1. Two amino acid pairs in the Gc glycoprotein of severe fever with thrombocytopenia syndrome virus responsible for the enhanced virulence.
- Author
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Wulandari S, Nyampong S, Beránková M, Lokupathirage SMW, Yoshimatsu K, Shimoda H, and Hayasaka D
- Subjects
- Animals, Virulence, Mice, Cats, Receptor, Interferon alpha-beta genetics, Viral Envelope Proteins genetics, Viral Envelope Proteins metabolism, Humans, Glycoproteins genetics, Glycoproteins metabolism, Bunyaviridae Infections virology, Phlebovirus genetics, Phlebovirus pathogenicity, Phlebovirus isolation & purification, Severe Fever with Thrombocytopenia Syndrome virology, Mice, Knockout
- 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., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)
- Published
- 2025
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