[Therapeutic antibodies and related products: choosing the right structure for success]

Alain Beck1, Elsa Wagner-Rousset, Thierry Wurch

  • 1Centre d'immunologie Pierre Fabre (www.cipf.com), 5, avenue Napoléon III, 74160 Saint-Julien-en-Genevois, France. alain.beck@pierre-fabre.com

Medecine Sciences : M/S
|December 29, 2009
PubMed

Monoclonal antibodies (mAb) and related-products represent the fastest growing class of therapeutics in the biotechnological and pharmaceutical industry. In just as short as 20 years, more than 30 immunoglobulins (IgG) and derivatives have been approved in a wide range of indications (oncology, inflammation and auto-immunity, transplantation, angioplasty, hematology, ophthalmology, viral infections, allergy). The mAb structure toolbox contains mouse, chimeric, humanized and human antibodies from different isotypes (IgG1, 2 and 4), as well as IgG-related products (immunoconjugates, radio-immunoconjugates, Fab fragments, Fc-fusion proteins and peptides, bispecifics). Furthermore from a structural point of view, mAb glycosylation is linked to their production systems and may impact on their effector functions and immunogenicity. Based on the current knowledge, choosing the right antibody format, isotype and glycosylation profile are some of the key issues to address early during the lead selection.

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