[Monoclonal antibodies and therapeutics].
More than 25 years after their discovery, monoclonal antibodies are now the most rapid expanding pharmaceutical viable drugs in clinical trials. The emergence of these antibodies was made possible by the development of genetic recombinant techniques. It is now possible to obtain engineered antibodies: chimearic or humanized or fully human monoclonal antibodies via the use of phage display technology or of transgenic mice. These antibodies are tolerable to the human immune system and eleven have been approved for therapeutic by the US Food and Drug Administration (FDA), the majority of them in the past four years. At least an additional 400 monoclonal antibodies are in clinical trials to treat cancer, transplant rejection or to combat autoimmune or infectious diseases. Important advances have been made in the design of highly specific fragment antibodies, fused or not with drugs or radioisotopes, and in the large industrial scale production with different expression systems (bacteria, yeasts, mammalian cells and transgenic plants and animals). In the next future new molecular promising strategies will enhance affinity, stability and expression levels and reduce the price of these engineering monoclonal to permit their use to treat a large number of diseases.
Desgranges
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Unité Inserm 03-34, institut de génétique moléculaire, hôpital Saint-Louis, 27, rue Juliette-Dodu, 75010 Paris, France. claude.desgranges@chu-stlouis.fr
D000911:Antibodies, Monoclonal / Q000627:therapeutic use*; D001327:Autoimmune Diseases / Q000188:drug therapy; D006084:Graft Rejection / Q000188:drug therapy; D006801:Humans; D009369:Neoplasms / Q000188:drug therapy; D011993:Recombinant Fusion Proteins / Q000627:therapeutic use; D014481:United States; D014486:United States Food and Drug Administration
D000911:Antibodies, Monoclonal; D011993:Recombinant Fusion Proteins