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Area of Science:

  • Immunology
  • Structural Biology
  • Microbiology

Background:

  • The NAIP/NLRC4 inflammasome is crucial for sensing Gram-negative bacterial components.
  • Previous studies indicated NAIP's role in activating NLRC4 upon ligand binding.
  • The precise mechanism of NAIP ligand recognition and activation remained unclear.

Purpose of the Study:

  • To elucidate the activation mechanism of NAIP upon ligand binding.
  • To investigate the dynamics of the ligand-binding region of inactive NAIP5.
  • To determine the structural basis of NAIP5-FliC interaction.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to solve the structure of NAIP5-FliC complex.
  • Analysis of protein-ligand interactions at atomic resolution.
  • Investigating the dynamics of the ligand-binding region.

Main Results:

  • Determined the cryo-EM structure of NAIP5 bound to FliC at 2.9-Å resolution.
  • Revealed a "trap and lock" mechanism for FliC recognition by NAIP5.
  • Identified specific interactions involving FliC domains (D0C, D0N) and NAIP5 regions (hydrophobic pocket, insertion domain, C-terminal tail).

Conclusions:

  • FliC binding to NAIP5 involves sequential trapping and locking events mediated by distinct FliC and NAIP5 domains.
  • This mechanism induces conformational changes in NAIP5, likely leading to NLRC4 inflammasome activation.
  • Provides a detailed structural understanding of NAIP-mediated bacterial sensing.