Evidence map›Paper›PMID 24584474›Full record

ArticleThe Journal of general virology2014

Novel antibody binding determinants on the capsid surface of serotype O foot-and-mouth disease virus.

Amin S Asfor, Sasmita Upadhyaya, Nick J Knowles, Donald P King, David J Paton, Mana Mahapatra

Abstract read
In one paragraph

Article in The Journal of general virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

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  9. Vaccine matching and antigenic variability of foot-and-mouth disease virus serotypes O and A from 2018 Ethiopian isolates.International microbiology : the official journal of the Spanish Society for Microbiology · 2022
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  12. Review
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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

6 authors.

Amin S AsforThe Pirbright Institute, Pirbright Laboratory, Ash Road, Woking, Surrey GU24 0NF, UK.
Sasmita UpadhyayaThe Pirbright Institute, Pirbright Laboratory, Ash Road, Woking, Surrey GU24 0NF, UK.
Nick J KnowlesThe Pirbright Institute, Pirbright Laboratory, Ash Road, Woking, Surrey GU24 0NF, UK.
Donald P KingThe Pirbright Institute, Pirbright Laboratory, Ash Road, Woking, Surrey GU24 0NF, UK.
David J PatonThe Pirbright Institute, Pirbright Laboratory, Ash Road, Woking, Surrey GU24 0NF, UK.
Mana MahapatraThe Pirbright Institute, Pirbright Laboratory, Ash Road, Woking, Surrey GU24 0NF, UK.

Funding

Biotechnology and Biological Sciences Research Council BB/F009186/1Biotechnology and Biological Sciences Research Council BB/H009175/1
6 · The paper itself

Abstract

Five neutralizing antigenic sites have been described for serotype O foot-and-mouth disease viruses (FMDV) based on monoclonal antibody (mAb) escape mutant studies. However, a mutant virus selected to escape neutralization of mAb binding at all five sites was previously shown to confer complete cross-protection with the parental virus in guinea pig challenge studies, suggesting that amino acid residues outside the mAb binding sites contribute to antibody-mediated in vivo neutralization of FMDV. Comparison of the ability of bovine antisera to neutralize a panel of serotype O FMDV identified three novel putative sites at VP2-74, VP2-191 and VP3-85, where amino acid substitutions correlated with changes in sero-reactivity. The impact of these positions was tested using site-directed mutagenesis to effect substitutions at critical amino acid residues within an infectious copy of FMDV O1 Kaufbeuren (O1K). Recovered viruses containing additional mutations at VP2-74 and VP2-191 exhibited greater resistance to neutralization with both O1K guinea pig and O BFS bovine antisera than a virus that was engineered to include only mutations at the five known antigenic sites. The changes at VP2-74 and VP3-85 are adjacent to critical amino acids that define antigenic sites 2 and 4, respectively. However VP2-191 (17 Å away from VP2-72), located at the threefold axis and more distant from previously identified antigenic sites, exhibited the most profound effect. These findings extend our knowledge of the surface features of the FMDV capsid known to elicit neutralizing antibodies, and will improve our strategies for vaccine strain selection and rational vaccine design.

Indexed as

AnimalsAntibodies, NeutralizingAntibodies, ViralCapsid ProteinsCattleDNA Mutational AnalysisEpitopesFoot-and-Mouth Disease VirusGuinea PigsMolecular Sequence DataNeutralization TestsProtein BindingSequence Analysis, DNAAntibodies, NeutralizingAntibodies, ViralCapsid ProteinsEpitopes

Identifiers

PMID24584474
PMCPMC3983758

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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.