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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Base Sequence
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Cell Nucleus / metabolism
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Chlorocebus aethiops
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HeLa Cells
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Humans
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Immunity, Innate
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Interferon Type I / pharmacology
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Measles / immunology
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Measles / virology*
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Measles virus / metabolism*
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Molecular Sequence Data
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Phosphoproteins / chemistry
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Phosphoproteins / genetics
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Phosphoproteins / metabolism*
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Phosphorylation / drug effects
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STAT1 Transcription Factor / metabolism*
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Sequence Alignment
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Signal Transduction
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Tyrosine / physiology*
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Vero Cells
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Viral Proteins / chemistry
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Viral Proteins / genetics
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Viral Proteins / metabolism*
Substances
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Interferon Type I
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P protein, Sendai virus
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Phosphoproteins
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STAT1 Transcription Factor
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V protein, measles virus
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Viral Proteins
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Tyrosine