Evidence map›Paper›PMID 37430064›Full record

ArticleNature structural & molecular biology2023

Structural and functional characteristics of the SARS-CoV-2 Omicron subvariant BA.2 spike protein.

Jun Zhang, Weichun Tang, Hailong Gao, Christy L Lavine, Wei Shi, Hanqin Peng, Haisun Zhu, Krishna Anand, Matina Kosikova, Hyung Joon Kwon and 11 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
5.2field-weighted citation impact, top 3% 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

21 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Viral syncytia evolve to resist interferon.Nature communications · 2026
    Article
  3. Recurrent SARS-CoV-2 Omicron broadly neutralizing humanized antibodies in different single human VProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  7. Review
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  13. Review
  14. Article
  15. Article
  16. Article
  17. Multi-faceted immunoglobulin M meets its elusive receptor.Nature structural & molecular biology · 2023
    Article
  18. GABA transport cycle: beyond a GAT feeling.Nature structural & molecular biology · 2023
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

21 authors at 7 institutions in 1 country.

Jun Zhang *Division of Molecular Medicine, Boston Children's Hospital, Boston, MA, USA.ORCID 0000-0002-1289-0624
Weichun Tang *Laboratory of Pediatric and Respiratory Viral Diseases, Division of Viral Products, Office of Vaccines Research and Review, Center for Biologics Evaluation and Research, United States Food and Drug Administration, Silver Spring, MD, USA.
Hailong Gao *Division of Molecular Medicine, Boston Children's Hospital, Boston, MA, USA.
Christy L LavineCenter for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Boston, MA, USA.
Wei ShiDivision of Molecular Medicine, Boston Children's Hospital, Boston, MA, USA.ORCID 0000-0002-0741-6813
Hanqin PengDivision of Molecular Medicine, Boston Children's Hospital, Boston, MA, USA.ORCID 0000-0002-5357-8215
Haisun ZhuInstitute for Protein Innovation, Harvard Institutes of Medicine, Boston, MA, USA.ORCID 0000-0001-8395-9409
Krishna AnandInstitute for Protein Innovation, Harvard Institutes of Medicine, Boston, MA, USA.
Matina KosikovaLaboratory of Pediatric and Respiratory Viral Diseases, Division of Viral Products, Office of Vaccines Research and Review, Center for Biologics Evaluation and Research, United States Food and Drug Administration, Silver Spring, MD, USA.
Hyung Joon KwonLaboratory of Pediatric and Respiratory Viral Diseases, Division of Viral Products, Office of Vaccines Research and Review, Center for Biologics Evaluation and Research, United States Food and Drug Administration, Silver Spring, MD, USA.
Pei TongDivision of Allergy and Clinical Immunology, Department of Medicine, Brigham and Women's Hospital; Ragon Institute of MGH, MIT and Harvard, Boston, MA, USA.
Avneesh GautamDivision of Allergy and Clinical Immunology, Department of Medicine, Brigham and Women's Hospital; Ragon Institute of MGH, MIT and Harvard, Boston, MA, USA.ORCID 0000-0003-1745-5530
Sophia Rits-VollochDivision of Molecular Medicine, Boston Children's Hospital, Boston, MA, USA.
Shaowei WangCodex BioSolutions, Inc., Rockville, MD, USA.
Megan L MayerThe Harvard Cryo-EM Center for Structural Biology, Boston, MA, USA.
Duane R WesemannDivision of Allergy and Clinical Immunology, Department of Medicine, Brigham and Women's Hospital; Ragon Institute of MGH, MIT and Harvard, Boston, MA, USA.
Michael S SeamanCenter for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Boston, MA, USA.
Jianming LuCodex BioSolutions, Inc., Rockville, MD, USA.
Tianshu XiaoDivision of Molecular Medicine, Boston Children's Hospital, Boston, MA, USA. xiao@crystal.harvard.edu.ORCID 0000-0003-1287-1228
Hang XieLaboratory of Pediatric and Respiratory Viral Diseases, Division of Viral Products, Office of Vaccines Research and Review, Center for Biologics Evaluation and Research, United States Food and Drug Administration, Silver Spring, MD, USA. Hang.Xie@fda.hhs.gov.ORCID 0000-0001-8318-5554
Bing ChenDivision of Molecular Medicine, Boston Children's Hospital, Boston, MA, USA. bchen@crystal.harvard.edu.ORCID 0000-0002-8625-1657
Boston Children's Hospital · USCenter for Biologics Evaluation and Research · USBrigham and Women's Hospital · USBeth Israel Deaconess Medical Center · USInstitute for Protein Innovation · USCodex Biosolutions (United States) · USGeorgetown University · US

Funding

Structure of the full-length spike protein of SARS-CoV-2 in the context of membraneR01AI147884 · NIAID · BOSTON CHILDREN'S HOSPITAL · PI CHEN, BING · 2020 to 2024
$3.4M
NIAID NIH HHS R01 AI147884
6 · The paper itself

Abstract

The Omicron subvariant BA.2 has become the dominant circulating strain of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) in many countries. Here, we have characterized structural, functional and antigenic properties of the full-length BA.2 spike (S) protein and compared replication of the authentic virus in cell culture and an animal model with previously prevalent variants. BA.2 S can fuse membranes slightly more efficiently than Omicron BA.1, but still less efficiently than other previous variants. Both BA.1 and BA.2 viruses replicated substantially faster in animal lungs than the early G614 (B.1) strain in the absence of pre-existing immunity, possibly explaining the increased transmissibility despite their functionally compromised spikes. As in BA.1, mutations in the BA.2 S remodel its antigenic surfaces, leading to strong resistance to neutralizing antibodies. These results suggest that both immune evasion and replicative advantage may contribute to the heightened transmissibility of the Omicron subvariants.

Indexed as

COVID-19AnimalsSARS-CoV-2Spike Glycoprotein, CoronavirusSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID37430064
OpenAlexW4383704089

What OpenQuestion holds

Textmetadata
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.