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Membrane attack complex of complement: a structural analysis of its assembly

E R Podack, A F Esser, G Biesecker

    The Journal of Experimental Medicine
    |February 1, 1980
    PubMed
    Summary
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    This study reveals the structural assembly of the membrane attack complex (MAC) in complement. Key findings show protein micelle formation and dissociation facilitate MAC dimerization and membrane damage.

    Area of Science:

    • Immunology
    • Structural Biology
    • Biochemistry

    Background:

    • The complement system is crucial for innate immunity.
    • The membrane attack complex (MAC) forms pores in target cell membranes.
    • Understanding MAC assembly is key to its function and potential therapeutic targeting.

    Purpose of the Study:

    • To elucidate the structural mechanisms of membrane attack complex (MAC) assembly.
    • To characterize intermediate complexes during MAC formation.
    • To investigate the role of protein micelle formation in MAC assembly.

    Main Methods:

    • Electron microscopy was used to visualize complex structures.
    • Sucrose density-gradient ultracentrifugation determined sedimentation rates and complex composition.

    Related Experiment Videos

  • Lipid vesicles (dioleoyl lecithin) were used to study membrane-bound complexes.
  • Deoxycholate (DOC) extraction was employed to isolate protein components.

    • Main Results:

    • C5b-6 complex exhibits an elongated shape (160 x 60 x 60 Å) and forms paracrystals.
    • C5b-7 forms soluble tetrameric protein micelles with a 36S sedimentation rate.
    • C5b-8 dissociates micelles, appearing as a half-ring attached to vesicles (18S).
    • C5b-9 dimerization, mediated by C9, is essential for MAC formation (33S dimer, 23S monomer).
    • High MAC concentrations cause membrane bilayer defects due to lipid binding.

    Conclusions:

    • Protein micelle formation at the C5b-7 stage and its dissociation by C8 facilitate C5b-9 dimerization.
    • Dimerization of C5b-9 by C9 is a critical step in MAC assembly.
    • The MAC's lipid-binding capacity directly contributes to membrane destruction.