ArticleJournal of virology2020
Foot-and-Mouth Disease Virus Capsid Protein VP1 Interacts with Host Ribosomal Protein SA To Maintain Activation of the MAPK Signal Pathway and Promote Virus Replication.
Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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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.
The trial behind it
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Who cites it
34 citing papers in PubMed, 52 citations in OpenAlex.
- RPSA enhances African swine fever virus entry via caveola-mediated endocytic pathway.Journal of virology · 2026Article
- Adaptive Evolution of Serotype O Foot-and-Mouth Disease Virus Under Vaccine Pressure: Combined VP1 T142/Q153 Mutations Drive Antigenic Alteration and Immune Evasion.Transboundary and emerging diseases · 2026Article
- Ribosomal protein L35 negatively regulates FMDV replication by recruiting AMFR to promote the ubiquitination and degradation of VP2.Journal of virology · 2025Article
- Membrane protein CRISPR screen identifies RPSA as an essential host factor for porcine epidemic diarrhea virus replication.Journal of virology · 2025Article
- The pathogenesis of foot-and-mouth disease virus: current understandings and knowledge gaps.Veterinary research · 2025Review
- Foot-and-mouth disease: genomic and proteomic structure, antigenic sites, serotype relationships, immune evasion, recent vaccine development strategies, and future perspectives.Veterinary research · 2025Review
- HnRNPC triggers the degradation of MITA to suppress the interferon-mediated antiviral response.Veterinary research · 2025Article
- Exploring antiviral strategies to combat African swine fever.FEMS microbiology reviews · 2025Review
- Foot-and-mouth disease in Asia.Virus research · 2025Review
- Review
- The Influence of Extra-Ribosomal Functions of Eukaryotic Ribosomal Proteins on Viral Infection.Biomolecules · 2024Review
- Host miRNA and mRNA profiles during in DEF and duck after DHAV-1 infection.Scientific reports · 2024Article
- The dual role of ribosomal protein SA in pathogen infection: the key role of structure and localization.Molecular biology reports · 2024Review
- Exploring the Role of Licorice and Its Derivatives in Cell Signaling Pathway NF-Journal of nutrition and metabolism · 2024Review
- A review of foot-and-mouth disease in Ethiopia: epidemiological aspects, economic implications, and control strategies.Virology journal · 2023Review
- The Host Protein CAD Regulates the Replication of FMDV through the Function of Pyrimidines'Journal of virology · 2023Article
- Foot-and-Mouth Disease Virus: Molecular Interplays with IFN Response and the Importance of the Model.Viruses · 2022Review
- Phospho-proteomics identifies a critical role of ATF2 in pseudorabies virus replication.Virologica Sinica · 2022Article
- Differential expression profile and in-silico functional analysis of long noncoding RNA and mRNA in duck embryo fibroblasts infected with duck plague virus.BMC genomics · 2022Article
- The Role of Deubiquitinases in Virus Replication and Host Innate Immune Response.Frontiers in microbiology · 2022Review
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Foot-and-mouth disease virus (FMDV) is the causative agent of foot-and-mouth disease, a highly contagious, economically important viral disease. The structural protein VP1 plays significant roles during FMDV infection. Here, we identified that VP1 interacted with host ribosomal protein SA (RPSA). RPSA is a viral receptor for dengue virus and classical swine fever virus infections. However, the incubation of susceptible cells using the anti-RPSA antibodies did not block the infection of FMDV. Overexpression of porcine RPSA in the insusceptible cells could not trigger FMDV infection, suggesting that RPSA was not responsible for FMDV entry and infection. On the contrary, we found that overexpression of RPSA suppressed FMDV replication, and knockdown of RPSA enhanced FMDV replication. We further determined that FMDV infection activated the mitogen-activated protein kinase (MAPK) pathway and demonstrated that MAPK pathway activation was critically important for FMDV replication. RPSA negatively regulated MAPK pathway activation during FMDV infection and displayed an antiviral function. FMDV VP1 interacted with RPSA to abrogate the RPSA-mediated suppressive role in MAPK pathway activation. Together, our study indicated that MAPK pathway activation was required for FMDV replication and that host RPSA played a negatively regulatory role on MAPK pathway activation to suppress FMDV replication. FMDV VP1 bound to RPSA to promote viral replication by repressing RPSA-mediated function and maintaining the activation of MAPK signal pathway.
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Registered trials
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.