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Related Experiment Videos

A new complement function: solubilization of antigen-antibody aggregates.

G W Miller, V Nussenzweig

    Proceedings of the National Academy of Sciences of the United States of America
    |February 1, 1975
    PubMed
    Summary
    This summary is machine-generated.

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    Antigen-antibody aggregates dissolve in serum via complement activation, forming smaller immune complexes. This process, dependent on magnesium ions, involves complement component 3 and can be influenced by the properdin system.

    Area of Science:

    • Immunology
    • Biochemistry

    Background:

    • Antigen-antibody aggregates form immune complexes.
    • Solubilization of these complexes is crucial for immune response regulation.

    Purpose of the Study:

    • To investigate the mechanism of antigen-antibody aggregate solubilization by fresh serum.
    • To identify the key components and conditions required for immune complex dissolution.

    Main Methods:

    • Incubation of antigen-antibody aggregates with fresh serum at 37°C.
    • Analysis of resulting immune complexes for antigen, antibody, and complement (C3) determinants.
    • Testing the effect of divalent cations (Mg++, Ca++) and complement-deficient sera.

    Main Results:

    • Solubilization yields smaller immune complexes containing antigen, antibody, and C3.

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  • The process is complement-dependent, requiring Mg++ but not Ca++.
  • Solubilization is accelerated by Ca++ in certain sera, suggesting properdin system involvement.
  • Monovalent antibody fragments (Fab) can also induce solubilization.

    • Conclusions:

    • Complement-mediated solubilization of antigen-antibody aggregates is a complex process.
    • It involves complement activation, likely through both classical and alternative pathways.
    • Complement fragments may directly induce solubilization by binding to antibodies within the aggregate.