The measles virus phosphoprotein interacts with the linker domain of STAT1.

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

Virology

journal_title

Virology

authors

Devaux P,Priniski L,Cattaneo R

doi

10.1016/j.virol.2013.06.019

subject

Has Abstract

pub_date

2013-09-01 00:00:00

pages

250-6

issue

1-2

eissn

0042-6822

issn

1096-0341

pii

S0042-6822(13)00387-5

journal_volume

444

pub_type

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