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Article type: Research Article
Authors: Parren, Paul W. H. I.;
Affiliations: Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, and Laboratory for Clinical and Experimental Immunology, University of Amsterdam, Amsterdam, The Netherlands
Note: [] Address reprint requests to Paul Parren, Baxter, Biology Skill Center, 10555 West Flagler Street, Miami, FL 33174, USA.
Abstract: Production of human monoclonal antibodies (MAbs) of predefined specificity using conventional hybridoma technology has proved to be difficult. Immunotherapeutic intervention in humans with rodent MAbs, however, is disadvantageous because of the antigenicity of these proteins and may result in human antibody responses against this foreign agent. To circumvent this problem, recombinant DNA techniques have been developed to transplant the specificity of a rodent MAb into a human antibody. Two basic approaches are being employed: first, combining rodent MAb variable regions with human constant regions; and more recently, “reshaping” human MAbs by grafting complementarity-determining regions (CDR) into the human antibody framework. These humanized MAbs can now be used to study human Fc-dependent effector mechanisms in detail, which seems essential to optimize potential in vivo application.
Keywords: recombinant antibodies, immunotherapy, effector functions, humanization
DOI: 10.3233/HAB-1992-3304
Journal: Human Antibodies, vol. 3, no. 3, pp. 137-145, 1992
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