Evidence map›Paper›PMID 35662412›Full record

ArticleCell2022

Potent cross-reactive antibodies following Omicron breakthrough in vaccinees.

Rungtiwa Nutalai, Daming Zhou, Aekkachai Tuekprakhon, Helen M Ginn, Piyada Supasa, Chang Liu, Jiandong Huo, Alexander J Mentzer, Helen M E Duyvesteyn, Aiste Dijokaite-Guraliuc and 26 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing 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

123 citing papers in PubMed.

  1. Article
  2. Nanobodies targeting SARS-CoV-2 variants.Acta pharmaceutica Sinica. B · 2026
    Review
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63 more citing papers are in PubMed but not listed here.

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

36 authors.

Rungtiwa NutalaiWellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Daming ZhouDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK; Chinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK.
Aekkachai TuekprakhonWellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Helen M GinnDiamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
Piyada SupasaWellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Chang LiuWellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Chinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK.
Jiandong HuoDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK.
Alexander J MentzerWellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Oxford University Hospitals NHS Foundation Trust, Oxford, UK.
Helen M E DuyvesteynDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK.
Aiste Dijokaite-GuraliucWellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK.
Donal SkellyOxford University Hospitals NHS Foundation Trust, Oxford, UK; Peter Medawar Building for Pathogen Research, Oxford, UK; Nuffield Department of Clinical Neurosciences, University of Oxford, Oxford, UK.
Thomas G RitterOxford University Hospitals NHS Foundation Trust, Oxford, UK.
Ali AminiOxford University Hospitals NHS Foundation Trust, Oxford, UK; Peter Medawar Building for Pathogen Research, Oxford, UK; Translational Gastroenterology Unit, University of Oxford, Oxford, UK.
Sagida BibiOxford Vaccine Group, Department of Paediatrics, University of Oxford, Oxford, UK.
Sandra AdeleOxford University Hospitals NHS Foundation Trust, Oxford, UK.
Sile Ann JohnsonOxford University Hospitals NHS Foundation Trust, Oxford, UK.
Bede ConstantinidesNuffield Department of Medicine, University of Oxford, Oxford, UK.
Hermione WebsterNuffield Department of Medicine, University of Oxford, Oxford, UK.
Nigel TempertonViral Pseudotype Unit, Medway School of Pharmacy, University of Kent and Greenwich, Chatham Maritime, Kent ME4 4TB, UK.
Paul KlenermanOxford University Hospitals NHS Foundation Trust, Oxford, UK; Peter Medawar Building for Pathogen Research, Oxford, UK; Translational Gastroenterology Unit, University of Oxford, Oxford, UK; NIHR Oxford Biomedical Research Centre, Oxford, UK.
Eleanor BarnesOxford University Hospitals NHS Foundation Trust, Oxford, UK; Peter Medawar Building for Pathogen Research, Oxford, UK; Translational Gastroenterology Unit, University of Oxford, Oxford, UK; NIHR Oxford Biomedical Research Centre, Oxford, UK.
Susanna J DunachieOxford University Hospitals NHS Foundation Trust, Oxford, UK; Peter Medawar Building for Pathogen Research, Oxford, UK; Nuffield Department of Medicine, University of Oxford, Oxford, UK; Centre For Tropical Medicine and Global Health, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Mahidol-Oxford Tropical Medicine Research Unit, Bangkok, Thailand.
Derrick CrookNuffield Department of Medicine, University of Oxford, Oxford, UK.
Andrew J PollardOxford Vaccine Group, Department of Paediatrics, University of Oxford, Oxford, UK; NIHR Oxford Biomedical Research Centre, Oxford, UK.
Teresa LambeChinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK; Oxford Vaccine Group, Department of Paediatrics, University of Oxford, Oxford, UK.
Philip GoulderPeter Medawar Building for Pathogen Research, Oxford, UK; Department of Paediatrics, University of Oxford, Oxford, UK.
OPTIC consortium, ISARIC4C consortium
Neil G PatersonDiamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
Mark A WilliamsDiamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
David R HallDiamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
Juthathip MongkolsapayaWellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Chinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK.
Elizabeth E FryDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK.
Wanwisa DejnirattisaiWellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK. Electronic address: dwanwisa@well.ox.ac.uk.
Jingshan RenDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK. Electronic address: ren@strubi.ox.ac.uk.
David I StuartDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Oxford, UK; Chinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK; Diamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK. Electronic address: dave@strubi.ox.ac.uk.
Gavin R ScreatonWellcome Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford, UK; Chinese Academy of Medical Science (CAMS) Oxford Institute (COI), University of Oxford, Oxford, UK. Electronic address: gavin.screaton@medsci.ox.ac.uk.

Funding

Department of Health NIHR300791Medical Research Council MC_PC_17137Medical Research Council MC_PC_19059Medical Research Council MR/N00065X/1Medical Research Council MR/V001329/1Wellcome TrustWellcome Trust 060208/Z/00/ZWellcome Trust 090532/Z/09/ZWellcome Trust 101122/Z/13/ZWellcome Trust 203141/Z/16/ZWellcome Trust WT109965MA
6 · The paper itself

Abstract

Highly transmissible Omicron variants of SARS-CoV-2 currently dominate globally. Here, we compare neutralization of Omicron BA.1, BA.1.1, and BA.2. BA.2 RBD has slightly higher ACE2 affinity than BA.1 and slightly reduced neutralization by vaccine serum, possibly associated with its increased transmissibility. Neutralization differences between sub-lineages for mAbs (including therapeutics) mostly arise from variation in residues bordering the ACE2 binding site; however, more distant mutations S371F (BA.2) and R346K (BA.1.1) markedly reduce neutralization by therapeutic antibody Vir-S309. In-depth structure-and-function analyses of 27 potent RBD-binding mAbs isolated from vaccinated volunteers following breakthrough Omicron-BA.1 infection reveals that they are focused in two main clusters within the RBD, with potent right-shoulder antibodies showing increased prevalence. Selection and somatic maturation have optimized antibody potency in less-mutated epitopes and recovered potency in highly mutated epitopes. All 27 mAbs potently neutralize early pandemic strains, and many show broad reactivity with variants of concern.

Indexed as

Antibodies, MonoclonalSARS-CoV-2Spike Glycoprotein, CoronavirusAngiotensin-Converting Enzyme 2Antibodies, ViralCOVID-19COVID-19 VaccinesEpitopesHumansNeutralization TestsAngiotensin-Converting Enzyme 2Antibodies, MonoclonalAntibodies, ViralCOVID-19 VaccinesEpitopesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2antibody responsesBA.1BA.1.1BA.2COVID-19crystallographyimmune escapeneutralizationOmicronreceptor binding domainSARS-CoV-2variants of concern

Identifiers

PMID35662412
PMCPMC9120130

What OpenQuestion holds

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Registered trials

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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.