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Subcellular localization of nucleocapsid protein of SFTSV and its assembly into the ribonucleoprotein complex with L protein and viral RNA
Title: | Subcellular localization of nucleocapsid protein of SFTSV and its assembly into the ribonucleoprotein complex with L protein and viral RNA |
Authors: | Lokupathirage, Sithumini M. W. Browse this author | Tsuda, Yoshimi Browse this author | Ikegame, Kodai Browse this author | Noda, Kisho Browse this author | Muthusinghe, Devinda S. Browse this author | Kozawa, Fumiya Browse this author | Manzoor, Rashid Browse this author | Shimizu, Kenta Browse this author | Yoshimatsu, Kumiko Browse this author →KAKEN DB |
Issue Date: | 26-Nov-2021 |
Publisher: | Nature Portfolio |
Journal Title: | Scientific reports |
Volume: | 11 |
Issue: | 1 |
Start Page: | 22977 |
Publisher DOI: | 10.1038/s41598-021-01985-x |
Abstract: | Severe fever with thrombocytopenia syndrome virus (SFTSV) is an emerging bunyavirus that causes novel zoonotic diseases in Asian countries including China, Japan, South Korea, and Vietnam. In phleboviruses, viral proteins play a critical role in viral particle formation inside the host cells. Viral glycoproteins (GPs) and RNA-dependent RNA polymerase (RdRp) are colocalized in the Golgi apparatus and endoplasmic reticulum-Golgi intermediate compartment (ERGIC). The nucleocapsid (N) protein was widely expressed in the cytoplasm, even in cells coexpressing GP. However, the role of SFTSV N protein remains unclear. The subcellular localization of SFTSV structural proteins was investigated using a confocal microscope. Subsequently, minigenome and immunoprecipitation assays were carried out. The N protein interacts with viral RNA (vRNA) and further shows translational activity with RdRp which is L protein and localized in the ERGIC and Golgi apparatus when co-expressed with GP. On the other hand, mutant N protein did not interact with vRNA either localized in the ERGIC or Golgi apparatus. The interaction between the N protein of SFTSV and vRNA is important for the localization of viral proteins and viral assembly. This study provides useful insights into the life cycle of SFTSV, which will lead to the detection of antiviral targets. |
Type: | article |
URI: | http://hdl.handle.net/2115/83951 |
Appears in Collections: | 遺伝子病制御研究所 (Institute for Genetic Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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