Evidence map›Paper›PMID 39466880›Full record

ArticlePLoS pathogens2024

Delineating the functional activity of antibodies with cross-reactivity to SARS-CoV-2, SARS-CoV-1 and related sarbecoviruses.

Felicitas Ruiz, William B Foreman, Michelle Lilly, Viren A Baharani, Delphine M Depierreux, Vrasha Chohan, Ashley L Taylor, Jamie Guenthoer, Duncan Ralph, Frederick A Matsen Iv and 5 more

Abstract read
In one paragraph

Article in PLoS pathogens, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

15 authors.

Felicitas RuizHuman Biology Division, Fred Hutchinson Cancer Center, Seattle, Washington, United States of America.
William B ForemanDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, Utah, United States of America.
Michelle LillyHuman Biology Division, Fred Hutchinson Cancer Center, Seattle, Washington, United States of America.
Viren A BaharaniLaboratory of Retrovirology, The Rockefeller University, New York, New York, United States of America.
Delphine M DepierreuxHuman Biology Division, Fred Hutchinson Cancer Center, Seattle, Washington, United States of America.
Vrasha ChohanHuman Biology Division, Fred Hutchinson Cancer Center, Seattle, Washington, United States of America.
Ashley L TaylorDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, Utah, United States of America.
Jamie GuenthoerHuman Biology Division, Fred Hutchinson Cancer Center, Seattle, Washington, United States of America.
Duncan RalphPublic Health Sciences Division, Fred Hutchinson Cancer Center, Seattle, Washington, United States of America.
Frederick A Matsen IvPublic Health Sciences Division, Fred Hutchinson Cancer Center, Seattle, Washington, United States of America.
Helen Y ChuDivision of Allergy and Infectious Diseases, University of Washington, Seattle, Washington, United States of America.
Paul D BieniaszLaboratory of Retrovirology, The Rockefeller University, New York, New York, United States of America.
Marceline CôtéDepartment of Biochemistry, Microbiology and Immunology, and Centre for Infection, Immunity and Inflammation, University of Ottawa, Ottawa, Canada.
Tyler N StarrDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, Utah, United States of America.ORCID 0000-0001-6713-6904
Julie OverbaughHuman Biology Division, Fred Hutchinson Cancer Center, Seattle, Washington, United States of America.ORCID 0000-0002-0239-9444

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Jared P Rutter · 1986 to 2026
$72.6M
Structure-based design of broadly protective coronavirus vaccinesP01AI167966 · NIAID · UNIVERSITY OF WASHINGTON · PI BALI PULENDRAN · 2022 to 2026
$15.3M
The longevity and nature of the anti-SARS-CoV-2 cellular and humoral immune responsesP01AI165075 · NIAID · ROCKEFELLER UNIVERSITY · PI BJORKMAN, PAMELA J · 2022 to 2023
$10.7M
Comprehensive profiling of SARS-CoV-2 antibody responses and escape pathwaysR01AI138709 · NIAID · FRED HUTCHINSON CANCER RESEARCH CENTER · PI OVERBAUGH, JULIE M. · 2018 to 2022
$5.0M
Blending deep learning with probabilistic mechanistic models to predict and understand the evolution and function of adaptive immune receptorsR01AI146028 · NIAID · FRED HUTCHINSON CANCER RESEARCH CENTER · PI MATSEN, FREDERICK ALBERT · 2019 to 2024
$3.4M
The evolutionary landscape of HIV broadly neutralizing antibody developmentDP2AI177890 · NIAID · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Tyler Nelson Starr · 2023 to 2026
$1.8M
From genomics to natural language processing: A protected environment for research computing in the health scienceS10OD021644 · OD · UNIVERSITY OF UTAH · PI CHEATHAM, THOMAS E. · 2017 to 2017
$494k
NCI NIH HHS P30 CA042014NIAID NIH HHS DP2 AI177890NIAID NIH HHS P01 AI165075NIAID NIH HHS P01 AI167966NIAID NIH HHS R01 AI138709NIAID NIH HHS R01 AI146028NIH HHS S10 OD021644
6 · The paper itself

Abstract

The recurring spillover of pathogenic coronaviruses and demonstrated capacity of sarbecoviruses, such SARS-CoV-2, to rapidly evolve in humans underscores the need to better understand immune responses to this virus family. For this purpose, we characterized the functional breadth and potency of antibodies targeting the receptor binding domain (RBD) of the spike glycoprotein that exhibited cross-reactivity against SARS-CoV-2 variants, SARS-CoV-1 and sarbecoviruses from diverse clades and animal origins with spillover potential. One neutralizing antibody, C68.61, showed remarkable neutralization breadth against both SARS-CoV-2 variants and viruses from different sarbecovirus clades. C68.61, which targets a conserved RBD class 5 epitope, did not select for escape variants of SARS-CoV-2 or SARS-CoV-1 in culture nor have predicted escape variants among circulating SARS-CoV-2 strains, suggesting this epitope is functionally constrained. We identified 11 additional SARS-CoV-2/SARS-CoV-1 cross-reactive antibodies that target the more sequence conserved class 4 and class 5 epitopes within RBD that show activity against a subset of diverse sarbecoviruses with one antibody binding every single sarbecovirus RBD tested. A subset of these antibodies exhibited Fc-mediated effector functions as potent as antibodies that impact infection outcome in animal models. Thus, our study identified antibodies targeting conserved regions across SARS-CoV-2 variants and sarbecoviruses that may serve as therapeutics for pandemic preparedness as well as blueprints for the design of immunogens capable of eliciting cross-neutralizing responses.

Indexed as

Antibodies, NeutralizingAntibodies, ViralCOVID-19Cross ReactionsSARS-CoV-2Spike Glycoprotein, CoronavirusAnimalsEpitopesHumansMiceSevere acute respiratory syndrome-related coronavirusAntibodies, NeutralizingAntibodies, ViralEpitopesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID39466880
PMCPMC11542851

What OpenQuestion holds

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LicenceCC BY
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.