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Related Experiment Videos

Antigenic structure of histone H2B.

S Muller, M Couppez, J P Briand

    Biochimica Et Biophysica Acta
    |March 1, 1985
    PubMed
    Summary

    Researchers mapped histone H2B antigenic determinants using overlapping fragments. Seven key regions were identified, with some unique to antibodies from autoimmune mice, revealing insights into histone H2B antigenicity.

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    Area of Science:

    • Immunology
    • Molecular Biology
    • Biochemistry

    Background:

    • Histone H2B is a core component of nucleosomes.
    • Understanding histone H2B antigenicity is crucial for immunological studies.

    Purpose of the Study:

    • To precisely localize antigenic determinants on the histone H2B molecule.
    • To investigate the role of different antibody sources in epitope mapping.

    Main Methods:

    • Utilized 23 overlapping histone H2B fragments generated by chemical/enzymatic cleavage and solid-phase peptide synthesis.
    • Employed enzyme-linked immunosorbent assay (ELISA) to measure peptide-antibody binding.
    • Tested antisera against calf thymus and chicken erythrocyte H2B, plus monoclonal antibodies from autoimmune mice.

    Main Results:

    • Identified seven distinct antigenic determinants on histone H2B (residues 1-11, 6-18, 15-25, 26-35, 50-65, 94-113, 114-125).
    • Discovered two determinants (residues 6-18 and 26-35) were specifically recognized by antibodies from autoimmune mice.
    • Confirmed antigenicity at both the N- and C-termini of H2B.
    • Observed a correlation between hydrophilicity and antigenicity for four epitopes.

    Conclusions:

    • The study successfully mapped key antigenic sites on histone H2B.
    • Antibodies from autoimmune sources revealed unique epitopes, expanding the understanding of H2B antigenicity.
    • Histone H2B N- and C-termini are immunologically active regions.

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