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Title: Tyrosine 110 in the measles virus phosphoprotein is required to block STAT1 phosphorylation

Abstract

The measles virus (MV) P gene encodes three proteins: P, an essential polymerase cofactor, and C and V, which have multiple functions including immune evasion. We show here that the MV P protein also contributes to immune evasion, and that tyrosine 110 is required to block nuclear translocation of the signal transducer and activator of transcription factors (STAT) after interferon type I treatment. In particular, MV P inhibits STAT1 phosphorylation. This is shown not only by transient expression but also by reverse genetic analyses based on a new functional infectious cDNA derived from a MV vaccine vial (Moraten strain). Our study also identifies a conserved sequence around P protein tyrosine 110 as a candidate interaction site with a cellular protein.

Authors:
 [1];  [1];  [1];  [1];  [2]
  1. Molecular Medicine Program and Virology and Gene Therapy Graduate Track, Mayo Clinic College of Medicine, Rochester, MN 55905 (United States)
  2. Molecular Medicine Program and Virology and Gene Therapy Graduate Track, Mayo Clinic College of Medicine, Rochester, MN 55905 (United States). E-mail: cattaneo.roberto@mayo.edu
Publication Date:
OSTI Identifier:
20977001
Resource Type:
Journal Article
Resource Relation:
Journal Name: Virology; Journal Volume: 360; Journal Issue: 1; Other Information: DOI: 10.1016/j.virol.2006.09.049; PII: S0042-6822(06)00712-4; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; GENES; IMMUNITY; INTERFERON; MEASLES VIRUS; PHOSPHOPROTEINS; PHOSPHORYLATION; POLYMERASES; TRANSCRIPTION FACTORS; TRANSLOCATION; TYROSINE; VACCINES

Citation Formats

Devaux, Patricia, Messling, Veronika von, Songsungthong, Warangkhana, Springfeld, Christoph, and Cattaneo, Roberto. Tyrosine 110 in the measles virus phosphoprotein is required to block STAT1 phosphorylation. United States: N. p., 2007. Web. doi:10.1016/j.virol.2006.09.049.
Devaux, Patricia, Messling, Veronika von, Songsungthong, Warangkhana, Springfeld, Christoph, & Cattaneo, Roberto. Tyrosine 110 in the measles virus phosphoprotein is required to block STAT1 phosphorylation. United States. doi:10.1016/j.virol.2006.09.049.
Devaux, Patricia, Messling, Veronika von, Songsungthong, Warangkhana, Springfeld, Christoph, and Cattaneo, Roberto. Fri . "Tyrosine 110 in the measles virus phosphoprotein is required to block STAT1 phosphorylation". United States. doi:10.1016/j.virol.2006.09.049.
@article{osti_20977001,
title = {Tyrosine 110 in the measles virus phosphoprotein is required to block STAT1 phosphorylation},
author = {Devaux, Patricia and Messling, Veronika von and Songsungthong, Warangkhana and Springfeld, Christoph and Cattaneo, Roberto},
abstractNote = {The measles virus (MV) P gene encodes three proteins: P, an essential polymerase cofactor, and C and V, which have multiple functions including immune evasion. We show here that the MV P protein also contributes to immune evasion, and that tyrosine 110 is required to block nuclear translocation of the signal transducer and activator of transcription factors (STAT) after interferon type I treatment. In particular, MV P inhibits STAT1 phosphorylation. This is shown not only by transient expression but also by reverse genetic analyses based on a new functional infectious cDNA derived from a MV vaccine vial (Moraten strain). Our study also identifies a conserved sequence around P protein tyrosine 110 as a candidate interaction site with a cellular protein.},
doi = {10.1016/j.virol.2006.09.049},
journal = {Virology},
number = 1,
volume = 360,
place = {United States},
year = {Fri Mar 30 00:00:00 EDT 2007},
month = {Fri Mar 30 00:00:00 EDT 2007}
}