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.
journal_name
Virologyjournal_title
Virologyauthors
Devaux P,Priniski L,Cattaneo Rdoi
10.1016/j.virol.2013.06.019subject
Has Abstractpub_date
2013-09-01 00:00:00pages
250-6issue
1-2eissn
0042-6822issn
1096-0341pii
S0042-6822(13)00387-5journal_volume
444pub_type
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