Evidence map›Paper›PMID 34552091›Full record

ArticleNature communications2021

A potent SARS-CoV-2 neutralising nanobody shows therapeutic efficacy in the Syrian golden hamster model of COVID-19.

Jiandong Huo, Halina Mikolajek, Audrey Le Bas, Jordan J Clark, Parul Sharma, Anja Kipar, Joshua Dormon, Chelsea Norman, Miriam Weckener, Daniel K Clare and 23 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed, 2 pooled it
8.3field-weighted citation impact, top 2% 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

105 citing papers in PubMed, 2 syntheses or guidelines pooled it, 153 citations in OpenAlex.

  1. Mucosal immune response in biology, disease prevention and treatment.Signal transduction and targeted therapy · 2025
    Pooled it
  2. Pooled it
  3. Review
  4. AVIDbase: A biologically accurate structural dataset of nanobody-antigen complexes.Protein science : a publication of the Protein Society · 2026
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45 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

33 authors at 8 institutions in 5 countries.

Jiandong HuoStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus, Didcot, UK.ORCID 0000-0002-7899-1815
Halina MikolajekDiamond Light Source Ltd, Harwell Science Campus, Didcot, UK.
Audrey Le BasStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus, Didcot, UK.
Jordan J ClarkDepartment of Infection Biology & Microbiomes, Institute of Infection, Veterinary and Ecological Sciences, University of Liverpool, Liverpool, UK.ORCID 0000-0003-1790-7883
Parul SharmaDepartment of Infection Biology & Microbiomes, Institute of Infection, Veterinary and Ecological Sciences, University of Liverpool, Liverpool, UK.
Anja KiparDepartment of Infection Biology & Microbiomes, Institute of Infection, Veterinary and Ecological Sciences, University of Liverpool, Liverpool, UK.
Joshua DormonStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus, Didcot, UK.
Chelsea NormanStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus, Didcot, UK.
Miriam WeckenerStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus, Didcot, UK.
Daniel K ClareDiamond Light Source Ltd, Harwell Science Campus, Didcot, UK.
Peter J HarrisonProtein Production UK, The Rosalind Franklin Institute - Diamond Light Source, The Research Complex at Harwell, Science Campus, Didcot, UK.
Julia A TreeNational Infection Service, Public Health England, Porton Down, Salisbury, UK.
Karen R ButtigiegNational Infection Service, Public Health England, Porton Down, Salisbury, UK.
Francisco J SalgueroNational Infection Service, Public Health England, Porton Down, Salisbury, UK.
Robert WatsonNational Infection Service, Public Health England, Porton Down, Salisbury, UK.ORCID 0000-0003-3146-3457
Daniel KnottNational Infection Service, Public Health England, Porton Down, Salisbury, UK.
Oliver CarnellNational Infection Service, Public Health England, Porton Down, Salisbury, UK.ORCID 0000-0001-8847-5489
Didier NgaboNational Infection Service, Public Health England, Porton Down, Salisbury, UK.ORCID 0000-0003-1818-1439
Michael J ElmoreNational Infection Service, Public Health England, Porton Down, Salisbury, UK.ORCID 0000-0001-9425-2660
Susan FotheringhamNational Infection Service, Public Health England, Porton Down, Salisbury, UK.
Adam HardingSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Lucile MoyniéStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus, Didcot, UK.
Philip N WardDivision of Structural Biology, The Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK.ORCID 0000-0003-2546-3426
Maud DumouxStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus, Didcot, UK.ORCID 0000-0002-1732-1041
Tessa PrinceDiamond Light Source Ltd, Harwell Science Campus, Didcot, UK.ORCID 0000-0002-8796-2629
Yper HallNational Infection Service, Public Health England, Porton Down, Salisbury, UK.
Julian A HiscoxDiamond Light Source Ltd, Harwell Science Campus, Didcot, UK.
Andrew OwenDepartment of Pharmacology and Therapeutics, Centre of Excellence in Long-acting Therapeutics (CELT), University of Liverpool, Liverpool, UK.ORCID 0000-0002-9819-7651
William JamesSir William Dunn School of Pathology, University of Oxford, Oxford, UK.ORCID 0000-0002-2506-1198
Miles W CarrollNational Infection Service, Public Health England, Porton Down, Salisbury, UK.
James P StewartDiamond Light Source Ltd, Harwell Science Campus, Didcot, UK.ORCID 0000-0002-8928-2037
James H NaismithStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus, Didcot, UK. james.naismith@strubi.ox.ac.uk.ORCID 0000-0001-6744-5061
Raymond J OwensStructural Biology, The Rosalind Franklin Institute, Harwell Science Campus, Didcot, UK. ray.owens@strubi.ox.ac.uk.ORCID 0000-0002-3705-2993
Public Health England · GBDiamond Light Source · GBCentre for Human Genetics · GBUniversity of Liverpool · GBRosalind Franklin Institute · GBUniversity of Oxford · GBAgency for Science, Technology and Research · SGUniversity of Georgia · US

Funding

Medical Research Council MR/W005611/1RCUK | Engineering and Physical Sciences Research Council (EPSRC) EP/ S025243/1RCUK | MRC | Medical Research Foundation MR/W005611/1Wellcome TrustWellcome Trust (Wellcome) 100209/Z/12/Z
6 · The paper itself

Abstract

SARS-CoV-2 remains a global threat to human health particularly as escape mutants emerge. There is an unmet need for effective treatments against COVID-19 for which neutralizing single domain antibodies (nanobodies) have significant potential. Their small size and stability mean that nanobodies are compatible with respiratory administration. We report four nanobodies (C5, H3, C1, F2) engineered as homotrimers with pmolar affinity for the receptor binding domain (RBD) of the SARS-CoV-2 spike protein. Crystal structures show C5 and H3 overlap the ACE2 epitope, whilst C1 and F2 bind to a different epitope. Cryo Electron Microscopy shows C5 binding results in an all down arrangement of the Spike protein. C1, H3 and C5 all neutralize the Victoria strain, and the highly transmissible Alpha (B.1.1.7 first identified in Kent, UK) strain and C1 also neutralizes the Beta (B.1.35, first identified in South Africa). Administration of C5-trimer via the respiratory route showed potent therapeutic efficacy in the Syrian hamster model of COVID-19 and separately, effective prophylaxis. The molecule was similarly potent by intraperitoneal injection.

Indexed as

COVID-19 Drug TreatmentAdministration, IntranasalAnimalsAntibodies, NeutralizingCryoelectron MicroscopyCrystallography, X-RayDisease Models, AnimalDose-Response Relationship, ImmunologicEpitopesFemaleMaleMesocricetusNeutralization TestsSARS-CoV-2Single-Domain AntibodiesSpike Glycoprotein, CoronavirusAntibodies, NeutralizingEpitopesSingle-Domain AntibodiesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID34552091
PMCPMC8458290
OpenAlexW3185920256

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.