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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\u2009h 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.\n          <\/jats:p>","DOI":"10.1128\/jvi.02134-19","type":"journal-article","created":{"date-parts":[[2020,1,10]],"date-time":"2020-01-10T14:04:55Z","timestamp":1578665095000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":25,"title":["Elongin C Contributes to RNA Polymerase II Degradation by the Interferon Antagonist NSs of La Crosse Orthobunyavirus"],"prefix":"10.1128","volume":"94","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1711-4800","authenticated-orcid":false,"given":"Andreas","family":"Schoen","sequence":"first","affiliation":[{"name":"Institute for Virology, FB10-Veterinary Medicine, Justus Liebig 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