ArticleVirus genes2023
Identification of monoclonal antibody targeting epitope on p72 trimeric spike of African swine fever virus.
Article in Virus genes, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The trial behind it
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Establishment and Evaluation of a Multicolor Latex Microsphere-Based Lateral Flow Immunoassay for the Simultaneous Detection of Antibodies Against African and Classical Swine Fever Viruses.Transboundary and emerging diseases · 2026Article
- Identification and Characterization of Three Novel B-Cell Epitopes in African Swine Fever Virus p22 Protein.Microorganisms · 2025Article
- Identification of a New Conserved Antigenic Epitope by Specific Monoclonal Antibodies Targeting the African Swine Fever Virus Capsid Protein p17.Veterinary sciences · 2024Article
- Specific Monoclonal Antibodies against African Swine Fever Virus Protease pS273R Revealed a Novel and Conserved Antigenic Epitope.International journal of molecular sciences · 2024Article
- Identification of Linear Epitopes in the C-Terminal Region of ASFV p72 Protein.Microorganisms · 2023Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
African swine fever virus (ASFV) is highly contagious and can cause lethal disease in pigs. ASFV p72 protein is a major capsid protein that presents as trimer in the virion. Epitopes on the surface of p72 trimer are considered as protective antigens. In this study, recombinant p72 protein and p72-baculovirus were constructed and obtained. Three monoclonal antibodies (mAbs) specific to ASFV p72 protein, designated as 1A3, 2B5 and 4A5, were generated. Among them, 4A5 showed strong reactivity with ASFV infected cells. Subsequently, the epitope recognized by 4A5 was mapped and identified using a series of overlapping peptides generated from p72 protein. IFA and western blot analyses showed that 4A5 recognized the linear epitope of p72 monomer located between amino acids 245-285 and recognized the conformational epitope located at the surface and top of the p72 trimer. These findings will enrich our knowledge regarding the epitope on p72 protein and provide valuable information for further characterization of the antigenicity and molecular functions of p72 protein.
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Registered trials
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