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

Patricia Devaux, Veronika von Messling, Warangkhana Songsungthong, Christoph Springfeld, Roberto Cattaneo

Research output: Contribution to journalArticlepeer-review

133 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)72-83
Number of pages12
Issue number1
StatePublished - Mar 30 2007


  • Innate immunity
  • Interferon signaling
  • Measles virus
  • Phosphoprotein

ASJC Scopus subject areas

  • Virology


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