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Related Experiment Videos

Functional antibody lacking a variable-region disulfide bridge.

S Rudikoff, J G Pumphrey

    Proceedings of the National Academy of Sciences of the United States of America
    |October 1, 1986
    PubMed
    Summary
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    Antibodies can function without a disulfide bridge in the heavy chain variable region. This study found that tyrosine can replace the usual half-cystine, allowing antigen binding and precipitation.

    Area of Science:

    • Immunology
    • Molecular Biology
    • Protein Chemistry

    Background:

    • Antibody structure typically includes invariant disulfide bridges in the variable region, considered essential for proper folding and function.
    • Previous research reported a partial cDNA sequence of ABPC48 plasmacytoma heavy chain with a tyrosine substitution for a half-cystine.

    Purpose of the Study:

    • To investigate the structural and functional implications of a tyrosine substitution for a half-cystine in the antibody heavy chain variable region.
    • To determine if the disulfide bridge is obligatory for antibody function.

    Main Methods:

    • Analysis of the heavy chain protein produced by ABPC48 plasmacytoma.
    • Functional assays to assess antigen binding and precipitation capabilities.

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    Main Results:

    • ABPC48 heavy chains quantitatively express tyrosine instead of the second half-cystine in the variable region.
    • The antibody population from ABPC48 demonstrates antigen binding and precipitation capabilities.

    Conclusions:

    • The presence of a disulfide bridge in the antibody heavy chain variable region is not necessary for the proper function of this specific antibody.
    • Disulfide bridges may not be obligatory for antibody function in general, challenging previous assumptions.