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Related Experiment Videos

Staphylococcal protein A and human IgG subclasses and allotypes

E Van Loghem, B Frangione, B Recht

    Scandinavian Journal of Immunology
    |March 1, 1982
    PubMed
    Summary

    Staphylococcal protein A binds most immunoglobulin G (IgG) subclasses, but not typically IgG3. Specific amino acid differences in the CH2 and CH3 domains determine IgG3 binding to protein A.

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    Area of Science:

    • Immunology
    • Protein Biochemistry
    • Molecular Biology

    Background:

    • Staphylococcal protein A is a cell-wall associated protein with known affinity for immunoglobulin G (IgG).
    • Protein A's binding properties are subclass-specific, with variations observed across different IgG subclasses.
    • Understanding these interactions is crucial for applications in diagnostics and therapeutics.

    Purpose of the Study:

    • To elucidate the molecular basis for the differential binding of Staphylococcal protein A to various IgG subclasses, particularly IgG3.
    • To identify specific structural determinants within IgG molecules that mediate or prevent protein A interaction.

    Main Methods:

    • Comparative analysis of IgG subclass sequences.
    • Focus on amino acid variations in the CH2 and CH3 domains of IgG proteins.

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  • Correlation of specific amino acid residues with observed protein A binding phenotypes.

    • Main Results:

    • Staphylococcal protein A binds IgG1, IgG2, and IgG4 subclasses.
    • Most IgG3 proteins do not bind protein A, with exceptions for specific alleles (G3m(u-): G3m(b0,b3,b5,s,v)).
    • Amino acid differences at position 339 (Ala vs. Thr) in the CH2 domain distinguish G3m(u-) and G3m(u+) IgG3 proteins.
    • Histidine at position 435 in the CH3 domain is associated with protein A binding, while Arginine is associated with non-binding.

    Conclusions:

    • Specific amino acid residues in the CH2 and CH3 domains of IgG molecules dictate Staphylococcal protein A binding.
    • The presence of Histidine at position 435 in the CH3 domain is a key determinant for protein A interaction across IgG subclasses.
    • Understanding these structural correlates enables prediction and manipulation of protein A-IgG interactions.