ArticleJournal of virology2002
Alphavirus minus-strand RNA synthesis: identification of a role for Arg183 of the nsP4 polymerase.
Article in Journal of virology, 2002. 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, 27 citations in OpenAlex.
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- Dissecting the Role of E2 Protein Domains in Alphavirus Pathogenicity.Journal of virology · 2015Article
- Alphavirus RNA synthesis and non-structural protein functions.The Journal of general virology · 2015Review
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- Requirement for the amino-terminal domain of sindbis virus nsP4 during virus infection.Journal of virology · 2011Article
- Role for conserved residues of sindbis virus nonstructural protein 2 methyltransferase-like domain in regulation of minus-strand synthesis and development of cytopathic infection.Journal of virology · 2008Article
- Role for nsP2 proteins in the cessation of alphavirus minus-strand synthesis by host cells.Journal of virology · 2006Article
- A mutant of Sindbis virus which is able to replicate in cells with reduced CTP makes a replicase/transcriptase with a decreased Km for CTP.Journal of virology · 2004Article
- Identification of the amino acid sequence in Sindbis virus nsP4 that binds to the promoter for the synthesis of the subgenomic RNA.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Functional analysis of nsP3 phosphoprotein mutants of Sindbis virus.Journal of virology · 2003Article
- Alphavirus minus-strand synthesis and persistence in mouse embryo fibroblasts derived from mice lacking RNase L and protein kinase R.Journal of virology · 2003Article
- Modification of Asn374 of nsP1 suppresses a Sindbis virus nsP4 minus-strand polymerase mutant.Journal of virology · 2002Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
A partially conserved region spanning amino acids 142 to 191 of the Sindbis virus (SIN) nsP4 core polymerase is implicated in host restriction, elongation, and promoter recognition. We extended the analysis of this region by substituting Ser, Ala, or Lys for a highly conserved Arg183 residue immediately preceding its absolutely conserved Ser184-Ala-Val-Pro-Ser188 sequence. In chicken cells, the nsP4 Arg183 mutants had a nonconditionally lethal, temperature-sensitive (ts) growth phenotype caused by a ts defect in minus-strand synthesis whose extent varied with the particular amino acid substituted (Ser>Ala>Lys). Plus-strand synthesis by nsP4 Arg183 mutant polymerases was unaffected when corrected for minus-strand numbers, although 26S mRNA synthesis was enhanced at the elevated temperature compared to wild type. The ts defect was not due to a failure to form or accumulate nsP4 at 40 degrees C. In contrast to their growth in chicken cells, the nsP4 Arg183 mutants replicated equally poorly, if at all, in mosquito cells. We conclude that Arg183 within the Pro180-Asn-Ile-Arg-Ser184 sequence of the SIN nsP4 polymerase contributes to the efficient initiation of minus strands or the formation of its replicase and that a host factor(s) participates in this event.
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