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Conformational changes in C1q upon binding to IgG oligomers.

R J Vandenberg, S B Easterbrook-Smith

    FEBS Letters
    |October 27, 1986
    PubMed
    Summary

    1-anilino-8-naphthalenesulfonate (ANS) binds C1q, inhibiting immune complex interactions. Oligomeric IgG binding to C1q-ANS induces conformational changes, evidenced by increased fluorescence, suggesting a role in immune complex formation.

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    Area of Science:

    • Immunology
    • Biochemistry
    • Structural Biology

    Background:

    • The complement system, particularly the C1 complex, plays a crucial role in innate and adaptive immunity.
    • C1q, the recognition protein of the C1 complex, initiates the classical complement pathway by binding to immune complexes.
    • Understanding the molecular interactions between C1q and immune complexes is vital for deciphering immune responses and developing immunotherapies.

    Purpose of the Study:

    • To investigate the binding characteristics of 1-anilino-8-naphthalenesulfonate (ANS) to C1q and its effect on C1q-immune complex interactions.
    • To determine if C1q undergoes conformational changes upon binding to different forms of immunoglobulin G (IgG).
    • To elucidate the role of ANS as a fluorescent probe for studying C1q-IgG interactions.

    Main Methods:

    • Utilized ANS as a fluorescent probe to monitor C1q binding and conformational changes.
    • Investigated the inhibitory effect of ANS on C1q-immune complex interactions across a concentration range.
    • Compared the binding affinity of ANS to C1q versus IgG.
    • Assessed the impact of monomeric and oligomeric IgG on the fluorescence of C1q-bound ANS.
    • Examined the effect of diethylpyrocarbonate pretreatment of C1q on its interaction with IgG oligomers.

    Main Results:

    • 1-anilino-8-naphthalenesulfonate (ANS) inhibited C1q-immune complex interactions at 2-4 mM concentrations.
    • ANS exhibited a 20-fold higher affinity for C1q than for IgG, enabling selective C1q labeling.
    • Binding of oligomeric IgG, but not monomeric IgG, to C1q-bound ANS resulted in a significant increase in fluorescence.
    • Diethylpyrocarbonate treatment of C1q abolished the fluorescence increase upon addition of IgG oligomers.

    Conclusions:

    • C1q undergoes significant conformational changes upon binding to oligomeric IgG.
    • ANS serves as a valuable fluorescent probe for detecting these C1q conformational alterations.
    • These findings provide insights into the molecular mechanisms of immune complex recognition and complement activation.

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