Evidence map›Paper›PMID 40176146›Full record

ArticleVeterinary research2025

Epitope mapping of a neutralizing antibody against rabbit hemorrhagic disease virus GI.2.

Ana Podadera, Mila Leuthold, José Manuel Martín-Alonso, Rosa Casais, Angel Luis Álvarez, M J Lobo-Castañón, Francisco Parra, Kevin Paul Dalton

Abstract read
In one paragraph

Article in Veterinary research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

8 authors.

Ana PodaderaInstituto Universitario de Biotecnología de Asturias, Departamento de Bioquímica y Biología Molecular, Edificio Santiago Gascón, Universidad de Oviedo, Campus El Cristo, 33006, Oviedo, Spain.
Mila LeutholdMedicinal Chemistry, Institute of Pharmacy and Molecular Biotechnology, University of Heidelberg, 69120, Heidelberg, Germany.
José Manuel Martín-AlonsoInstituto Universitario de Biotecnología de Asturias, Departamento de Bioquímica y Biología Molecular, Edificio Santiago Gascón, Universidad de Oviedo, Campus El Cristo, 33006, Oviedo, Spain.
Rosa CasaisSERIDA, Servicio Regional de Investigación y Desarrollo Agroalimentario, Centro de Biotecnología Animal, 33394, Gijón, Asturias, Spain.
Angel Luis ÁlvarezInstituto Universitario de Biotecnología de Asturias, Departamento de Bioquímica y Biología Molecular, Edificio Santiago Gascón, Universidad de Oviedo, Campus El Cristo, 33006, Oviedo, Spain.
M J Lobo-CastañónDepartamento de Química Física y Analítica, Universidad de Oviedo, Av. Julián Clavería 8, 33006, Oviedo, Spain.
Francisco ParraInstituto Universitario de Biotecnología de Asturias, Departamento de Bioquímica y Biología Molecular, Edificio Santiago Gascón, Universidad de Oviedo, Campus El Cristo, 33006, Oviedo, Spain.
Kevin Paul DaltonInstituto Universitario de Biotecnología de Asturias, Departamento de Bioquímica y Biología Molecular, Edificio Santiago Gascón, Universidad de Oviedo, Campus El Cristo, 33006, Oviedo, Spain. daltonkevin@uniovi.es.ORCID http://orcid.org/0000-0002-7086-1979

Funding

Ministerio de Economía y Competitividad MCI-21-PID2020-120349RB-100
6 · The paper itself

Abstract

In 2010, rabbit hemorrhagic disease virus (RHDV) GI.2 emerged, and unlike RHDV GI.1, it caused mortality in young rabbits, while existing vaccines were not fully protective. The GI.2-specific monoclonal antibody (mAb) 2D9 has been used as a tool to discriminate between these viruses in diagnostic tests. In this study, we mapped the binding epitope for 2D9 on the GI.2 The VP60 capsid protein demonstrated the neutralizing capacity of this mAb, which was able to prevent GI.2 infections in an experimental challenge. Our results suggest that external loops (1, 4 and 5) in the P2 subdomain of VP60 contribute to the discontinuous neutralizing epitope recognized by mAb 2D9. Moreover, analysis of naturally occurring RHDV GI.2 isolates revealed key residues involved in mAb 2D9 binding that are under selective pressure. The findings described in this work provide valuable information regarding our understanding of virus neutralization and immune escape, which may help in the development of novel antiviral compounds.

Indexed as

Antibodies, NeutralizingAntibodies, ViralCaliciviridae InfectionsEpitope MappingHemorrhagic Disease Virus, RabbitAnimalsAntibodies, MonoclonalEpitopesRabbitsViral Structural ProteinsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralEpitopesviral protein 60, rabbit hemorrhagic disease virusViral Structural ProteinsmAb-2D9/RHDV GI.2P-domainRHDV GI.2virus neutralizationVLP

Identifiers

PMID40176146
PMCPMC11963670

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LicenceCC BY
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Registered trials

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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.