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A unique human IgE‐binding epitope on the Bermuda grass pollen recognized by mouse lambda‐type monoclonal antibodies
Author(s) -
CHANG Z. N.,
CHI C. W.,
SUN H. F.,
TSAI L. C.,
LEE D. T.,
HAN S. H.
Publication year - 1991
Publication title -
clinical and experimental allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 154
eISSN - 1365-2222
pISSN - 0954-7894
DOI - 10.1111/j.1365-2222.1991.tb01692.x
Subject(s) - epitope , monoclonal antibody , antibody , antigen , immunoglobulin e , biology , microbiology and biotechnology , glycoprotein , virology , immunology , chemistry
Summary A group of six mouse monoclonal antibodies (MoAbs) with the unusual lambda‐type light chain were generated by fusion of NS‐1 cells with splenic cells derived from BALB/c mice immunized with crude extracts of Bermuda grass pollen (BGP). Four of them were IgG1, one was IgG2b, and one was IgG3. Binding inhibition assay showed that they recognized the same (or very similar) epitope. Using sera from BGP‐allergic patients, it was found that the specific binding between the IgE antibodies and the MoAb 26–11‐fixed antigen could be blocked by MoAb 26–11 itself and another MoAb 9–13 in a dose‐dependent manner. It appears that the epitope recognized by the lambda‐type MoAbs is a human IgE‐binding antigenic determinant. Further physicochemical analyses showed that this epitope was stable under heat but sensitive to treatments of sodium periodate and proteinase K. Results from these studies indicate that this unique epitope which leads to the generation of lambda‐type MoAbs is part of a glycoprotein.