生物
对偶(语法数字)
干扰素
关闭
病毒学
干扰素γ
细胞生物学
免疫学
细胞因子
艺术
文学类
核工程
工程类
作者
Munesh Kumar Harioudh,Joseph Pérez,Zhenlu Chong,Sharmila Nair,Lomon So,Kevin D. McCormick,Arundhati Ghosh,Lulu Shao,Rashmi Srivastava,Frank Soveg,Thomas S. Ebert,Maninjay K. Atianand,Veit Hornung,Ram Savan,Michael S. Diamond,Saumendra N. Sarkar
标识
DOI:10.1016/j.immuni.2024.02.002
摘要
Summary
In response to viral infection, how cells balance translational shutdown to limit viral replication and the induction of antiviral components like interferons (IFNs) is not well understood. Moreover, how distinct isoforms of IFN-induced oligoadenylate synthetase 1 (OAS1) contribute to this antiviral response also requires further elucidation. Here, we show that human, but not mouse, OAS1 inhibits SARS-CoV-2 replication through its canonical enzyme activity via RNase L. In contrast, both mouse and human OAS1 protect against West Nile virus infection by a mechanism distinct from canonical RNase L activation. OAS1 binds AU-rich elements (AREs) of specific mRNAs, including IFNβ. This binding leads to the sequestration of IFNβ mRNA to the endomembrane regions, resulting in prolonged half-life and continued translation. Thus, OAS1 is an ARE-binding protein with two mechanisms of antiviral activity: driving inhibition of translation but also a broader, non-canonical function of protecting IFN expression from translational shutdown.
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