ArticleFrontiers in veterinary science2021
A High-Throughput Method to Analyze the Interaction Proteins With p22 Protein of African Swine Fever Virus
Article in Frontiers in veterinary science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- A field deployable duplex RPA-CRISPR/Cas12a assay for rapid and sensitive detection of African swine fever virus.Archives of virology · 2026Article
- Identification and Characterization of Three Novel B-Cell Epitopes in African Swine Fever Virus p22 Protein.Microorganisms · 2025Article
- The African swine fever virus p22 inhibits the JAK-STAT signaling pathway by promoting the TAX1BP1-mediated degradation of the type I interferon receptor.PLoS pathogens · 2025Article
- Article
- Advancement in the development of gene/protein-based vaccines against African swine fever virus.Current research in microbial sciences · 2024Review
- Novel p22 and p30 dual-proteins combination based indirect ELISA for detecting antibodies against African swine fever virus.Frontiers in veterinary science · 2023Article
- Examination of Immunogenic Properties of Recombinant Antigens Based on p22 Protein from African Swine Fever Virus.Journal of veterinary research · 2022Article
- Evaluation of the Function of the ASFVViruses · 2021Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
African swine fever virus (ASFV) has been identified as the agent of African swine fever, resulting in a mortality rate of nearly 100% in domestic pigs worldwide. Protein p22 encoded by gene KP177R has been reported to be localized at the inner envelope of the virus, while the function of p22 remains unclear. In this study, p22 interacting proteins of the host were identified by a high-throughput method and analyzed by Gene ontology terms and Kyoto Encyclopedia of Gene and Genomes (KEGG) pathways; numerous cellular proteins in 293-T that interacted with p22 protein were identified. These interacting proteins were related to the biological processes of binding, cell structure, signal transduction, cell adhesion, etc. At the same time, the interacted proteins participated in several KEGG pathways like ribosome, spliceosome, etc. The key proteins in the protein-protein interaction network were closely related to actin filament organization and movement, resulting in affecting the process of phagocytosis and endocytosis. A large number of proteins that interacted with p22 were identified, providing a large database, which should be very useful to elucidate the function of p22 in the near future, laying the foundation for elucidating the mechanism of ASFV.
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Registered trials
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