Nuclear TRIM25 Specifically Targets Influenza Virus Ribonucleoproteins to Block the Onset of RNA Chain Elongation

Content Provider	Scilit
Author	Meyerson, Nicholas R. Zhou, Ligang Guo, Yusong R. Zhao, Chen Tao, Yizhi J. Krug, Robert M. Sawyer, Sara L.
Copyright Year	2017
Description	Journal: Cell host & microbe Summary TRIM25 is an E3 ubiquitin ligase that activates RIG-I to promote the antiviral interferon response. The NS1 protein from all strains of influenza A virus binds TRIM25, although not all virus strains block the interferon response, suggesting alternative mechanisms for TRIM25 action. Here we present a nuclear role for TRIM25 in specifically restricting influenza A virus replication. TRIM25 inhibits viral RNA synthesis through a direct mechanism that is independent of its ubiquitin ligase activity and the interferon pathway. This activity can be inhibited by the viral NS1 protein. TRIM25 inhibition of viral RNA synthesis results from its binding to viral ribonucleoproteins (vRNPs), the structures containing individual viral RNA segments, the viral polymerase, and multiple viral nucleoproteins. TRIM25 binding does not inhibit initiation of capped-RNA-primed viral mRNA synthesis by the viral polymerase. Rather, the onset of RNA chain elongation is inhibited because TRIM25 prohibits the movement of RNA into the polymerase complex.
Related Links	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6309188/pdf http://www.cell.com/article/S1931312817304389/pdf
e-ISSN	19346069
DOI	10.1016/j.chom.2017.10.003
Journal	Cell host & microbe
Issue Number	5
Volume Number	22
Language	English
Publisher	Elsevier BV
Publisher Date	2017-10-26
Access Restriction	Open
Subject Keyword	Journal: Cell host & microbe Cell Biology Influenza Virus Nuclear Trim25 Viral Ribonucleoproteins Viral Rna Synthesis
Content Type	Text
Resource Type	Article