Evidence map›Paper›PMID 39488210›Full record

ArticleImmunity2024

Isolation and escape mapping of broadly neutralizing antibodies against emerging delta-coronaviruses.

Megi Rexhepaj, Daniel Asarnow, Lisa Perruzza, Young-Jun Park, Barbara Guarino, Mathew Mccallum, Katja Culap, Christian Saliba, Giada Leoni, Alessio Balmelli and 11 more

Abstract read
In one paragraph

Article in Immunity, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Computational design of an ultrapotent deltacoronavirus miniprotein inhibitor.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. TMPRSS2-mediated coronavirus spike activation and inhibition.Nature structural & molecular biology · 2026
    Article
  6. Cell entry mechanisms of porcine enteric coronaviruses.The Journal of biological chemistry · 2026
    Review
  7. Article
  8. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

21 authors.

Megi RexhepajDepartment of Biochemistry, University of Washington, Seattle, WA, USA.
Daniel AsarnowDepartment of Biochemistry, University of Washington, Seattle, WA, USA.
Lisa PerruzzaHumabs Biomed SA, a Subsidiary of Vir. Biotechnology, 6500 Bellinzona, Switzerland.
Young-Jun ParkDepartment of Biochemistry, University of Washington, Seattle, WA, USA; Howard Hughes Medical Institute, Seattle, WA 98195, USA.
Barbara GuarinoHumabs Biomed SA, a Subsidiary of Vir. Biotechnology, 6500 Bellinzona, Switzerland.
Mathew MccallumDepartment of Biochemistry, University of Washington, Seattle, WA, USA.
Katja CulapHumabs Biomed SA, a Subsidiary of Vir. Biotechnology, 6500 Bellinzona, Switzerland.
Christian SalibaHumabs Biomed SA, a Subsidiary of Vir. Biotechnology, 6500 Bellinzona, Switzerland.
Giada LeoniHumabs Biomed SA, a Subsidiary of Vir. Biotechnology, 6500 Bellinzona, Switzerland.
Alessio BalmelliHumabs Biomed SA, a Subsidiary of Vir. Biotechnology, 6500 Bellinzona, Switzerland.
Courtney N YoshiyamaDepartment of Biochemistry, University of Washington, Seattle, WA, USA.
Miles S DickinsonDepartment of Biochemistry, University of Washington, Seattle, WA, USA.
Joel QuispeDepartment of Biochemistry, University of Washington, Seattle, WA, USA.
Jack T BrownDepartment of Biochemistry, University of Washington, Seattle, WA, USA.
M Alejandra TortoriciDepartment of Biochemistry, University of Washington, Seattle, WA, USA; Howard Hughes Medical Institute, Seattle, WA 98195, USA.
Kaitlin R SprouseDepartment of Biochemistry, University of Washington, Seattle, WA, USA; Howard Hughes Medical Institute, Seattle, WA 98195, USA.
Ashley L TaylorDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112, USA.
Davide CortiHumabs Biomed SA, a Subsidiary of Vir. Biotechnology, 6500 Bellinzona, Switzerland.
Tyler N StarrDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112, USA. Electronic address: tyler.starr@biochem.utah.edu.
Fabio BenigniHumabs Biomed SA, a Subsidiary of Vir. Biotechnology, 6500 Bellinzona, Switzerland. Electronic address: fbenigni@vir.bio.
David VeeslerDepartment of Biochemistry, University of Washington, Seattle, WA, USA; Howard Hughes Medical Institute, Seattle, WA 98195, USA. Electronic address: dveesler@uw.edu.

Funding

Centers for Research on Structural Biology of Infectious Diseases: Universal Influenza Vaccine Research75N93022C00036 · NIAID · SEATTLE CHILDREN'S HOSPITAL · PI STAKER, BART · 2022 to 2025
$21.7M
Structure-based design of broadly protective coronavirus vaccinesP01AI167966 · NIAID · UNIVERSITY OF WASHINGTON · PI Francois J Villinger · 2022 to 2026
$15.3M
Unraveling the bat humoral immune response against zoonotic viruses to guide the design of next-generation therapeuticsDP1AI158186 · NIAID · UNIVERSITY OF WASHINGTON · PI VEESLER, DAVID · 2020 to 2024
$5.4M
Acquisition of a high resolution, high throughput cryo-electron microscopeS10OD023476 · OD · UNIVERSITY OF WASHINGTON · PI KOLLMAN, JUSTIN M · 2017 to 2017
$2.0M
Howard Hughes Medical InstituteNIAID NIH HHS 75N93022C00036NIAID NIH HHS DP1 AI158186NIAID NIH HHS P01 AI167966NIH HHS S10 OD023476Wellcome Trust
6 · The paper itself

Abstract

Porcine delta-coronavirus (PDCoV) spillovers were recently detected in febrile children, underscoring the recurrent zoonoses of divergent CoVs. To date, no vaccines or specific therapeutics are approved for use in humans against PDCoV. To prepare for possible future PDCoV epidemics, we isolated PDCoV spike (S)-directed monoclonal antibodies (mAbs) from humanized mice and found that two, designated PD33 and PD41, broadly neutralized a panel of PDCoV variants. Cryoelectron microscopy (cryo-EM) structures of PD33 and PD41 in complex with the S receptor-binding domain (RBD) and ectodomain trimer revealed the epitopes recognized by these mAbs, rationalizing their broad inhibitory activity. We show that both mAbs competitively interfere with host aminopeptidase N binding to neutralize PDCoV and used deep-mutational scanning epitope mapping to associate RBD antigenic sites with mAb-mediated neutralization potency. Our results indicate a PD33-PD41 mAb cocktail may heighten the barrier to escape. PD33 and PD41 are candidates for clinical advancement against future PDCoV outbreaks.

Indexed as

Antibodies, MonoclonalAntibodies, ViralEpitope MappingSpike Glycoprotein, CoronavirusAnimalsAntibodies, NeutralizingBroadly Neutralizing AntibodiesCryoelectron MicroscopyEpitopesHumansMiceAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralBroadly Neutralizing AntibodiesEpitopesSpike Glycoprotein, Coronaviruscryo-EM structuresdeep mutational scanningneutralizing antibodiesPDCoVporcine deltacoronavirusspike glycoproteinzoonosis

Identifiers

PMID39488210
PMCPMC12279085

What OpenQuestion holds

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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.