title: Different functions of the common P/V/W and V-specific domains of rinderpest virus V protein in blocking IFN signalling.
abstract: The V proteins of paramyxoviruses are composed of two evolutionarily distinct domains, the N-terminal 75 % being common to the viral P, V and W proteins, and not highly conserved between viruses, whilst the remaining 25 % consists of a cysteine-rich V-specific domain, which is conserved across almost all paramyxoviruses. There is evidence supporting a number of different functions of the V proteins of morbilliviruses in blocking the signalling pathways of type I and II IFNs, but it is not clear which domains of V are responsible for which activities and whether all these activities are required for effective blockade of IFN signalling. We have shown here that the two domains of rinderpest virus V protein have distinct functions: the N-terminal domain acted to bind STAT1, whilst the C-terminal V-specific domain interacted with the IFN receptor-associated kinases Jak1 and Tyk2. Effective blockade of IFN signalling required the intact V protein.
authors.affiliation: The Pirbright Institute, Ash Road, Pirbright, Surrey GU24 0NF, UK.
authors.forename: Senthil K
authors.initials: SK
authors.lastname: Chinnakannan
authors.affiliation: The Pirbright Institute, Ash Road, Pirbright, Surrey GU24 0NF, UK.
authors.forename: Barbara
authors.initials: B
authors.lastname: Holzer
authors.affiliation: The Pirbright Institute, Ash Road, Pirbright, Surrey GU24 0NF, UK.
authors.forename: Beatriz Sanz
authors.initials: BS
authors.lastname: Bernardo
authors.affiliation: The Pirbright Institute, Ash Road, Pirbright, Surrey GU24 0NF, UK.
authors.forename: Sambit K
authors.initials: SK
authors.lastname: Nanda
authors.affiliation: The Pirbright Institute, Ash Road, Pirbright, Surrey GU24 0NF, UK.
authors.forename: Michael D
authors.initials: MD
authors.lastname: Baron
mesh_terms: D000818:Animals; D002460:Cell Line; D006801:Humans; D007372:Interferons / Q000235:genetics / Q000378:metabolism*; D053613:Janus Kinase 1 / Q000235:genetics / Q000378:metabolism; D010766:Phosphorylation; D017434:Protein Structure, Tertiary; D012301:Rinderpest / Q000201:enzymology / Q000235:genetics / Q000378:metabolism* / Q000821:virology; D012302:Rinderpest virus / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D050794:STAT1 Transcription Factor / Q000235:genetics / Q000378:metabolism; D015398:Signal Transduction; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D050794:STAT1 Transcription Factor; C494079:STAT1 protein, human; C502891:V protein, Paramyxovirus; D014764:Viral Proteins; D007372:Interferons; D053613:Janus Kinase 1