title: Complementation of the human adenovirus type 5 VA RNAI defect by the Vaccinia virus E3L protein and serotype-specific VA RNAIs.
abstract: Human adenoviruses (HAdVs) encode for multifunctional non-coding virus-associated (VA) RNAs, which function as powerful suppressors of the cellular interferon (IFN) and RNA interference (RNAi) systems. In this study we tested the ability of various plant and animal virus encoded RNAi and IFN suppressor proteins to functionally substitute for the HAdV-5 VA RNAI. Our results revealed that only the Vaccinia virus (VACV) E3L protein was able to substitute for the HAdV-5 VA RNAI functions in virus-infected cells. Interestingly, the E3L protein rescues the translational defect but does not stimulate viral capsid mRNA accumulation observed with VA RNA. We further show that the E3L C-terminal region containing the dsRNA-binding domain is needed to enhance VA RNAI mutant virus replication. Additionally, we show that the HAdV-4 and HAdV-37 VA RNAI are more effective than the HAdV-5 VA RNAI in rescuing virus replication.
authors.affiliation: Department of Medical Biochemistry and Microbiology, Uppsala University, Husargatan 3, BMC, Box 582, Uppsala, Sweden.
authors.forename: Raviteja
authors.initials: R
authors.lastname: Inturi
authors.affiliation: Department of Medical Biochemistry and Microbiology, Uppsala University, Husargatan 3, BMC, Box 582, Uppsala, Sweden.
authors.forename: Wael
authors.initials: W
authors.lastname: Kamel
authors.affiliation: Department of Medical Biochemistry and Microbiology, Uppsala University, Husargatan 3, BMC, Box 582, Uppsala, Sweden.
authors.forename: Göran
authors.initials: G
authors.lastname: Akusjärvi
authors.affiliation: Department of Medical Biochemistry and Microbiology, Uppsala University, Husargatan 3, BMC, Box 582, Uppsala, Sweden. Electronic address: Tanel.Punga@imbim.uu.se.
authors.forename: Tanel
authors.initials: T
authors.lastname: Punga
mesh_terms: D000260:Adenoviruses, Human / Q000235:genetics* / Q000378:metabolism; D002213:Capsid / Q000378:metabolism; D015967:Gene Expression Regulation, Viral; D005816:Genetic Complementation Test; D057809:HEK293 Cells; D054884:Host-Pathogen Interactions; D006801:Humans; D009842:Oligopeptides / Q000378:metabolism; D010957:Plasmids / Q000737:chemistry / Q000378:metabolism; D034622:RNA Interference; D012333:RNA, Messenger / Q000037:antagonists & inhibitors / Q000235:genetics* / Q000378:metabolism; D012367:RNA, Viral / Q000037:antagonists & inhibitors / Q000235:genetics* / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000235:genetics* / Q000378:metabolism; D065288:Serogroup; D014162:Transfection; D014616:Vaccinia virus / Q000235:genetics* / Q000378:metabolism; D014764:Viral Proteins / Q000235:genetics* / Q000378:metabolism; D014779:Virus Replication
chemical_list: C081374:E3L protein, Vaccinia virus; D009842:Oligopeptides; D012333:RNA, Messenger; D012367:RNA, Viral; D016601:RNA-Binding Proteins; D014764:Viral Proteins; C085706:FLAG peptide
keywords: Adenovirus; E3L protein; Interferon response; RNAi; VA RNA; Vaccinia virus