Hendra virus V protein inhibits interferon signaling by preventing STAT1 and STAT2 nuclear accumulation.
The V protein of the recently emerged paramyxovirus, Nipah virus, has been shown to inhibit interferon (IFN) signal transduction through cytoplasmic sequestration of cellular STAT1 and STAT2 in high-molecular-weight complexes. Here we demonstrate that the closely related Hendra virus V protein also inhibits cellular responses to IFN through binding and cytoplasmic sequestration of both STAT1 and STAT2, but not STAT3. These findings demonstrate a V protein-mediated IFN signal evasion mechanism that is a general property of the known Henipavirus species.
Rodriguez
Jason J
JJ
Immunobiology Center, Mount Sinai School of Medicine, New York, New York 10029, USA.
Wang
Lin-Fa
LF
Horvath
Curt M
CM
D000595:Amino Acid Sequence; D002460:Cell Line; D002467:Cell Nucleus / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism*; D006801:Humans; D016898:Interferon-alpha / Q000378:metabolism*; D007371:Interferon-gamma / Q000378:metabolism*; D008969:Molecular Sequence Data; D050794:STAT1 Transcription Factor; D050795:STAT2 Transcription Factor; D015398:Signal Transduction / Q000187:drug effects*; D015534:Trans-Activators / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism / Q000494:pharmacology*
D004268:DNA-Binding Proteins; D016898:Interferon-alpha; D007371:Interferon-gamma; D050794:STAT1 Transcription Factor; D050795:STAT2 Transcription Factor; D015534:Trans-Activators; D014764:Viral Proteins; C494079:STAT1 protein, human; C494084:STAT2 protein, human; C110268:nonstructural protein C;nonstructural protein V;phosphoprotein P, Hendra virus