Evidence map›Paper›PMID 34855508›Full record

ArticleScience (New York, N.Y.)2022

Structural basis for continued antibody evasion by the SARS-CoV-2 receptor binding domain.

Katherine G Nabel, Sarah A Clark, Sundaresh Shankar, Junhua Pan, Lars E Clark, Pan Yang, Adrian Coscia, Lindsay G A McKay, Haley H Varnum, Vesna Brusic and 21 more

Erratum issuedAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing 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

61 citing papers in PubMed.

  1. Trial
  2. Constrained evolutionary funnels shape viral immune escape.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Constrained Evolutionary Funnels Shape Viral Immune Escape.bioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Predicting high-fitness viral protein variants with Bayesian active learning and biophysics.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Targeted photodynamic neutralization of SARS-CoV-2 mediated by singlet oxygen.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023
    Article

1 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

31 authors.

Katherine G Nabel *Department of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0002-4429-7075
Sarah A Clark *Department of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0001-9944-0919
Sundaresh Shankar *Department of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0001-9340-9945
Junhua Pan *Department of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0002-0070-955X
Lars E ClarkDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0002-6093-7597
Pan YangDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA.
Adrian CosciaDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0002-6836-9993
Lindsay G A McKayDepartment of Microbiology and National Emerging Infectious Diseases Laboratories, Boston University School of Medicine, Boston, MA 02118, USA.ORCID 0000-0003-0369-9067
Haley H VarnumDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA.
Vesna BrusicDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA.
Nicole V TolanDepartment of Pathology, Brigham and Women's Hospital, Boston, MA 02115, USA.
Guohai ZhouCenter for Clinical Investigation, Brigham and Women's Hospital, Boston, MA 02115, USA.
Michaël DesjardinsDivision of Infectious Diseases, Department of Medicine, Brigham and Women's Hospital, Boston, MA 02115, USA.ORCID 0000-0003-4028-8507
Sarah E TurbettDivision of Infectious Diseases, Department of Medicine, Massachusetts General Hospital, Boston, MA 02114, USA.ORCID 0000-0002-3603-8110
Sanjat KanjilalDivision of Infectious Diseases, Department of Medicine, Brigham and Women's Hospital, Boston, MA 02115, USA.ORCID 0000-0002-1221-5725
Amy C ShermanDivision of Infectious Diseases, Department of Medicine, Brigham and Women's Hospital, Boston, MA 02115, USA.ORCID 0000-0002-6075-3990
Anand DigheDepartment of Pathology, Massachusetts General Hospital, Boston, MA 02114, USA.
Regina C LaRocqueDivision of Infectious Diseases, Department of Medicine, Massachusetts General Hospital, Boston, MA 02114, USA.ORCID 0000-0003-4558-0339
Edward T RyanDivision of Infectious Diseases, Department of Medicine, Massachusetts General Hospital, Boston, MA 02114, USA.
Casey TylekAbbVie Bioresearch Center, Worcester, MA 01605, USA.
Joel F Cohen-SolalAbbVie Bioresearch Center, Worcester, MA 01605, USA.ORCID 0000-0002-1385-2566
Anhdao T DarcyAbbVie Bioresearch Center, Worcester, MA 01605, USA.
Davide TavellaAbbVie Bioresearch Center, Worcester, MA 01605, USA.ORCID 0000-0002-2030-2087
Anca ClabbersAbbVie Bioresearch Center, Worcester, MA 01605, USA.ORCID 0000-0002-4258-9680
Yao FanAbbVie Bioresearch Center, Worcester, MA 01605, USA.
Anthony GriffithsDepartment of Microbiology and National Emerging Infectious Diseases Laboratories, Boston University School of Medicine, Boston, MA 02118, USA.ORCID 0000-0001-5435-8364
Ivan R CorreiaAbbVie Bioresearch Center, Worcester, MA 01605, USA.ORCID 0000-0003-2295-7199
Jane SeagalAbbVie Bioresearch Center, Worcester, MA 01605, USA.ORCID 0000-0002-5959-5139
Lindsey R BadenCenter for Clinical Investigation, Brigham and Women's Hospital, Boston, MA 02115, USA.
Richelle C CharlesDivision of Infectious Diseases, Department of Medicine, Massachusetts General Hospital, Boston, MA 02114, USA.
Jonathan AbrahamDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0002-7937-3920

Funding

The Harvard Clinical and Translational Science CenterUL1TR002541 · NCATS · HARVARD MEDICAL SCHOOL · PI NADLER, LEE MARSHALL · 2018 to 2022
$93.0M
Medical Scientist Training ProgramT32GM007753 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WALENSKY, LOREN DAVID · 1985 to 2021
$50.0M
User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI Frank V Murphy · 2018 to 2026
$34.2M
MOLECULAR BIOPHYSICS TRAINING GRANTT32GM008313 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI MURTHY, VENKATESH N · 1989 to 2023
$14.6M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
ACL HHS U01CK000490NCATS NIH HHS UL1 TR002541NCEZID CDC HHS U01 CK000490NCRR NIH HHS S10 RR029205NIGMS NIH HHS P30 GM124165NIGMS NIH HHS T32 GM007753NIGMS NIH HHS T32 GM008313
6 · The paper itself

Abstract

Many studies have examined the impact of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants on neutralizing antibody activity after they have become dominant strains. Here, we evaluate the consequences of further viral evolution. We demonstrate mechanisms through which the SARS-CoV-2 receptor binding domain (RBD) can tolerate large numbers of simultaneous antibody escape mutations and show that pseudotypes containing up to seven mutations, as opposed to the one to three found in previously studied variants of concern, are more resistant to neutralization by therapeutic antibodies and serum from vaccine recipients. We identify an antibody that binds the RBD core to neutralize pseudotypes for all tested variants but show that the RBD can acquire an N-linked glycan to escape neutralization. Our findings portend continued emergence of escape variants as SARS-CoV-2 adapts to humans.

Indexed as

Immune EvasionAngiotensin-Converting Enzyme 2Antibodies, NeutralizingAntibodies, ViralBNT162 VaccineCOVID-19Cross ReactionsCryoelectron MicroscopyCrystallography, X-RayEpitopesEvolution, MolecularHumansModels, MolecularMutationPolysaccharidesProtein BindingACE2 protein, humanAngiotensin-Converting Enzyme 2Antibodies, NeutralizingAntibodies, ViralBNT162 VaccineEpitopesPolysaccharidesReceptors, CoronavirusSpike Glycoprotein, Coronavirusspike glycoprotein, SARS-CoVspike protein, SARS-CoV-2

Identifiers

PMID34855508
PMCPMC9127715

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.