ArticleVirology2013
Encephalomyocarditis virus Leader protein hinge domain is responsible for interactions with Ran GTPase.
Article in Virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 16 citations in OpenAlex.
- Inhibition of RAN attenuates influenza a virus replication and nucleoprotein nuclear export.Emerging microbes & infections · 2024Article
- Review
- The Leader Protein of Theiler's Virus Prevents the Activation of PKR.Journal of virology · 2019Article
- Senecavirus A 3C Protease Mediates Host Cell Apoptosis Late in Infection.Frontiers in immunology · 2019Article
- The Strategy of Picornavirus Evading Host Antiviral Responses: Non-structural Proteins Suppress the Production of IFNs.Frontiers in microbiology · 2018Review
- Cardiovirus Leader proteins bind exportins: Implications for virus replication and nucleocytoplasmic trafficking inhibition.Virology · 2016Article
- Multifunctional roles of leader protein of foot-and-mouth disease viruses in suppressing host antiviral responses.Veterinary research · 2015Review
- Three cardiovirus Leader proteins equivalently inhibit four different nucleocytoplasmic trafficking pathways.Virology · 2015Article
- Review
- Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Binding interactions between the encephalomyocarditis virus leader and protein 2A.Journal of virology · 2014Article
- Induction and suppression of innate antiviral responses by picornaviruses.Cytokine & growth factor reviews · 2014Review
- AMP-activated protein kinase phosphorylates EMCV, TMEV and SafV leader proteins at different sites.Virology · 2014Article
- Encephalomyocarditis virus leader is phosphorylated by CK2 and syk as a requirement for subsequent phosphorylation of cellular nucleoporins.Journal of virology · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Encephalomyocarditis virus (EMCV), a Cardiovirus, initiates its polyprotein with a short 67 amino acid Leader (L) sequence. The protein acts as a unique pathogenicity factor, with anti-host activities which include the triggering of nuclear pore complex hyperphosphorylation and direct binding inhibition of the active cellular transport protein, Ran GTPase. Chemical modifications and protein mutagenesis now map the Ran binding domain to the L hinge-linker region, and in particular, to amino acids 35-40. Large deletions affecting this region were shown previously to diminish Ran binding. New point mutations, especially K35Q, D37A and W40A, preserve the intact L structure, abolish Ran binding and are deficient for nucleoporin (Nup) hyperphosphorylation. Ran itself morphs through multiple configurations, but reacts most effectively with L when in the GDP format, preferably with an empty nucleotide binding pocket. Therefore, L:Ran binding, mediated by the linker-hinge, is a required step in L-induced nuclear transport inhibition.
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