{
   "source_x": "PMC",
   "title": "Ovarian Tumor (OTU)-domain Containing Viral Proteases Evade Ubiquitin- and ISG15-dependent Innate Immune Responses",
   "doi": "http://dx.doi.org/10.1016/j.chom.2007.09.014",
   "pmcid": "PMC2184509",
   "abstract": "Ubiquitin (Ub) and interferon stimulated gene product 15 (ISG15) reversibly conjugate to proteins via a conserved LRLRGG C-terminal motif, mediating important innate antiviral responses. The ovarian tumor (OTU) domain represents a superfamily of predicted proteases found in eukaryotic, bacterial and viral proteins, some of which have Ub-deconjugating activity. We show that the OTU domain-containing proteases of nairoviruses and arteriviruses hydrolyze Ub and ISG15 from cellular target proteins. This broad activity contrasts with the target specificity of known mammalian OTU domain-containing proteins. The biological significance of this activity of viral OTU domain-containing proteases was evidenced by their capacity to inhibit NF-\u03baB dependent signaling and to antagonize the antiviral effects of ISG15 during Sindbis virus infection in vivo. The deconjugating activity of viral OTU proteases represents a novel viral immune evasion mechanism that inhibits Ub-and ISG15-dependent antiviral pathways.",
   "authors": [
      "['Frias-Staheli, Natalia', 'Giannakopoulos, Nadia V.', 'Kikkert, Marjolein', 'Taylor, Shannon L.', 'Bridgen, Anne', 'Paragas, Jason J.', 'Richt, Juergen A.', 'Rowland, Raymond R.', 'Schmaljohn, Connie S.', 'Lenschow, Deborah J.', 'Snijder, Eric J.', 'Garc\u00eda-Sastre, Adolfo', 'Virgin, Herbert Whiting']"
   ],
   "id": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2184509"
}