| Literature DB >> 31299486 |
Hideki Tani1, Kengo Kawachi2, Miyuki Kimura3, Satoshi Taniguchi4, Masayuki Shimojima4, Shuetsu Fukushi4, Manabu Igarashi5, Shigeru Morikawa6, Masayuki Saijo7.
Abstract
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.Entities:
Keywords: Fusion epitope; Glycoprotein; Neutralizing antibody; SFTS virus
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Year: 2019 PMID: 31299486 DOI: 10.1016/j.virol.2019.06.014
Source DB: PubMed Journal: Virology ISSN: 0042-6822 Impact factor: 3.616