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(The FASEB Journal. 1998;12:1055-1060.)
© 1998 FASEB

RESEARCH COMMUNICATION

Functional mimicry: elicitation of a monoclonal anti-idiotypic antibody hydrolizing ß-lactams

Bérangère Avallea, Daniel Thomasa, and Alain Fribouleta,1

a Laboratoire de Technologie Enzymatique-UPRES-A CNRS 6022, Université de Technologie de Compiègne-BP 20529, 60205 Compiègne Cedex, France

Antigen mimicry by anti-idiotypic antibodies is investigated as a reliable strategy to achieve molecular imprinting of an enzymatic activity. A monoclonal anti-idiotypic antibody (Ab2-9G4H9) was elicited by using a monoclonal antibody (Ab1-7AF9) specific for the ß-lactamase active site. Catalytic features of Ab2 were characterized with ß-lactamase substrates. The antibody combining site appeared to have retained a part of the catalytic specificity. The relevance of the idiotypic mimicry concept for the generation of catalytic antibodies was further demonstrated by eliciting a third generation antibody (Ab3), which was shown to recognize ß-lactamase: the complete internal image properties of Ab2 9G4H9, including binding and catalytic properties, were thus checked.—Avalle, B., Thomas, D., Friboulet, A. Functional mimicry: elicitation of a monoclonal anti-idiotypic antibody hydrolizing ß-lactams. FASEB J. 12, 1055–1060 (1998)


Key Words: mimicry • catalytic antibody • abzyme • anti-idiotype • ß-lactamase




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