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The Measles Virus V Protein Binding Site to STAT2 Overlaps That of IRF9

Yuma Nagano, Aoi Sugiyama, Madoka Kimoto, Wakahara Takuya, Yasuyo Noguchi, Xinxin Jiang, Shinya Saijo, Nobutaka Shimizu, Nana Yabuno, Min Yao, Paul R. Gooley, Gregory W. Moseley, Takashi Tadokoro, Katsumi Maenaka, Toyoyuki Ose

2020Journal of Virology22 citationsDOIOpen Access PDF

Abstract

To evade host immunity, many pathogenic viruses inactivate host Janus kinase signal transducer and activator of transcription (STAT) signaling pathways using diverse strategies. Measles virus utilizes P and V proteins to counteract this signaling pathway. Data derived largely from cell-based assays have indicated several amino acid residues of P and V proteins as important. However, biophysical properties of V protein or its direct interaction with STAT molecules using purified proteins have not been studied. We have developed novel molecular tools enabling us to identify a novel molecular mechanism for immune evasion whereby V protein disrupts critical immune complexes, providing a clear strategy by which measles virus can suppress interferon-mediated antiviral gene expression.

Topics & Concepts

BiologyMeasles virusSTAT2STAT proteinSignal transductionVirusJanus kinaseInterferonCell biologyVirologySTAT3MeaslesVaccinationVirology and Viral Diseasesinterferon and immune responsesViral Infections and Vectors
The Measles Virus V Protein Binding Site to STAT2 Overlaps That of IRF9 | Litcius