Two amino acid pairs in the Gc glycoprotein of severe fever with thrombocytopenia syndrome virus responsible for the enhanced virulence
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
39541832
DOI
10.1016/j.virol.2024.110294
PII: S0042-6822(24)00318-0
Knihovny.cz E-zdroje
- Klíčová slova
- Gc protein, Mouse model, SFTS virus, Virulence,
- MeSH
- glykoproteiny genetika metabolismus MeSH
- infekce viry z čeledi Bunyaviridae virologie MeSH
- kočky MeSH
- lidé MeSH
- myši knockoutované * MeSH
- myši MeSH
- Phlebovirus * genetika patogenita izolace a purifikace MeSH
- proteiny virového obalu genetika metabolismus MeSH
- receptor interferonu alfa-beta genetika MeSH
- těžká forma horečky s trombocytopenickým syndromem * virologie MeSH
- virulence MeSH
- zvířata MeSH
- Check Tag
- kočky MeSH
- lidé MeSH
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- glykoproteiny MeSH
- proteiny virového obalu MeSH
- receptor interferonu alfa-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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