Premium
Functional mimicry: elicitation of a monoclonal antiidiotypic antibody hydrolizing β‐lactams
Author(s) -
Avalle Bérangére,
Thomas Daniel,
Friboulet Alain
Publication year - 1998
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.12.11.1055
Subject(s) - mimicry , monoclonal antibody , molecular mimicry , antibody , chemistry , antigen , microbiology and biotechnology , biology , immunology , ecology
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 β‐lactamase active site. Catalytic features of Ab2 were characterized with β‐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 β‐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 antiidiotypic antibody hydrolizing β‐lactams. FASEB J. 12, 1055–1060 (1998)