Gori Savellini Gianni, Gandolfo Claudia, Cusi Maria Grazia
Department of Medical Biotechnologies, Microbiology Section, University of Siena, Italy.
Department of Medical Biotechnologies, Microbiology Section, University of Siena, Italy.
Virology. 2015 Dec;486:255-62. doi: 10.1016/j.virol.2015.09.021. Epub 2015 Oct 27.
Toscana Virus (TOSV) is a Phlebovirus responsible for central nervous system (CNS) injury in humans. The TOSV non-structural protein (NSs), which interacting with RIG-I leads to its degradation, was analysed in the C terminus fragment in order to identify its functional domains. To this aim, two C-terminal truncated NSs proteins, Δ1C-NSs (aa 1-284) and Δ2C-NSs (aa 1-287) were tested. Only Δ1C-NSs did not present any inhibitory effect on RIG-I and it showed a greater stability than the whole NSs protein. Moreover, the deletion of the TLQ aa sequence interposed between the two ΔC constructs caused a greater accumulation of the protein with a weak inhibitory effect on RIG-I, indicating some involvement of these amino acids in the NSs activity. Nevertheless, all the truncated proteins were still able to interact with RIG-I, suggesting that the domains responsible for RIG-I signaling and RIG-I interaction are mapped on different regions of the protein.
托斯卡纳病毒（TOSV）是一种白蛉病毒，可导致人类中枢神经系统（CNS）损伤。为了鉴定其功能结构域，对与RIG-I相互作用导致其降解的TOSV非结构蛋白（NSs）的C末端片段进行了分析。为此，测试了两种C末端截短的NSs蛋白，即Δ1C-NSs（氨基酸1-284）和Δ2C-NSs（氨基酸1-287）。只有Δ1C-NSs对RIG-I没有任何抑制作用，并且它比完整的NSs蛋白表现出更高的稳定性。此外，在两个ΔC构建体之间插入的TLQ氨基酸序列的缺失导致该蛋白积累更多，对RIG-I的抑制作用较弱，表明这些氨基酸在NSs活性中有所参与。然而，所有截短蛋白仍能够与RIG-I相互作用，这表明负责RIG-I信号传导和RIG-I相互作用的结构域位于该蛋白的不同区域。
