Evidence map›Paper›PMID 38082099›Full record

ArticleCommunications biology2023

SARS-COV-2 Omicron variants conformationally escape a rare quaternary antibody binding mode.

Jule Goike, Ching-Lin Hsieh, Andrew P Horton, Elizabeth C Gardner, Ling Zhou, Foteini Bartzoka, Nianshuang Wang, Kamyab Javanmardi, Andrew Herbert, Shawn Abbassi and 20 more

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 17% 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

10 citing papers in PubMed, 1 synthesis or guideline pooled it, 8 citations in OpenAlex.

  1. Pooled it
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  4. Cross-reactive sarbecovirus antibodies induced by mosaic RBD nanoparticles.Proceedings of the National Academy of Sciences of the United States of America · 2025
    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

30 authors at 7 institutions in 1 country.

Jule Goike *Center for Systems and Synthetic Biology, Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.
Ching-Lin Hsieh *Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.ORCID 0000-0002-3665-5717
Andrew P Horton *Center for Systems and Synthetic Biology, Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.ORCID 0000-0002-0272-4411
Elizabeth C Gardner *Center for Systems and Synthetic Biology, Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.
Ling ZhouDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.
Foteini BartzokaCenter for Systems and Synthetic Biology, Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.
Nianshuang WangDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.
Kamyab JavanmardiCenter for Systems and Synthetic Biology, Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.
Andrew HerbertU.S. Army Medical Research Institute of Infectious Diseases, Frederick, MD, USA.
Shawn AbbassiU.S. Army Medical Research Institute of Infectious Diseases, Frederick, MD, USA.
Xuping XieDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, USA.ORCID 0000-0003-0918-016X
Hongjie XiaDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, USA.ORCID 0000-0002-2520-7038
Pei-Yong ShiDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, USA.ORCID 0000-0001-5553-1616
Rebecca RenbergDEVCOM Army Research Laboratory, Biotechnology Branch, Adelphi, MD, USA.ORCID 0000-0003-0640-5087
Thomas H Segall-ShapiroAntibody Discovery and Accelerated Protein Therapeutics, Department of Pathology and Genomic Medicine, Houston Methodist Research Institute, Houston Methodist Hospital, Houston, TX, USA.
Cynthia I TerraceDEVCOM Army Research Laboratory-South, Austin, TX, USA.
Wesley WuAntibody Discovery and Accelerated Protein Therapeutics, Department of Pathology and Genomic Medicine, Houston Methodist Research Institute, Houston Methodist Hospital, Houston, TX, USA.
Raghav ShroffCenter for Systems and Synthetic Biology, Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.
Michelle ByromCenter for Systems and Synthetic Biology, Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.
Andrew D EllingtonCenter for Systems and Synthetic Biology, Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.ORCID 0000-0001-6246-5338
Edward M MarcotteCenter for Systems and Synthetic Biology, Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.ORCID 0000-0001-8808-180X
James M MusserAntibody Discovery and Accelerated Protein Therapeutics, Department of Pathology and Genomic Medicine, Houston Methodist Research Institute, Houston Methodist Hospital, Houston, TX, USA.
Suresh V KuchipudiDepartment of Veterinary and Biomedical Science and Animal Diagnostic Laboratory, The Pennsylvania State University, University Park, PA, USA.ORCID 0000-0002-8640-254X
Vivek KapurDepartment of Animal Science and the Huck Institutes of the Life Sciences, The Pennsylvania State University, University Park, PA, USA.
George GeorgiouCenter for Systems and Synthetic Biology, Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA.ORCID 0000-0002-8823-3073
Scott C WeaverUniversity of Texas Medical Branch, World Reference Center for Emerging Viruses and Arboviruses, Galveston, TX, USA.ORCID 0000-0001-8016-8556
John M DyeU.S. Army Medical Research Institute of Infectious Diseases, Frederick, MD, USA.
Daniel R BoutzCenter for Systems and Synthetic Biology, Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA. drboutz@houstonmethodist.org.ORCID 0000-0001-7462-4105
Jason S McLellanDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA. jmclellan@austin.utexas.edu.ORCID 0000-0003-3991-542X
Jimmy D GolliharCenter for Systems and Synthetic Biology, Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX, USA. jgollihar2@houstonmethodist.org.ORCID 0000-0003-3957-2092
The University of Texas at Austin · USDEVCOM Army Research Laboratory · USMethodist Hospital · USThe University of Texas Medical Branch at Galveston · USUnited States Army Medical Research Institute of Infectious Diseases · USHouston Methodist · USPennsylvania State University · US

Funding

Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
Proteomics and model organism humanization to decode human geneticsR35GM122480 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI EDWARD M MARCOTTE · 2017 to 2026
$5.4M
Novel delivery platform and antigen design for an effective COVID-19 vaccineR01AI158177 · NIAID · PURDUE UNIVERSITY · PI MITTAL, SURESH K · 2020 to 2025
$3.9M
Structure, Function and Antigenicity of Coronavirus Spike ProteinsR01AI127521 · NIAID · UNIVERSITY OF TEXAS AT AUSTIN · PI MCLELLAN, JASON SCOTT, WARD, ANDREW BARRETT · 2017 to 2021
$3.1M
Customized and Integrated Multi-Angle Light Scattering (MALS)-based Multidetection SystemS10OD030276 · OD · BAYLOR COLLEGE OF MEDICINE · PI FERREON, JOSEPHINE CHU · 2022 to 2022
$335k
NIAID NIH HHS R01 AI127521NIAID NIH HHS R01 AI158177NIGMS NIH HHS P41 GM103311NIGMS NIH HHS R35 GM122480NIH HHS S10 OD030276
6 · The paper itself

Abstract

The ongoing evolution of SARS-CoV-2 into more easily transmissible and infectious variants has provided unprecedented insight into mutations enabling immune escape. Understanding how these mutations affect the dynamics of antibody-antigen interactions is crucial to the development of broadly protective antibodies and vaccines. Here we report the characterization of a potent neutralizing antibody (N3-1) identified from a COVID-19 patient during the first disease wave. Cryogenic electron microscopy revealed a quaternary binding mode that enables direct interactions with all three receptor-binding domains of the spike protein trimer, resulting in extraordinary avidity and potent neutralization of all major variants of concern until the emergence of Omicron. Structure-based rational design of N3-1 mutants improved binding to all Omicron variants but only partially restored neutralization of the conformationally distinct Omicron BA.1. This study provides new insights into immune evasion through changes in spike protein dynamics and highlights considerations for future conformationally biased multivalent vaccine designs.

Indexed as

COVID-19SARS-CoV-2Antibodies, NeutralizingHumansSpike Glycoprotein, CoronavirusAntibodies, NeutralizingSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID38082099
PMCPMC10713552
OpenAlexW4389574240

What OpenQuestion holds

Textmetadata
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.