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Structural and dynamical aspects of membrane immunochemistry using model membranes.

P Brûlet, H M McConnell

    Biochemistry
    |March 22, 1977
    PubMed
    Summary

    Antibody and complement interactions with lipid haptens in liposomes are influenced by hapten structure, lipid composition, and cholesterol. Hapten accessibility and mobility significantly affect these immune responses.

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    Area of Science:

    • Immunology
    • Biochemistry
    • Membrane Biophysics

    Background:

    • Lipid haptens, functionalized with paramagnetic nitroxide (spin-label) groups, were synthesized with varying linker chain lengths and compositions.
    • These novel lipid haptens were incorporated into liposomes composed of cholesterol and dipalmitoylphosphatidylcholine (DPPC) at low molar concentrations (0.01-0.5 mol%).

    Purpose of the Study:

    • To investigate the binding of specific antinitroxide IgG (and Fab) antibodies to these liposomes.
    • To evaluate the subsequent fixation of complement mediated by antibody binding to the lipid haptens.
    • To elucidate the structure-activity relationships governing immune recognition of membrane-embedded haptens.

    Main Methods:

    • Synthesis of three distinct phospholipid haptens featuring a nitroxide spin-label.
    • Incorporation of lipid haptens into liposomes with varying cholesterol and DPPC ratios.
    • Quantification of specific IgG (and Fab) antibody binding to liposomes.
    • Measurement of complement fixation levels in response to antibody-hapten interactions.

    Main Results:

    • Antibody binding and complement fixation were strongly dependent on hapten structure and lipid composition for haptens with limited extension above the bilayer (10-20 Å), indicating steric hindrance effects.
    • Complement fixation by IgG antibodies against nitroxide lipid haptens was highly sensitive to hapten lateral mobility at concentrations ≤ 0.1 mol%, suggesting a requirement for hapten clustering or accessibility.
    • Cholesterol inclusion in liposomes enhanced hapten exposure, antibody binding, and complement fixation, likely through steric effects on bilayer structure and potentially by modulating membrane fluidity at low hapten concentrations.

    Conclusions:

    • The accessibility of lipid haptens to antibody binding sites is critically influenced by hapten structure and the surrounding lipid environment, particularly when steric factors limit exposure.
    • Lateral mobility of lipid haptens plays a crucial role in complement fixation, especially at low molar concentrations, highlighting the importance of membrane dynamics in immune recognition.
    • Cholesterol significantly modulates immune responses to lipid haptens by influencing bilayer structure, hapten presentation, and membrane fluidity, thereby impacting antibody binding and complement activation.

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