ArticleJournal of virology2013
The N terminus of Andes virus L protein suppresses mRNA and protein expression in mammalian cells.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 23 citations in OpenAlex.
- Hantavirus L protein exhibits shutoff activity mediated by its N-terminal endonuclease domain.Scientific reports · 2026Article
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- Structural characterization of the full-length Hantaan virus polymerase.PLoS pathogens · 2024Article
- Structural and functional characterization of the Sin Nombre virus L protein.PLoS pathogens · 2023Article
- The mechanism of genome replication and transcription in bunyaviruses.PLoS pathogens · 2023Review
- Conformational changes in Lassa virus L protein associated with promoter binding and RNA synthesis activity.Nature communications · 2021Article
- Review
- The RNA Replication Site of Tula Orthohantavirus Resides within a Remodelled Golgi Network.Cells · 2020Article
- Transcription and replication mechanisms of Bunyaviridae and Arenaviridae L proteins.Virus research · 2017Review
- Article
- Atomic Structure and Biochemical Characterization of an RNA Endonuclease in the N Terminus of Andes Virus L Protein.PLoS pathogens · 2016Article
- Article
- Differential lymphocyte and antibody responses in deer mice infected with Sin Nombre hantavirus or Andes hantavirus.Journal of virology · 2014Article
- Interaction between hantavirus nucleocapsid protein (N) and RNA-dependent RNA polymerase (RdRp) mutants reveals the requirement of an N-RdRp interaction for viral RNA synthesis.Journal of virology · 2014Article
- Discovery of a unique novel clade of mosquito-associated bunyaviruses.Journal of virology · 2013Article
- Uncovering the mysteries of hantavirus infections.Nature reviews. Microbiology · 2013Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Little is known about the structure and function of the 250-kDa L protein of hantaviruses, although it plays a central role in virus genome transcription and replication. When attempting to study Andes virus (ANDV) L protein in mammalian cells, we encountered difficulties. Even in a strong overexpression system, ANDV L protein could not be detected by immunoblotting. Deletion analysis revealed that the 534 N-terminal amino acid residues determine the low-expression phenotype. Inhibition of translation due to RNA secondary structures around the start codon, rapid proteasomal degradation, and reduced half-life time were excluded. However, ANDV L protein expression could be rescued upon mutation of the catalytic PD-E-K motif and further conserved residues of the putative endonuclease at the N terminus of the protein. In addition, wild-type ANDV L rather than expressible L mutants suppressed the level of L mRNA, as well as reporter mRNAs. Wild-type L protein also reduced the synthesis of cellular proteins in the high-molecular-weight range. Using expressible ANDV L mutants as a tool for localization studies, we show that L protein colocalizes with ANDV N and NSs but not Gc protein. A fraction of L protein also colocalized with the cellular processing (P) body component DCP1a. Overall, these data suggest that ANDV L protein possesses a highly active endonuclease at the N terminus suppressing the level of its own as well as heterologous mRNAs upon recombinant expression in mammalian cells.
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