Identification of the amino acid residue important for fusion of severe fever with thrombocytopenia syndrome virus glycoprotein
| Autor: | Kengo Kawachi, Masayuki Shimojima, Miyuki Kimura, Shigeru Morikawa, Manabu Igarashi, Hideki Tani, Masayuki Saijo, Satoshi Taniguchi, Shuetsu Fukushi |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Phlebovirus
Arginine Bioinformatics Giant Cells Cell Fusion Serine 03 medical and health sciences Virology medicine 030304 developmental biology chemistry.chemical_classification 0303 health sciences Syncytium biology 030302 biochemistry & molecular biology SFTS virus Lipid bilayer fusion Virus Internalization biology.organism_classification medicine.disease Severe fever with thrombocytopenia syndrome Amino Acid Substitution chemistry Mutagenesis Site-Directed Glycoprotein Viral Fusion Proteins Severe fever with thrombocytopenia syndrome virus |
| Zdroj: | Virology. 535:102-110 |
| ISSN: | 0042-6822 |
| Popis: | Severe fever with thrombocytopenia syndrome (SFTS) is an infectious disease with a high fatality rate, caused by SFTS virus (SFTSV). Because little is known about the nature of SFTSV, basic studies are required for the developments of vaccines and effective therapies. In the present study, we identified the amino acid residue important for membrane fusion induced by the SFTSV glycoprotein (GP). Syncytium formations were observed in cells expressing the GPs of SFTSV Japanese strain (YG-1 and SPL030). In contrast, no or only weak syncytium formations were induced in cells expressing GP of SFTSV Chinese strain (HB29). The replacement of arginine at amino acid residue 962 with serine in HB29 GP (R962S) induced membrane fusion, while the replacement of serine at residue 962 with arginine in YG1 GP (S962R) did not. These data indicate that serine at residue 962 in the SFTSV-GP is critical for inducing membrane fusion and viral infection. |
| Databáze: | OpenAIRE |
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