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Disulfide bonds-driven assembly and structural complexity of PTX3: High-resolution structures insights into

Hanhan Guo1, Mengzhuo Hou2, Daping Wang1

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International Journal of Biological Macromolecules
|December 29, 2024
PubMed
Summary

Pentraxin-3 (PTX3) oligomerization, essential for immune defense, is driven by disulfide bonds. Cryo-EM revealed how PTX3 monomers assemble into higher-order structures, crucial for complement activation.

Keywords:
Cryo-EMDisulfide bondsOligomerizationPTX3

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Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • Pentraxin-3 (PTX3) is a key pattern-recognition molecule involved in innate immunity.
  • PTX3 plays critical roles in pathogen recognition and complement system activation.
  • The structural mechanisms governing PTX3 oligomerization and function remain largely unknown.

Purpose of the Study:

  • To elucidate the structural basis of Pentraxin-3 (PTX3) oligomerization.
  • To understand how PTX3 assembly influences its immune functions, particularly complement activation.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was utilized to determine PTX3 structures.
  • High-resolution structures of PTX3 octamers and tetramers were resolved.
  • Medium-resolution structures of PTX3 dimers and hexamers were also obtained.

Main Results:

  • PTX3 oligomerization is driven by dimeric units stabilized by C-terminal disulfide bonds.
  • N-terminal disulfide bonds further facilitate the assembly into larger PTX3 oligomers.
  • A hierarchical assembly process was identified, crucial for classical complement pathway activation.

Conclusions:

  • The study reveals the detailed structural mechanisms of PTX3 oligomerization.
  • Hierarchical assembly of PTX3 is essential for its role in the complement system.
  • These findings provide a foundation for developing PTX3-targeted therapeutics.