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Studies on anti-H reagents.

G L Daniels

    Revue Francaise De Transfusion Et Immuno-Hematologie
    |October 1, 1984
    PubMed
    Summary
    This summary is machine-generated.

    This study analyzed anti-H reagents, finding that most bind preferentially to Type 2 H trisaccharide. Specific reagents showed distinct binding and inhibition patterns, offering insights into H antigen variations.

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    Area of Science:

    • Immunology
    • Biochemistry
    • Glycobiology

    Background:

    • The human ABO blood group system is determined by fucosylated carbohydrate antigens, with H antigen being a precursor to A and B antigens.
    • Variations in H antigen expression, such as in Bombay (Oh) and para-Bombay (Ohm) phenotypes, present unique serological challenges.
    • Understanding the specificity of anti-H reagents is crucial for accurate blood group phenotyping and transfusion safety.

    Purpose of the Study:

    • To characterize the binding and inhibition specificities of various anti-H reagents, including monoclonal antibodies, human sera, and lectins.
    • To compare the reactivity of these reagents with the Type 2 H trisaccharide and other related oligosaccharides.
    • To investigate the behavior of anti-H reagents with red blood cells from individuals with different H antigen expression profiles, including Bombay phenotypes.

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    Main Methods:

    • Adsorption tests using Synsorb immunoadsorbents to assess binding to Type 2 H trisaccharide.
    • Inhibition tests with various oligosaccharides (e.g., 2'-fucosyllactose, lacto-difucotetraose) and body fluids (saliva, ovarian cyst fluid, milk).
    • Titration tests with red blood cells from cord and adult samples, including those from individuals with Bombay phenotypes.

    Main Results:

    • All analyzed anti-H reagents preferentially bound to the Type 2 H trisaccharide.
    • Monoclonal anti-Type 2 H (H11) and serum from a rare A1 (Toml.) individual exclusively bound to Type 2 H.
    • Bombay (Oh) sera were inhibited by saliva and H glycoprotein but not by certain other fucosylated oligosaccharides. H11 and Toml. serum showed distinct inhibition profiles compared to other reagents.
    • Lectins from Ulex europaeus, Lotus tetragonolobus, and eel serum were specifically inhibited by alpha-L-fucose.
    • Reactions of H11 and Toml. serum with cord vs. adult red cells differed from those of anti-HI sera and lectins, suggesting distinct binding mechanisms or epitope recognition.

    Conclusions:

    • The study delineates the specificities of diverse anti-H reagents, highlighting the exclusive binding of monoclonal anti-Type 2 H (H11) and Toml. serum to the Type 2 H trisaccharide.
    • Differential inhibition patterns reveal distinct molecular interactions and epitope recognition among anti-H antibodies and lectins.
    • The distinct behavior of H11 and Toml. serum compared to lectins and anti-HI sera in titration tests suggests unique characteristics relevant to H antigen phenotyping, particularly in rare blood groups.