Targeting of severe fever with thrombocytopenia syndrome virus structural proteins to the ERGIC (endoplasmic reticulum Golgi intermediate compartment) and Golgi complex

• Published in: Biomedical Research Vol. 39; no. 1; pp. 27 - 38
• Main Authors: LUNDU, Tapiwa, TSUDA, Yoshimi, ITO, Ryo, SHIMIZU, Kenta, KOBAYASHI, Shintaro, YOSHII, Kentaro, YOSHIMATSU, Kumiko, ARIKAWA, Jiro, KARIWA, Hiroaki
• Format: Journal Article
• Language: English
• Published: Japan Biomedical Research Press 01.01.2018; Japan Science and Technology Agency
• Subjects: Compartments; Confocal microscopy; DNA-directed RNA polymerase; Endoplasmic reticulum; Fever; Glycoproteins; Golgi apparatus; Hemagglutinins; Localization; Microscopy; Nucleocapsids; Proteins; RNA polymerase; RNA-directed RNA polymerase; Structural proteins; Thrombocytopenia; Viruses
• ISSN: 0388-6107; 1880-313X; 1880-313X
• DOI: 10.2220/biomedres.39.27

Severe fever with thrombocytopenia syndrome phlebovirus (SFTSV) is a newly emerged phlebovirus identified in China, Japan, and South Korea. Phlebovirus glycoproteins (GP) play a key role in targeting viral structural components to the budding compartments in the ER–Golgi intermediate compartment (ERGIC) and Golgi complex. However, the role of SFTSV GP in targeting structural proteins to the ERGIC and Golgi complex remains unresolved. In this study, we show that SFTSV GP plays a significant role in targeting RNA-dependent RNA polymerase (L) and nucleocapsid protein (NP) to the budding sites. Confocal microscopy was used to investigate the subcellular localization of SFTSV structural proteins. In SFTSV-infected cells, GP and L localized to the ER, ERGIC and Golgi complex, whereas NP localized to the ERGIC and Golgi complex. In addition, GP colocalized with L and NP in infected cells. In cells singly transfected with GP, L or NP, GP localized to the same subcellular compartments as in infected cells. However, L or NP alone did not localize to the ER, ERGIC, or Golgi complex. Cotransfection experiments showed that GP altered the localization of L to the ERGIC and Golgi complex but not that of NP. Interestingly, plasmid-expressed NP fused with a hemagglutinin tag localized to the ERGIC and Golgi complex when expressed in SFTSV-infected cells and colocalised with GP, suggesting that GP plays a role in the subcellular localization of L and NP in infected cells. Thus, the SFTSV structural components start to assemble at the ERGIC to Golgi complex. GP is required for transporting L and NP to the ERGIC and Golgi complex. In addition, targeting of NP requires interaction with other factors besides GP.