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Single amino acid substitution altering antigen-binding specificity.

S Rudikoff, A M Giusti, W D Cook

    Proceedings of the National Academy of Sciences of the United States of America
    |March 1, 1982
    PubMed
    Summary
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    A single amino acid change in an antibody (S107 myeloma protein) prevents phosphocholine binding. This alteration in the heavy chain highlights how minor mutations can significantly impact antibody specificity.

    Area of Science:

    • Immunology
    • Structural Biology
    • Molecular Genetics

    Background:

    • Myeloma proteins are antibodies produced by cancerous plasma cells.
    • S107 is a known phosphocholine-binding myeloma protein.
    • Understanding antibody-antigen interactions is crucial for immunology.

    Purpose of the Study:

    • To characterize an antigen-binding variant of the S107 myeloma protein.
    • To identify the molecular basis for altered phosphocholine binding.
    • To investigate the role of specific amino acid substitutions in antibody function.

    Main Methods:

    • Cloning of S107 myeloma protein in soft agar.
    • Isolation and characterization of an antigen-binding variant.
    • Chain recombination experiments and amino acid sequence analysis.

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  • Structural analysis of the phosphocholine-binding site.

    • Main Results:

    • The variant protein lost phosphocholine-binding ability while retaining idiotype determinants.
    • The binding defect was localized to the heavy chain.
    • A single amino acid substitution (glutamic acid to alanine at position 35) in the heavy chain's first hypervariable region was identified.
    • This substitution disrupts a critical hydrogen bond in the binding site, explaining the loss of function.

    Conclusions:

    • A single amino acid substitution in the antibody's heavy chain can abolish antigen-binding specificity.
    • The glutamic acid at position 35 is critical for the structural integrity and function of the phosphocholine-binding site.
    • Somatic mutations, even minor ones, can significantly alter antibody binding properties.