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

Virology. 2007 Mar 30;360(1):72-83. doi: 10.1016/j.virol.2006.09.049. Epub 2006 Nov 16.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • Cell Nucleus / metabolism
  • Chlorocebus aethiops
  • HeLa Cells
  • Humans
  • Immunity, Innate
  • Interferon Type I / pharmacology
  • Measles / immunology
  • Measles / virology*
  • Measles virus / metabolism*
  • Molecular Sequence Data
  • Phosphoproteins / chemistry
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Phosphorylation / drug effects
  • STAT1 Transcription Factor / metabolism*
  • Sequence Alignment
  • Signal Transduction
  • Tyrosine / physiology*
  • Vero Cells
  • Viral Proteins / chemistry
  • Viral Proteins / genetics
  • Viral Proteins / metabolism*


  • Interferon Type I
  • P protein, Sendai virus
  • Phosphoproteins
  • STAT1 Transcription Factor
  • V protein, measles virus
  • Viral Proteins
  • Tyrosine