboratory of Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Marceline CôtéDepartment of Biochemistry, Microbiology and Immunology, and Center for Infection, Immunity, and Inflammation, University of Ottawa, Ottawa, ON K1H 8M5, Canada.
Priti KumarDepartment of Internal Medicine, Section of Infectious Diseases, Yale University School of Medicine, New Haven, CT 06520.
Joseph SodroskiDepartment of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Boston, MA, USA.
Di XiaLaboratory of Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Pradeep D UchilDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT, USA.
Marzena PazgierInfectious Disease Division, Department of Medicine, Uniformed Services University of the Health Sciences, Bethesda, MD 20814-4712, USA.
Andrés FinziCentre de Recherche du CHUM (CRCHUM), Montreal, QC H2X 0A9, Canada.
Walther MothesDepartment of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT, USA.
Centre Hospitalier de l’Université de Montréal · CAYale University · USNational Institutes of Health · USUniformed Services University of the Health Sciences · USHarvard University · USUniversity of Ottawa · CA

Funding

Structure and Dynamics of the SARS-CoV-2 Spike ProteinR01AI163395 · NIAID · YALE UNIVERSITY · PI MOTHES, WALTHER H · 2021 to 2025
$4.1M
Predoctoral Training Program in VirologyT32AI055403 · NIAID · YALE UNIVERSITY · PI KUMAR, PRITI, MOTHES, WALTHER H · 2003 to 2024
$3.6M
NIAID NIH HHS R01 AI163395NIAID NIH HHS T32 AI055403
6 · The paper itself

Abstract

Emerging variants of concern for the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) can transmit more efficiently and partially evade protective immune responses, thus necessitating continued refinement of antibody therapies and immunogen design. Here we elucidate the structural basis and mode of action for two potent SARS-CoV-2 Spike (S) neutralizing monoclonal antibodies CV3-1 and CV3-25 that remained effective against emerging variants of concern in vitro and in vivo. CV3-1 bound to the (485-GFN-487) loop within the receptor-binding domain (RBD) in the "RBD-up" position and triggered potent shedding of the S1 subunit. In contrast, CV3-25 inhibited membrane fusion by binding to an epitope in the stem helix region of the S2 subunit that is highly conserved among β-coronaviruses. Thus, vaccine immunogen designs that incorporate the conserved regions in RBD and stem helix region are candidates to elicit pan-coronavirus protective immune responses.

Identifiers

PMID34373853
PMCPMC8351775
OpenAlexW3190857325

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.