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2016 ; 7
(ä): 10587
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Structural basis of complement membrane attack complex formation
#MMPMID26841837
Serna M
; Giles JL
; Morgan BP
; Bubeck D
Nat Commun
2016[Feb]; 7
(ä): 10587
PMID26841837
show ga
In response to complement activation, the membrane attack complex (MAC) assembles
from fluid-phase proteins to form pores in lipid bilayers. MAC directly lyses
pathogens by a 'multi-hit' mechanism; however, sublytic MAC pores on host cells
activate signalling pathways. Previous studies have described the structures of
individual MAC components and subcomplexes; however, the molecular details of its
assembly and mechanism of action remain unresolved. Here we report the electron
cryo-microscopy structure of human MAC at subnanometre resolution. Structural
analyses define the stoichiometry of the complete pore and identify a network of
interaction interfaces that determine its assembly mechanism. MAC adopts a
'split-washer' configuration, in contrast to the predicted closed ring observed
for perforin and cholesterol-dependent cytolysins. Assembly precursors partially
penetrate the lipid bilayer, resulting in an irregular ?-barrel pore. Our results
demonstrate how differences in symmetric and asymmetric components of the MAC
underpin a molecular basis for pore formation and suggest a mechanism of action
that extends beyond membrane penetration.
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