ArticleViruses2020
The Polarity of an Amino Acid at Position 1891 of Severe Fever with Thrombocytopenia Syndrome Virus L Protein Is Critical for the Polymerase Activity.
Article in Viruses, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Emerging Multi-Source Transmission of SFTS Virus on a Remote Japanese Island: A One-Health Perspective.International journal of molecular sciences · 2026Article
- Review
- Characterization of quasispecies of severe fever with thrombocytopenia syndrome virus.Journal of virology · 2025Article
- Analysis of Gene Differences Between F and B Epidemic Lineages of Bandavirus Dabieense.Microorganisms · 2025Article
- Advances in research on severe fever with thrombocytopenia syndrome virus.Frontiers in microbiology · 2025Review
- Genetic evolution and codon usage mode of SFTSV.Frontiers in microbiology · 2025Article
- Functional prediction of the potential NGLY1 mutations associated with rare disease CDG.Heliyon · 2024Article
- Genetic variants of Dabie bandavirus: classification and biological/clinical implications.Virology journal · 2023Review
- Effect of genomic variations in severe fever with thrombocytopenia syndrome virus on the disease lethality.Emerging microbes & infections · 2022Article
- Roles of the functional domains and conserved residues of the severe fever with thrombocytopenia syndrome virus L protein provide insights into the viral RNA transcription/replication mechanism.Virologica Sinica · 2022Article
- Subcellular localization of nucleocapsid protein of SFTSV and its assembly into the ribonucleoprotein complex with L protein and viral RNA.Scientific reports · 2021Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Severe fever with thrombocytopenia syndrome virus subclone B7 shows strong plaque formation and cytopathic effect induction compared with other subclones and the parental strain YG1. Compared to YG1 and the other subclones, only B7 possesses a single substitution in the L protein at the amino acid position 1891, in which N is changed to K (N1891K). In this study, we evaluate the effects of this mutation on L protein activity via a cell-based minigenome assay. Substitutions of N with basic amino acids (K or R) enhanced polymerase activity, while substitutions with an acidic amino acid (E) decreased this activity. Mutation to other neutral amino acids showed no significant effect on activity. These results suggest that the characteristic of the amino acid at position 1891 of the L protein are critical for its function, especially with respect to the charge status. Our data indicate that this C-terminal domain of the L protein may be crucial to its functions in genome transcription and viral replication.
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