Evidence map›Paper›PMID 38723626›Full record

ArticleCell reports. Medicine2024

A structure-function analysis shows SARS-CoV-2 BA.2.86 balances antibody escape and ACE2 affinity.

Chang Liu, Daming Zhou, Aiste Dijokaite-Guraliuc, Piyada Supasa, Helen M E Duyvesteyn, Helen M Ginn, Muneeswaran Selvaraj, Alexander J Mentzer, Raksha Das, Thushan I de Silva and 20 more

Abstract read
In one paragraph

Article in Cell reports. Medicine, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

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  6. Review
  7. Article
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  11. Article
  12. Article
  13. SARS-CoV-2 and Environmental Changes: The Perfect Storm.Current issues in molecular biology · 2024
    Review
  14. Article
  15. Article
  16. Article
  17. Article
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.

Chang LiuChinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK; Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Daming ZhouChinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, Centre for Human Genetics, Oxford, UK.
Aiste Dijokaite-GuraliucCentre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Piyada SupasaChinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK.
Helen M E DuyvesteynDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, Centre for Human Genetics, Oxford, UK.
Helen M GinnCentre for Free Electron Laser Science, Hamburg, Germany.
Muneeswaran SelvarajChinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK.
Alexander J MentzerCentre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK; NIHR Oxford Biomedical Research Centre, Oxford University Hospitals NHS Foundation Trust, Oxford, UK.
Raksha DasChinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK.
Thushan I de SilvaDivision of Clinical Medicine, School of Medicine and Population Health, University of Sheffield, Sheffield, UK; Sheffield Teaching Hospitals NHS Foundation Trust, Sheffield, UK.
Thomas G RitterNIHR Oxford Biomedical Research Centre, Oxford University Hospitals NHS Foundation Trust, Oxford, UK.
Megan PlowrightSheffield Teaching Hospitals NHS Foundation Trust, Sheffield, UK.
Thomas A H NewmanSheffield Teaching Hospitals NHS Foundation Trust, Sheffield, UK.
Lizzie StaffordNIHR Oxford Biomedical Research Centre, Oxford University Hospitals NHS Foundation Trust, Oxford, UK.
Barbara KronsteinerNDM Centre for Global Health Research, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Peter Medawar Building for Pathogen Research, University of Oxford, Oxford, UK.
Nigel TempertonViral Pseudotype Unit, Medway School of Pharmacy, University of Kent and University of Greenwich Chatham Maritime, Kent ME4 4TB, UK.
Yuan LuiRadcliffe Department of Medicine, John Radcliffe Hospital, University of Oxford, Oxford, UK.
Martin FellermeyerRadcliffe Department of Medicine, John Radcliffe Hospital, University of Oxford, Oxford, UK.
Philip GoulderPeter Medawar Building for Pathogen Research, University of Oxford, Oxford, UK; Department of Paediatrics, University of Oxford, Oxford, UK.
Paul KlenermanNIHR Oxford Biomedical Research Centre, Oxford University Hospitals NHS Foundation Trust, Oxford, UK; Peter Medawar Building for Pathogen Research, University of Oxford, Oxford, UK; Translational Gastroenterology Unit, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Susanna J DunachieNIHR Oxford Biomedical Research Centre, Oxford University Hospitals NHS Foundation Trust, Oxford, UK; NDM Centre for Global Health Research, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Peter Medawar Building for Pathogen Research, University of Oxford, Oxford, UK; Mahidol-Oxford Tropical Medicine Research Unit, Mahidol University, Bangkok, Thailand.
Michael I BartonDiamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
Mikhail A KutuzovDiamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
Omer DushekDiamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
OPTIC Consortium
Elizabeth E FryDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, Centre for Human Genetics, Oxford, UK. Electronic address: liz@strubi.ox.ac.uk.
Juthathip MongkolsapayaChinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK; Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Mahidol-Oxford Tropical Medicine Research Unit, Mahidol University, Bangkok, Thailand. Electronic address: juthathip.mongkolsapaya@well.ox.ac.uk.
Jingshan RenDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, Centre for Human Genetics, Oxford, UK. Electronic address: ren@strubi.ox.ac.uk.
David I StuartChinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, Centre for Human Genetics, Oxford, UK; Sir William Dunn School of Pathology, Oxford, UK. Electronic address: dave@strubi.ox.ac.uk.
Gavin R ScreatonChinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK; Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK. Electronic address: gavin.screaton@medsci.ox.ac.uk.

Funding

Medical Research Council MR/X009297/1
6 · The paper itself

Abstract

BA.2.86, a recently described sublineage of SARS-CoV-2 Omicron, contains many mutations in the spike gene. It appears to have originated from BA.2 and is distinct from the XBB variants responsible for many infections in 2023. The global spread and plethora of mutations in BA.2.86 has caused concern that it may possess greater immune-evasive potential, leading to a new wave of infection. Here, we examine the ability of BA.2.86 to evade the antibody response to infection using a panel of vaccinated or naturally infected sera and find that it shows marginally less immune evasion than XBB.1.5. We locate BA.2.86 in the antigenic landscape of recent variants and look at its ability to escape panels of potent monoclonal antibodies generated against contemporary SARS-CoV-2 infections. We demonstrate, and provide a structural explanation for, increased affinity of BA.2.86 to ACE2, which may increase transmissibility.

Indexed as

Angiotensin-Converting Enzyme 2Antibodies, ViralCOVID-19Immune EvasionSARS-CoV-2Spike Glycoprotein, CoronavirusAntibodies, MonoclonalAntibodies, NeutralizingAntibody AffinityHumansMutationStructure-Activity RelationshipACE2 protein, humanAngiotensin-Converting Enzyme 2Antibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2ACE2 bindingantigenic escapeBA.2.65coronavirusreceptor bindingSARS-CoV-2virus evolutionvirus structure

Identifiers

PMID38723626
PMCPMC11148769

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.