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CryoEM reveals how the complement membrane attack complex ruptures lipid bilayers.

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The membrane attack complex (MAC) uses distinct mechanisms to disrupt cell membranes. It bends membranes initially and later increases rigidity, leading to pore formation for pathogen lysis and cell regulation.

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Area of Science:

  • Immunology
  • Structural Biology
  • Biophysics

Background:

  • The membrane attack complex (MAC) is a crucial component of the complement system, involved in innate immunity.
  • MAC forms pores in target cell membranes, leading to lysis and impacting tissue homeostasis.
  • The precise mechanism by which MAC disrupts lipid bilayers remains incompletely understood.

Purpose of the Study:

  • To elucidate the structural mechanisms by which the membrane attack complex (MAC) interacts with and disrupts lipid bilayers.
  • To provide a detailed structural understanding of MAC pore formation and its functional implications.

Main Methods:

  • Electron cryo-microscopy (CryoEM) was employed to determine high-resolution structures of MAC intermediates.
  • Flicker spectroscopy was utilized to probe the biophysical interactions of MAC components with lipid bilayers.
  • Structural reconstructions revealed the dynamic assembly and architecture of the MAC pore.

Main Results:

  • MAC exhibits dual modes of interaction with lipid bilayers: initial association with the outer leaflet (C6/C7) reducing bending energy, followed by bilayer traversal (C8/C9) increasing membrane rigidity.
  • CryoEM reconstructions unveiled the plasticity of the MAC pore and the role of C5b6 as a scaffold for β-barrel assembly.
  • A glycan scaffold was identified as supporting the structure of the assembled MAC pore.

Conclusions:

  • The study provides a structural framework for understanding how β-pore forming proteins, like MAC, breach membranes.
  • MAC employs a multi-step mechanism involving distinct protein-lipid interactions to achieve membrane disruption.
  • This research sheds light on the molecular mechanisms underlying MAC-mediated pathogen killing and regulation of cellular functions.