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Antibody--hapten interactions in solution.

R A Dwek, R Jones, D Marsh

    Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
    |November 6, 1975
    PubMed
    Summary
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    Researchers mapped the myeloma protein MOPC 315’s antigen-binding site using spin labels and NMR. They determined the site’s dimensions, rigidity, and identified key histidine residues involved in hapten binding.

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Immunology

    Background:

    • Myeloma protein MOPC 315 is a well-characterized antibody.
    • Understanding antibody-antigen interactions is crucial in immunology.
    • The Fv fragment retains the antigen-binding site of the parent antibody.

    Purpose of the Study:

    • To determine the relative orientations of amino acid residues within the antigen-combining site of MOPC 315.
    • To characterize the structural and dynamic properties of the Fv fragment's binding site.
    • To identify residues critical for hapten binding and explore lanthanide interactions.

    Main Methods:

    • Enzymatic digestion to obtain the Fv fragment.
    • Electron spin resonance (E.S.R.) spectroscopy of spin-labeled haptens.

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  • Nuclear magnetic resonance (N.M.R.) spectroscopy, including difference spectroscopy.
  • Lanthanide binding studies using Gd III and fluorescence spectroscopy.

    • Main Results:

    • The Fv combining site is a rigid cleft (1.1 x 0.9 x 0.6 nm).
    • N.M.R. identified specific histidine residues (His 102H and His 97L) near the binding site.
    • Lanthanide binding site identified, influencing both lanthanide and hapten affinity.

    Conclusions:

    • The study provides detailed structural insights into the MOPC 315 antibody-combining site.
    • Key residues and structural features contributing to antigen recognition were elucidated.
    • The findings contribute to understanding antibody structure-function relationships and potential therapeutic targeting.