Evidence map›Paper›PMID 35505237›Full record

ArticleCommunications biology2022

Pseudotyped Bat Coronavirus RaTG13 is efficiently neutralised by convalescent sera from SARS-CoV-2 infected patients.

Diego Cantoni, Martin Mayora-Neto, Nazia Thakur, Ahmed M E Elrefaey, Joseph Newman, Sneha Vishwanath, Angalee Nadesalingam, Andrew Chan, Peter Smith, Javier Castillo-Olivares and 5 more

Abstract read
In one paragraph

Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

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  15. Serological evidence of virus infection inFrontiers in public health · 2023
    Article
  16. 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

15 authors.

Diego CantoniViral Pseudotype Unit, Medway School of Pharmacy, Universities of Kent & Greenwich, Chatham, UK.
Martin Mayora-NetoViral Pseudotype Unit, Medway School of Pharmacy, Universities of Kent & Greenwich, Chatham, UK.ORCID 0000-0002-5331-5554
Nazia ThakurThe Pirbright Institute, Guildford, Surrey, GU24 0NF, UK.ORCID 0000-0002-4450-5911
Ahmed M E ElrefaeyThe Pirbright Institute, Guildford, Surrey, GU24 0NF, UK.ORCID 0000-0001-6944-9971
Joseph NewmanThe Pirbright Institute, Guildford, Surrey, GU24 0NF, UK.ORCID 0000-0003-0717-8672
Sneha VishwanathLaboratory of Viral Zoonotics, Department of Veterinary Medicine, University of Cambridge, Cambridge, UK.
Angalee NadesalingamDIOSynVax, University of Cambridge, Madingley Road, CB3-0ES, Cambridge, UK.
Andrew ChanDIOSynVax, University of Cambridge, Madingley Road, CB3-0ES, Cambridge, UK.
Peter SmithDIOSynVax, University of Cambridge, Madingley Road, CB3-0ES, Cambridge, UK.
Javier Castillo-OlivaresDIOSynVax, University of Cambridge, Madingley Road, CB3-0ES, Cambridge, UK.
Helen BaxendaleRoyal Papworth Hospital NHS Foundation Trust, Cambridge, UK.
Bryan CharlestonThe Pirbright Institute, Guildford, Surrey, GU24 0NF, UK.
Jonathan HeeneyLaboratory of Viral Zoonotics, Department of Veterinary Medicine, University of Cambridge, Cambridge, UK.ORCID 0000-0003-2702-1621
Dalan BaileyThe Pirbright Institute, Guildford, Surrey, GU24 0NF, UK. dalan.bailey@pirbright.ac.uk.ORCID 0000-0002-5640-2266
Nigel TempertonViral Pseudotype Unit, Medway School of Pharmacy, Universities of Kent & Greenwich, Chatham, UK. n.temperton@kent.ac.uk.ORCID 0000-0002-7978-3815

Funding

Biotechnology and Biological Sciences Research Council BBS/E/I/00007034Biotechnology and Biological Sciences Research Council BBS/E/I/00007038Biotechnology and Biological Sciences Research Council BBS/E/I/COV07001Department of HealthMedical Research Council MC_PC_20016Medical Research Council MR/W005611/1Wellcome Trust
6 · The paper itself

Abstract

RaTG13 is a close relative of SARS-CoV-2, the virus responsible for the COVID-19 pandemic, sharing 96% sequence similarity at the genome-wide level. The spike receptor binding domain (RBD) of RaTG13 contains a number of amino acid substitutions when compared to SARS-CoV-2, likely impacting affinity for the ACE2 receptor. Antigenic differences between the viruses are less well understood, especially whether RaTG13 spike can be efficiently neutralised by antibodies generated from infection with, or vaccination against, SARS-CoV-2. Using RaTG13 and SARS-CoV-2 pseudotypes we compared neutralisation using convalescent sera from previously infected patients or vaccinated healthcare workers. Surprisingly, our results revealed that RaTG13 was more efficiently neutralised than SARS-CoV-2. In addition, neutralisation assays using spike mutants harbouring single and combinatorial amino acid substitutions within the RBD demonstrated that both spike proteins can tolerate multiple changes without dramatically reducing neutralisation. Moreover, introducing the 484 K mutation into RaTG13 resulted in increased neutralisation, in contrast to the same mutation in SARS-CoV-2 (E484K). This is despite E484K having a well-documented role in immune evasion in variants of concern (VOC) such as B.1.351 (Beta). These results indicate that the future spill-over of RaTG13 and/or related sarbecoviruses could be mitigated using current SARS-CoV-2-based vaccination strategies.

Indexed as

ChiropteraCOVID-19AnimalsCOVID-19 SerotherapyHumansImmunization, PassiveMembrane GlycoproteinsPandemicsSARS-CoV-2Spike Glycoprotein, CoronavirusViral Envelope ProteinsMembrane GlycoproteinsSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2Viral Envelope Proteins

Identifiers

PMID35505237
PMCPMC9065041

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.