Monoclonal Antibodies against Human IgE

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Abstract
The specificity of five monoclonal anti-IgE antibodies (Mabs) was studied in direct latex agglutination and agglutination-inhibition experiments by particle-counting immunoassay. Twenty IgE myeloma proteins and several purified Dε0-, Dε1-, and Dε2-containing pepsin and papain fragments of IgE-DES(κ) were used in the evaluation. The results demonstrate two Mabs with isotypic specificity for two distinct epitopes of the Fcε-fragment within the Dε1- and Dε2-determinants. One Mab recognized only the immunizing IgE protein and was directed against determinants on the Fdε-fragment probably related to the idiotype. Anti-Em(1) allotypic Mabs recognized all 20 IgE myeloma proteins including two of Japanese origin and the Em(1)-allotype was confined to Dε2-determinants. Interestingly, one Mab (ALE) reacted with all 8 IgE myeloma proteins of the λ light-chain type but none out of 12 bearing κ chains. ALE seems therefore to recognize a new marker on IgE besides the known idiotypic, allotypic and isotypic ones. These results illustrate that a critical specificity control of Mabs is always warranted. Moreover, one should be aware of possible interference in IgE assays from the kind of determinants recognized by ALE whenever intact IgE myeloma proteins are used to raise polyclonal antisera, to get immunosorbent-purified anti-IgE antibodies or when used as tracers and standards.

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