Solution structure of the C-terminal domain of the measles virus V protein in its free form and mechanistic analysis of STAT2 targeting.

ABSTRACT: Viruses commonly evade the host antiviral interferon (IFN) response by targeting key components of the Janus kinase-signal transducer and activator of transcription (JAK-STAT) pathway, typically STAT1 and STAT2. Among the well-characterized viral IFN antagonists, measles virus (MeV), a member of the Morbillivirus genus, encodes a multifunctional V protein (MeV-V) that directly interacts with STAT proteins. The C-terminal domain (CTD) of MeV-V selectively binds to STAT2, disrupting the formation of the IFN-stimulated gene factor 3 (ISGF3) complex by inhibiting the STAT2-interferon regulatory factor 9 (IRF9) association. Here, we report a solution structure covering the MeV-V_CTD in its unbound form, as determined by nuclear magnetic resonance spectroscopy. While the overall

SUBMITTER: Morita K 

PROVIDER: S-EPMC12548473 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature