ReviewVeterinary research2015
Multifunctional roles of leader protein of foot-and-mouth disease viruses in suppressing host antiviral responses.
Review in Veterinary research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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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.
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Who cites it
25 citing papers in PubMed, 37 citations in OpenAlex.
- The La Region of Foot-and-Mouth Disease Virus: Essential for L Protein Cellular Distribution but Not Functional Activity.International journal of molecular sciences · 2026Article
- Epidemiology and economics of foot-and-mouth disease: current understanding 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
- RING finger protein 5 is a key anti-FMDV host factor through inhibition of virion assembly.PLoS pathogens · 2025Article
- Heat shock protein 70 enhances viral replication by stabilizing Senecavirus A nonstructural proteins L and 3D.Veterinary research · 2024Article
- Review
- Innate sensing of picornavirus infection involves cGAS-STING-mediated antiviral responses triggered by mitochondrial DNA release.PLoS pathogens · 2023Article
- Establishing an In Vitro System to Assess How Specific Antibodies Drive the Evolution of Foot-and-Mouth Disease Virus.Viruses · 2022Article
- FMDV 3A Antagonizes the Effect of ANXA1 to Positively Modulate Viral Replication.Journal of virology · 2022Article
- Article
- Inhibition of Antiviral Innate Immunity by Foot-and-Mouth Disease Virus LJournal of virology · 2021Article
- A Comprehensive Review of the Immunological Response against Foot-and-Mouth Disease Virus Infection and Its Evasion Mechanisms.Vaccines · 2020Review
- Foot-and-Mouth Disease Virus 3B Protein Interacts with Pattern Recognition Receptor RIG-I to Block RIG-I-Mediated Immune Signaling and Inhibit Host Antiviral Response.Journal of immunology (Baltimore, Md. : 1950) · 2020Article
- Modification of the second translation initiation site restricts the replication of foot-and-mouth disease virus in PK-15 cells.Applied microbiology and biotechnology · 2020Article
- Genetic Determinants of Altered Virulence of Type O Foot-and-Mouth Disease Virus.Journal of virology · 2020Article
- NLRP3 inflammasome activation by Foot-and-mouth disease virus infection mainly induced by viral RNA and non-structural protein 2B.RNA biology · 2020Article
- Advances in Foot-and-Mouth Disease Virus Proteins Regulating Host Innate Immunity.Frontiers in microbiology · 2020Review
- Foot-and-Mouth Disease Virus Antagonizes NOD2-Mediated Antiviral Effects by Inhibiting NOD2 Protein Expression.Journal of virology · 2019Article
- Irreversible inactivation of ISG15 by a viral leader protease enables alternative infection detection strategies.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Plant Viral Proteases: Beyond the Role of Peptide Cutters.Frontiers in plant science · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Foot-and-mouth disease virus (FMDV) leader protein (L(pro)) is a papain-like proteinase, which plays an important role in FMDV pathogenesis. L(pro) exists as two forms, Lab and Lb, due to translation being initiated from two different start codons separated by 84 nucleotides. L(pro) self-cleaves from the nascent viral polyprotein precursor as the first mature viral protein. In addition to its role as a viral proteinase, L(pro) also has the ability to antagonize host antiviral effects. To promote FMDV replication, L(pro) can suppress host antiviral responses by three different mechanisms: (1) cleavage of eukaryotic translation initiation factor 4 γ (eIF4G) to shut off host protein synthesis; (2) inhibition of host innate immune responses through restriction of interferon-α/β production; and (3) L(pro) can also act as a deubiquitinase and catalyze deubiquitination of innate immune signaling molecules. In the light of recent functional and biochemical findings regarding L(pro), this review introduces the basic properties of L(pro) and the mechanisms by which it antagonizes host antiviral responses.
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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.