Affiliations: Department of Microbiology and Molecular Genetics and The Molecular Biology Institute, University of California, Los Angeles, USA
Correspondence:
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Correspondence and reprint requests to: Manuel L. Penichet, MD, PhD, Department of Microbiology and Molecular Genetics, University of California, Los Angeles, CA 90095, USA.
Abstract: Advances in genetic engineering and expression systems have led to rapid progress in the development of immunoglobulins fused to other proteins. These ‘antibody fusion proteins’ have novel properties and include antibodies fused to the cytokine interleukin-2. In the present review we describe strategies for construction of these antibody-interleukin-2 fusion proteins and discuss their in vitro and in vivo properties. Antibody-interleukin-2 fusion proteins retain both antibody associated functions such as antigen binding, complement activation and Fc gamma receptor binding as well as interleukin-2 associated functions such as the stimulation of proliferation of CTLL2 cells. In vivo, they produce strong potentiation of the host immune response against any associated antigen. In addition these novel molecules are able to target tumor cells and produce a specific and effective T cell response capable of eliminating the tumor. These properties suggest that antibody-interleukin-2 fusion proteins will be useful in the diagnosis and/or treatment of human cancer as well as in the potentiation of human immune response against any associated antigen.
