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Complement fixation by model immune complexes free in solution and bound onto cell surfaces.

D M Segal, R L Guyer, P H Plotz

    Biochemistry
    |May 1, 1979
    PubMed
    Summary
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    This study investigated how Immunoglobin (IgG) oligomers of varying sizes trigger complement fixation. Larger IgG clusters showed increased efficiency in initiating the complement cascade, suggesting size matters for immune response.

    Area of Science:

    • Immunology
    • Biochemistry
    • Molecular Biology

    Background:

    • Immunoglobulin G (IgG) plays a crucial role in the immune system.
    • The complement system is a key component of innate immunity.
    • Understanding IgG's interaction with complement is vital for immune response research.

    Purpose of the Study:

    • To investigate the role of IgG oligomer size in complement fixation.
    • To determine the lytic efficiency of different IgG assemblages.
    • To elucidate the mechanism of complement activation by cell-bound IgG.

    Main Methods:

    • Covalent cross-linking of anti-2,4-dinitrophenyl IgG molecules into oligomers (monomer, dimer, trimer, heavy fractions).
    • Separation and characterization of IgG oligomers.

    Related Experiment Videos

  • Assay of complement fixation and complement-mediated lysis using radioiodinated oligomers attached to hapten-sensitized sheep red blood cells (N3ph-SRBC).

    • Main Results:

    • All IgG oligomers, including monomers, dimers, and trimers, could fix complement.
    • Lytic efficiency increased with the number of bound IgG molecules, complement concentration, hapten density, and oligomer size.
    • Larger IgG clusters demonstrated higher efficiency in initiating complement-mediated lysis.

    Conclusions:

    • The initiation of the complement cascade by IgG is dependent on the size of cell-bound IgG clusters.
    • Two adjacent IgG molecules are likely insufficient to trigger complement activation.
    • Increasing cluster size of IgG on cell surfaces enhances complement fixation and subsequent lysis.