1. Different functions of the common P/V/W and V-specific domains of rinderpest virus V protein in blocking IFN signalling
- Author
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Beatriz Sanz Bernardo, Senthil Chinnakannan, Michael D. Baron, Barbara Holzer, and Sambit K. Nanda
- Subjects
RNA viruses ,Rinderpest ,Rinderpest virus ,Cell Line ,Viral Proteins ,Protein structure ,Virology ,Animals ,Humans ,STAT1 ,Phosphorylation ,biology ,Animal ,Kinase ,Janus Kinase 1 ,Standard ,Protein Structure, Tertiary ,STAT1 Transcription Factor ,Cell culture ,Tyrosine kinase 2 ,biology.protein ,Interferons ,Signal transduction ,Signal Transduction - 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.
- Published
- 2014
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