Evidence map›Paper›PMID 34024246›Full record

ArticlemAbs

Potent SARS-CoV-2 binding and neutralization through maturation of iconic SARS-CoV-1 antibodies.

Romain Rouet, Ohan Mazigi, Gregory J Walker, David B Langley, Meghna Sobti, Peter Schofield, Helen Lenthall, Jennifer Jackson, Stephanie Ubiparipovic, Jake Y Henry and 10 more

Abstract read
In one paragraph

Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
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  9. Affinity maturation endows potent activity onto class 6 SARS-CoV-2 broadly neutralizing antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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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

20 authors.

Romain RouetImmunology Department, Garvan Institute of Medical Research, Sydney, NSW, Australia.
Ohan MazigiImmunology Department, Garvan Institute of Medical Research, Sydney, NSW, Australia.
Gregory J WalkerImmunology Department, UNSW Sydney, Faculty of Medicine, Sydney, NSW, Australia.
David B LangleyImmunology Department, Garvan Institute of Medical Research, Sydney, NSW, Australia.
Meghna SobtiImmunology Department, UNSW Sydney, St Vincent's Clinical School, Sydney, NSW, Australia.
Peter SchofieldImmunology Department, Garvan Institute of Medical Research, Sydney, NSW, Australia.
Helen LenthallImmunology Department, Garvan Institute of Medical Research, Sydney, NSW, Australia.
Jennifer JacksonImmunology Department, Garvan Institute of Medical Research, Sydney, NSW, Australia.
Stephanie UbiparipovicImmunology Department, Garvan Institute of Medical Research, Sydney, NSW, Australia.
Jake Y HenryImmunology Department, Garvan Institute of Medical Research, Sydney, NSW, Australia.
Arunasingam AbayasingamImmunology Department, UNSW Sydney, Faculty of Medicine, Sydney, NSW, Australia.
Deborah BurnettImmunology Department, Garvan Institute of Medical Research, Sydney, NSW, Australia.
Anthony KelleherImmunology Department, UNSW Sydney, Faculty of Medicine, Sydney, NSW, Australia.
Robert BrinkImmunology Department, Garvan Institute of Medical Research, Sydney, NSW, Australia.
Rowena A BullImmunology Department, UNSW Sydney, Faculty of Medicine, Sydney, NSW, Australia.
Stuart TurvilleImmunology Department, UNSW Sydney, Faculty of Medicine, Sydney, NSW, Australia.
Alastair G StewartImmunology Department, UNSW Sydney, St Vincent's Clinical School, Sydney, NSW, Australia.
Christopher C GoodnowImmunology Department, Garvan Institute of Medical Research, Sydney, NSW, Australia.
William D RawlinsonImmunology Department, UNSW Sydney, Faculty of Medicine, Sydney, NSW, Australia.
Daniel ChristImmunology Department, Garvan Institute of Medical Research, Sydney, NSW, Australia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antibodies against coronavirus spike protein potently protect against infection and disease, but whether such protection can be extended to variant coronaviruses is unclear. This is exemplified by a set of iconic and well-characterized monoclonal antibodies developed after the 2003 SARS outbreak, including mAbs m396, CR3022, CR3014 and 80R, which potently neutralize SARS-CoV-1, but not SARS-CoV-2. Here, we explore antibody engineering strategies to change and broaden their specificity, enabling nanomolar binding and potent neutralization of SARS-CoV-2. Intriguingly, while many of the matured clones maintained specificity of the parental antibody, new specificities were also observed, which was further confirmed by X-ray crystallography and cryo-electron microscopy, indicating that a limited set of VH antibody domains can give rise to variants targeting diverse epitopes, when paired with a diverse VL repertoire. Our findings open up over 15 years of antibody development efforts against SARS-CoV-1 to the SARS-CoV-2 field and outline general principles for the maturation of antibody specificity against emerging viruses.

Indexed as

Antibodies, NeutralizingAntibodies, ViralAntibody SpecificityCOVID-19Cross ReactionsHumansMutagenesis, Site-DirectedSARS-CoV-2Severe acute respiratory syndrome-related coronavirusAntibodies, NeutralizingAntibodies, Viralantibody engineeringantibody maturationMonoclonal antibodiesphage displaySARS-CoV-2structural studies

Identifiers

PMID34024246
PMCPMC8158043

What OpenQuestion holds

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LicenceCC BY-NC
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.