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Membrane attack complex of complement. Evidence for its dimeric structure based on hybrid formation

E R Podack, H J Müller-Eberhard

    The Journal of Biological Chemistry
    |April 10, 1981
    PubMed
    Summary
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    New experiments show the membrane attack complex (MAC) of complement is a dimer. This finding, using differentially labeled C5b-6, clarifies MAC structure and function in cell lysis.

    Area of Science:

    • Immunology
    • Molecular Biology
    • Structural Biology

    Background:

    • The membrane attack complex (MAC) is a crucial component of the complement system, involved in cell lysis.
    • Understanding the quaternary structure of MAC is essential for elucidating its mechanism of action.

    Purpose of the Study:

    • To investigate the oligomeric state of the membrane attack complex (MAC) during its assembly.
    • To determine if the C5b-6 complex within the MAC exists as a monomer or dimer.

    Main Methods:

    • Preparation of differentially radiolabeled monomeric C5b-6 (biotin-125I-C5b-6 and 131I-C5b-6).
    • Assembly of MAC on phospholipid vesicles using labeled C5b-6 and purified C7, C8, and C9.
    • Purification of assembled MAC and binding to avidin-Sepharose for analysis of radiolabels.

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  • Electron microscopy of biotinated MAC hybrids and avidin-ferritin conjugates.

    • Main Results:

    • Co-purification of both 125I and 131I labels with the assembled MAC, confirming the presence of both C5b-6 forms.
    • Experimental data analysis strongly supported a dimeric structure for MAC, not a higher oligomer.
    • Fluid-phase soluble SC5b-9 was determined to be monomeric.
    • Electron microscopy showed biotinated MAC hybrids resemble complement-mediated membrane lesions, with avidin-ferritin binding to the ring structure.

    Conclusions:

    • The membrane attack complex (MAC) of complement adopts a dimeric structure, with C5b-6 forming an integral part of the ring structure.
    • This dimeric nature of MAC is critical for its function in forming membrane pores and mediating cell lysis.
    • The findings provide significant insight into the structural organization and assembly pathway of the complement MAC.