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- W2999444576 abstract "The mosquito-borne La Crosse virus (LACV; genus Orthobunyavirus , family Peribunyaviridae , order Bunyavirales ) is prevalent in the United States and can cause severe childhood meningoencephalitis. Its main virulence factor, the nonstructural protein NSs, is a strong inhibitor of the antiviral type I interferon (IFN) system. NSs acts by imposing a global host mRNA synthesis shutoff, mediated by NSs-driven proteasomal degradation of the RPB1 subunit of RNA polymerase II. Here, we show that RPB1 degradation commences as early as 1 h postinfection, and identify the E3 ubiquitin ligase subunit Elongin C (and its binding partners Elongins A and B) as an NSs cofactor involved in RPB1 degradation and in suppression of global as well as IFN-related mRNA synthesis." @default.
- W2999444576 created "2020-01-23" @default.
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- W2999444576 date "2020-03-17" @default.
- W2999444576 modified "2023-10-15" @default.
- W2999444576 title "Elongin C Contributes to RNA Polymerase II Degradation by the Interferon Antagonist NSs of La Crosse Orthobunyavirus" @default.
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- W2999444576 doi "https://doi.org/10.1128/jvi.02134-19" @default.
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