Abstract
The measles virus (MV) phosphoprotein (P) and V proteins block the interferon (IFN) response by impeding phosphorylation of the signal transducer and activator of transcription 1 (STAT1) by the Janus kinase 1 (JAK1). We characterized how STAT1 mutants interact with P and JAK1 phosphorylation. Certain mutants of the linker, the Src-homology 2 domain (SH2), or the transactivation domain had reduced or abolished phosphorylation through JAK1 after IFN treatment. Other mutants, mainly localized in the linker, failed to interact with P as documented by the lack of interference with nuclear translocation. Thus the functional footprint of P on STAT1 localizes mainly to the linker domain; there is also some overlap with the STAT1 phosphorylation functional footprint on the SH2 domain. Based on these observations, we discuss how the MV-P might operate to inhibit the JAK/STAT pathway.
Original language | English (US) |
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Pages (from-to) | 250-256 |
Number of pages | 7 |
Journal | Virology |
Volume | 444 |
Issue number | 1-2 |
DOIs | |
State | Published - Sep 2013 |
Keywords
- Innate immunity
- Interferon signaling
- Measles virus
- Phosphoprotein
- STAT1
ASJC Scopus subject areas
- Virology