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CryoEM reveals how the complement membrane attack complex ruptures lipid bilayers
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CryoEM reveals how the complement membrane attack complex ruptures lipid bilayers
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Journal Article
CryoEM reveals how the complement membrane attack complex ruptures lipid bilayers
2018
Overview
The membrane attack complex (MAC) is one of the immune system’s first responders. Complement proteins assemble on target membranes to form pores that lyse pathogens and impact tissue homeostasis of self-cells. How MAC disrupts the membrane barrier remains unclear. Here we use electron cryo-microscopy and flicker spectroscopy to show that MAC interacts with lipid bilayers in two distinct ways. Whereas C6 and C7 associate with the outer leaflet and reduce the energy for membrane bending, C8 and C9 traverse the bilayer increasing membrane rigidity. CryoEM reconstructions reveal plasticity of the MAC pore and demonstrate how C5b6 acts as a platform, directing assembly of a giant β-barrel whose structure is supported by a glycan scaffold. Our work provides a structural basis for understanding how β-pore forming proteins breach the membrane and reveals a mechanism for how MAC kills pathogens and regulates cell functions.
The complement membrane attack complex (MAC) is a lytic immune pore that kills pathogens. Here the authors use cryoEM to provide a structural and biophysical mechanism for how β-pore forming proteins breach the lipid bilayer, providing pathways to explore pore-formation in molecular detail.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 14/63
/ Complement C6 - ultrastructure
/ Complement C7 - ultrastructure
/ Complement C8 - ultrastructure
/ Complement C9 - ultrastructure
/ Complement Membrane Attack Complex - chemistry
/ Complement Membrane Attack Complex - metabolism
/ Complement Membrane Attack Complex - ultrastructure
/ Cryoelectron Microscopy - methods
/ Flicker
/ Glycan
/ Humanities and Social Sciences
/ Humans
/ Image Processing, Computer-Assisted
/ Lipids
/ Polysaccharides - metabolism
/ Protein Interaction Domains and Motifs
/ Proteins
/ Rigidity
/ Science
