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This study integrates deep mutational scanning with inhibitors to reveal Enterovirus replication mechanisms. It clarifies viral protein functions and interactions, advancing our understanding of positive-sense RNA virus replication.

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Area of Science:

  • Virology
  • Molecular Biology
  • Structural Biology

Background:

  • Replication organelles are crucial for positive-sense RNA virus replication but their molecular mechanisms are poorly understood.
  • Deep mutational scanning (DMS) assesses mutation impacts but cannot specify functional effects.
  • Understanding these mechanisms is key to developing antiviral strategies.

Purpose of the Study:

  • To develop an integrated approach combining mutational scanning and inhibitor studies to dissect Enterovirus replication mechanisms.
  • To elucidate the functions of nonstructural viral proteins and their interactions with host factors.
  • To provide a refined model for positive-sense RNA virus replication.

Main Methods:

  • Integrated deep mutational scanning (DMS) with specific virus- and host-targeted inhibitors.
  • Utilized structural modeling to interpret mutational data.
  • Analyzed viral protein functional partitioning and host-pathogen interactions under different inhibitory conditions.

Main Results:

  • Clarified the modular architecture of the viral 2C protein, distinguishing its enzymatic and membrane-binding domains.
  • Demonstrated compensatory crosstalk between viral proteases (3C and 2A) upon 3C protease inhibition.
  • Showed that targeting host phospholipid synthesis alters mutational tolerance of the 3A protein, indicating variable host interaction preferences.

Conclusions:

  • The integrated DMS and inhibitor approach provides mechanistic insights into viral replication.
  • Revealed functional specialization within viral proteins and complex interplay between viral components and host factors.
  • This strategy refines structural predictions and enhances the model of positive-sense RNA virus replication.