Two amino acid pairs in the Gc glycoprotein of severe fever with thrombocytopenia syndrome virus responsible for the enhanced virulence

Shelly Wulandari, Samuel Nyampong, Michaela Beránková, Sithumini M.W. Lokupathirage, Kumiko Yoshimatsu, Hiroshi Shimoda, Daisuke Hayasaka

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Article number110294
JournalVirology
Volume601
DOIs
Publication statusPublished - Jan 2025

Keywords

  • Gc protein
  • Mouse model
  • SFTS virus
  • Virulence

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