Devaux Patricia, von Messling Veronika, Songsungthong Warangkhana, Springfeld Christoph, Cattaneo Roberto
Molecular Medicine Program and Virology and Gene Therapy Graduate Track, Mayo Clinic College of Medicine, Rochester, MN 55905, USA.
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.
麻疹病毒（MV）的P基因编码三种蛋白质：P，一种必需的聚合酶辅助因子，以及C和V，它们具有多种功能，包括免疫逃避。我们在此表明，MV的P蛋白也有助于免疫逃避，并且110位酪氨酸是I型干扰素处理后阻断信号转导和转录激活因子（STAT）核转位所必需的。特别是，MV P抑制STAT1磷酸化。这不仅通过瞬时表达得以证明，还通过基于源自MV疫苗瓶（莫拉坦株）的新功能性感染性cDNA的反向遗传分析得以证实。我们的研究还确定了P蛋白110位酪氨酸周围的保守序列作为与一种细胞蛋白的候选相互作用位点。
