ArticleJournal of virology2009
Random mutagenesis defines a domain of Theiler's virus leader protein that is essential for antagonism of nucleocytoplasmic trafficking and cytokine gene expression.
Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 33 citations in OpenAlex.
- Cardiovirus-Mediated PKR inhibition results from nucleocytoplasmic trafficking disruption.PLoS pathogens · 2025Article
- The leader proteins of Theiler's virus and Boone cardiovirus use a combination of short linear motifs (SLiMs) to target RSK kinases to the nuclear pore complex.Journal of virology · 2025Article
- The "DDVF" motif used by viral and bacterial proteins to hijack RSK kinases mimics a short linear motif (SLiM) found in proteins related to the RAS-ERK MAP kinase pathway.PLoS pathogens · 2025Article
- Virus Infection and mRNA Nuclear Export.International journal of molecular sciences · 2023Review
- Cardiovirus leader proteins retarget RSK kinases toward alternative substrates to perturb nucleocytoplasmic traffic.PLoS pathogens · 2022Article
- A case of convergent evolution: Several viral and bacterial pathogens hijack RSK kinases through a common linear motif.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Inflammatory monocytes and microglia play independent roles in inflammatory ictogenesis.Journal of neuroinflammation · 2022Article
- PKR activity modulation by phosphomimetic mutations of serine residues located three aminoacids upstream of double-stranded RNA binding motifs.Scientific reports · 2021Article
- The Leader Protein of Theiler's Virus Prevents the Activation of PKR.Journal of virology · 2019Article
- Intracellular localization of Saffold virus Leader (L) protein differs in Vero and HEp-2 cells.Emerging microbes & infections · 2016Article
- Interferon-stimulated genes-essential antiviral effectors implicated in resistance to Theiler's virus-induced demyelinating disease.Journal of neuroinflammation · 2015Article
- Three cardiovirus Leader proteins equivalently inhibit four different nucleocytoplasmic trafficking pathways.Virology · 2015Article
- Picornaviruses and nuclear functions: targeting a cellular compartment distinct from the replication site of a positive-strand RNA virus.Frontiers in microbiology · 2015Review
- Recombinant Encephalomyocarditis Viruses Elicit Neutralizing Antibodies against PRRSV and CSFV in Mice.PloS one · 2015Article
- Binding interactions between the encephalomyocarditis virus leader and protein 2A.Journal of virology · 2014Article
- AMP-activated protein kinase phosphorylates EMCV, TMEV and SafV leader proteins at different sites.Virology · 2014Article
- Viral subversion of nucleocytoplasmic trafficking.Traffic (Copenhagen, Denmark) · 2014Review
- Encephalomyocarditis virus leader is phosphorylated by CK2 and syk as a requirement for subsequent phosphorylation of cellular nucleoporins.Journal of virology · 2014Article
- Encephalomyocarditis virus Leader protein hinge domain is responsible for interactions with Ran GTPase.Virology · 2013Article
- Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The leader protein of cardioviruses, Theiler's murine encephalomyelitis virus (TMEV) and encephalomyocarditis virus (EMCV), is a multifunctional protein known to antagonize type I interferon expression and to interfere with nucleocytoplasmic trafficking of host proteins and mRNA. This protein plays an important role in the capacity of TMEV to establish persistent infection of the central nervous system. Mutant forms of the TMEV leader protein were generated by random mutagenesis and selected after retroviral transduction on the basis of the loss of the highly toxic nature of this protein. Selected mutations define a short C-terminal domain of the leader conserved in TMEV and Saffold virus but lacking in the EMCV leader and thus called the Theilo domain. Mutations in this domain had a dramatic impact on TMEV L protein activity. Like the zinc finger mutation, Theilo domain mutations affected all of the activities of the L protein tested: interferon gene transcription and IRF-3 dimerization antagonism, alteration of nucleocytoplasmic trafficking, nucleoporin 98 hyperphosphorylation, and viral persistence in vivo. This suggests that the Zn finger and the Theilo domain of the protein cooperate for function. Moreover, the fact that all of the activities tested were affected by these mutations suggests that the various leader protein functions are somehow coupled.
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Registered trials
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