Abstract
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.
MeSH Terms
Amino Acid Sequence
Cell Line
Cell Nucleus/metabolism
DNA-Binding Proteins/metabolism
Humans
Interferon-alpha/metabolism
Interferon-gamma/metabolism
Molecular Sequence Data
STAT1 Transcription Factor
STAT2 Transcription Factor
Signal Transduction/drug effects
Trans-Activators/metabolism
Viral Proteins/metabolism,pharmacology
Chemicals
DNA-Binding Proteins
Interferon-alpha
STAT1 Transcription Factor
STAT1 protein, human
STAT2 Transcription Factor
STAT2 protein, human
Trans-Activators
V protein, Hendra virus
Viral Proteins
Interferon-gamma
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Rodriguez Jason J
Immunobiology Center, Mount Sinai School of Medicine, New York, New York 10029, USA.
Wang Lin-Fa
Horvath Curt M
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