ArticleThe Journal of general virology2017
Determinants of the VP1/2A junction cleavage by the 3C protease in foot-and-mouth disease virus-infected cells.
Article in The Journal of general virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- Foot-and-mouth disease virus 3C protease as virulence determinant plays multiple roles in cleaving viral polyprotein and host factors.Virulence · 2026Review
- Development and immunogenicity of adenoviral Fc-fused FMDV virus-like particle vaccine in swine.The veterinary quarterly · 2025Article
- 3C protease-independent production of foot-and-mouth disease virus-like particles in Pichia pastoris.Applied microbiology and biotechnology · 2025Article
- Cell Culture Adaptive Amino Acid Substitutions in FMDV Structural Proteins: A Key Mechanism for Altered Receptor Tropism.Viruses · 2024Review
- Epidemiological Surveillance and Mutational Pattern Analysis of Foot-and-Mouth Disease Outbreaks in Bangladesh during 2012-2021.Transboundary and emerging diseases · 2023Article
- Synthesis and Initial Evaluation of a Novel Fluorophore for Selective FMDV 3C Protease Detection.Molecules (Basel, Switzerland) · 2020Article
- Cell culture propagation of foot-and-mouth disease virus: adaptive amino acid substitutions in structural proteins and their functional implications.Virus genes · 2020Review
- Identification of plasticity and interactions of a highly conserved motif within a picornavirus capsid precursor required for virus infectivity.Scientific reports · 2019Article
- Identification of a short, highly conserved, motif required for picornavirus capsid precursor processing at distal sites.PLoS pathogens · 2019Article
- Emergency Services of Viral RNAs: Repair and Remodeling.Microbiology and molecular biology reviews : MMBR · 2018Review
- Modifications to the Foot-and-Mouth Disease Virus 2A Peptide: Influence on Polyprotein Processing and Virus Replication.Journal of virology · 2018Article
- Selection of functional 2A sequences within foot-and-mouth disease virus; requirements for the NPGP motif with a distinct codon bias.RNA (New York, N.Y.) · 2018Article
- RNAi combining Sleeping Beauty transposon system inhibits ex vivo expression of foot-and-mouth disease virus VP1 in transgenic sheep cells.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The foot-and-mouth disease virus (FMDV) capsid precursor, P1-2A, is cleaved by FMDV 3C protease to yield VP0, VP3, VP1 and 2A. Cleavage of the VP1/2A junction is the slowest. Serotype O FMDVs with uncleaved VP1-2A (having a K210E substitution in VP1; at position P2 in cleavage site) have been described previously and acquired a second site substitution (VP1 E83K) during virus rescue. Furthermore, introduction of the VP1 E83K substitution alone generated a second site change at the VP1/2A junction (2A L2P, position P2' in cleavage site). These virus adaptations have now been analysed using next-generation sequencing to determine sub-consensus level changes in the virus; this revealed other variants within the E83K mutant virus population that changed residue VP1 K210. The construction of serotype A viruses with a blocked VP1/2A cleavage site (containing K210E) has now been achieved. A collection of alternative amino acid substitutions was made at this site, and the properties of the mutant viruses were determined. Only the presence of a positively charged residue at position P2 in the cleavage site permitted efficient cleavage of the VP1/2A junction, consistent with analyses of diverse FMDV genome sequences. Interestingly, in contrast to the serotype O virus results, no second site mutations occurred within the VP1 coding region of serotype A viruses with the blocked VP1/2A cleavage site. However, some of these viruses acquired changes in the 2C protein that is involved in enterovirus morphogenesis. These results have implications for the testing of potential antiviral agents targeting the FMDV 3C protease.
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