Two amino acid pairs in the Gc glycoprotein of severe fever with thrombocytopenia syndrome virus responsible for the enhanced virulence
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
39541832
DOI
10.1016/j.virol.2024.110294
PII: S0042-6822(24)00318-0
Knihovny.cz E-resources
- Keywords
- Gc protein, Mouse model, SFTS virus, Virulence,
- MeSH
- Glycoproteins genetics metabolism MeSH
- Bunyaviridae Infections virology MeSH
- Cats MeSH
- Humans MeSH
- Mice, Knockout * MeSH
- Mice MeSH
- Phlebovirus * genetics pathogenicity isolation & purification MeSH
- Viral Envelope Proteins genetics metabolism MeSH
- Receptor, Interferon alpha-beta genetics MeSH
- Severe Fever with Thrombocytopenia Syndrome * virology MeSH
- Virulence MeSH
- Animals MeSH
- Check Tag
- Cats MeSH
- Humans MeSH
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Glycoproteins MeSH
- Viral Envelope Proteins MeSH
- Receptor, Interferon alpha-beta MeSH
Severe fever with thrombocytopenia syndrome (SFTS) is a significant public health concern, with a high fatality rate in humans and cats. In this study, we explored the genetic determinants that contribute to the different virulence of SFTS virus (SFTSV) based on Tk-F123 and Ng-F264 strains isolated from cats. Tk-F123 was 100% lethal in type I interferon receptor-knockout mice, whereas Ng-F264 exhibited no fatality. We identified a pair of amino acid residues in the Gc protein, glycine and serine, at residues 581 and 934, respectively, derived from Tk-F123, leading to a fatal infection. Those in Ng-F264 were arginine and asparagine. These results suggest that this pair of residues affects the Gc protein function and regulates SFTSV virulence. Our findings provide useful clues for the elucidation of viral pathogenicity and the development of effective live-attenuated vaccines and antiviral strategies.
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