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Structural basis for STAT2 suppression by flavivirus NS5.

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Viruses like Zika and dengue suppress human STAT2 using their NS5 protein. Structural studies reveal how NS5 blocks STAT2, inhibiting antiviral responses and aiding infection.

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Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • Viruses suppress host cellular signal transducers of transcription 2 (STAT2) to establish infections.
  • The precise mechanism of viral antagonism of STAT2 is not fully understood due to limited structural data.

Purpose of the Study:

  • To elucidate the structural basis of STAT2 suppression by Zika virus (ZIKV) and dengue virus (DENV) non-structural protein 5 (NS5).
  • To investigate the functional implications of the NS5-STAT2 interaction in viral pathogenesis.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) and crystal structure determination of human STAT2 (hSTAT2) in complex with ZIKV NS5 and DENV NS5.
  • Biochemical assays to assess the impact of disrupting NS5-hSTAT2 interactions on viral functions.

Main Results:

  • The structures revealed a two-pronged interaction between NS5 and hSTAT2.
  • NS5's methyltransferase and RNA-dependent RNA polymerase (RdRP) domains create a cleft that binds hSTAT2's coiled-coil domain, blocking its association with interferon regulatory factor 9.
  • The NS5 RdRP domain also binds hSTAT2's amino-terminal domain.
  • Disrupting these interactions reduced NS5-mediated hSTAT2 degradation, interferon suppression, and viral replication.

Conclusions:

  • The study clarifies the mechanism by which ZIKV and DENV NS5 proteins antagonize hSTAT2.
  • This antagonism involves direct binding and disruption of STAT2 function, contributing to viral immune evasion and infection.