Antibody engineering and perspectives in therapy

Abstract

Techniques of genetic engineering, homologous recombination, and gene transfection make it feasible to produce antigen-binding molecules with widely varying structures. Novel proteins which possess the binding specificity of antibody associated with sequences such as an enzyme or toxin have potential use in immunoassays, in imaging, in immunotherapy. Antibody fusion proteins can also be used as a means to purify proteins or to study the function of surface protooncogenes. This paper reviews the recent data on the obtention and utilisation of the genetically engineered antibody molecules, as well as the approach which consists on the expression in vitro, in Escherichia coli, of a practically unlimited repertoire of Fab fragments and antibody sites.