[HTML][HTML] Tyrosine 110 in the measles virus phosphoprotein is required to block STAT1 phosphorylation
P Devaux, V von Messling, W Songsungthong… - Virology, 2007 - Elsevier
Virology, 2007•Elsevier
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 …
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 …
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.
Elsevier