Evidence map›Paper›PMID 38835241›Full record

ArticleOpen biology2024

Structural and functional characterization of nanobodies that neutralize Omicron variants of SARS-CoV-2.

Katy Cornish, Jiandong Huo, Luke Jones, Parul Sharma, Joseph W Thrush, Sahar Abdelkarim, Anja Kipar, Siva Ramadurai, Miriam Weckener, Halina Mikolajek and 16 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Open biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Nanobodies targeting SARS-CoV-2 variants.Acta pharmaceutica Sinica. B · 2026
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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

26 authors.

Katy CornishStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
Jiandong HuoStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
Luke JonesNuffield Department of Medicine, Pandemic Sciences Institute, University of Oxford , Oxford, UK.
Parul SharmaDepartment of Infection Biology & Microbiomes, Institute of Infection, Veterinary and Ecological Sciences, University of Liverpool , Liverpool, UK.
Joseph W ThrushStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.ORCID 0000-0001-6556-8113
Sahar AbdelkarimStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
Anja KiparDepartment of Infection Biology & Microbiomes, Institute of Infection, Veterinary and Ecological Sciences, University of Liverpool , Liverpool, UK.
Siva RamaduraiStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
Miriam WeckenerStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
Halina MikolajekDiamond Light Source Ltd, Harwell Science Campus , Didcot, UK.
Sai LiuJames & Lillian Martin Centre, Sir William Dunn School of Pathology, University of Oxford , Oxford, UK.
Imogen BuckleStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
Eleanor BentleyDepartment of Infection Biology & Microbiomes, Institute of Infection, Veterinary and Ecological Sciences, University of Liverpool , Liverpool, UK.
Adam KirbyDepartment of Infection Biology & Microbiomes, Institute of Infection, Veterinary and Ecological Sciences, University of Liverpool , Liverpool, UK.
Ximeng HanDepartment of Infection Biology & Microbiomes, Institute of Infection, Veterinary and Ecological Sciences, University of Liverpool , Liverpool, UK.
Stephen M LaidlawNuffield Department of Medicine, Pandemic Sciences Institute, University of Oxford , Oxford, UK.
Michelle HillJames & Lillian Martin Centre, Sir William Dunn School of Pathology, University of Oxford , Oxford, UK.
Lauren EyssenStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
Chelsea NormanStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
Audrey Le BasStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.ORCID 0000-0002-1100-6833
John ClarkeStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.ORCID 0000-0001-7891-7626
William JamesJames & Lillian Martin Centre, Sir William Dunn School of Pathology, University of Oxford , Oxford, UK.
James P StewartDepartment of Infection Biology & Microbiomes, Institute of Infection, Veterinary and Ecological Sciences, University of Liverpool , Liverpool, UK.ORCID 0000-0002-8928-2037
Miles CarrollNuffield Department of Medicine, Pandemic Sciences Institute, University of Oxford , Oxford, UK.
James H NaismithStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.
Raymond J OwensStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus , Didcot, UK.ORCID 0000-0002-3705-2993

Funding

BBSRCDiamond Light SourceEMEPSRC, Wellcome TrustMedical Research Council MR/V03958X/1Reading UniversityRosalind Franklin Universitythe Histology Laboratory, Institute of Veterinary Pathology, Vetsuisse Faculty, University of ZurichUS Food and Drug AdministrationWellcome Trust
6 · The paper itself

Abstract

The Omicron strains of SARS-CoV-2 pose a significant challenge to the development of effective antibody-based treatments as immune evasion has compromised most available immune therapeutics. Therefore, in the 'arms race' with the virus, there is a continuing need to identify new biologics for the prevention or treatment of SARS-CoV-2 infections. Here, we report the isolation of nanobodies that bind to the Omicron BA.1 spike protein by screening nanobody phage display libraries previously generated from llamas immunized with either the Wuhan or Beta spike proteins. The structure and binding properties of three of these nanobodies (A8, H6 and B5-5) have been characterized in detail providing insight into their binding epitopes on the Omicron spike protein. Trimeric versions of H6 and B5-5 neutralized the SARS-CoV-2 variant of concern BA.5 both

Indexed as

Antibodies, NeutralizingAntibodies, ViralCOVID-19SARS-CoV-2Single-Domain AntibodiesSpike Glycoprotein, CoronavirusAnimalsCamelids, New WorldCricetinaeEpitopesHumansModels, MolecularProtein BindingAntibodies, NeutralizingAntibodies, ViralEpitopesSingle-Domain AntibodiesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2COVID-19nanobodiesOmicronsSARS-CoV-2spike protein

Identifiers

PMID38835241
PMCPMC11285730

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.