title: Glycosylation of antibody therapeutics: optimisation for purpose.
abstract: Recombinant antibody therapeutics represent a significant success story in terms of clinical benefit delivered and revenue (profit) generated within the biopharmaceutical industry. Additionally, it is estimated that 30% of new drugs likely to be licensed during the next decade will be based on antibody products. High volume production with the maintenance of structural and functional fidelity of these large biological molecules results in high "cost of goods" that can limit their availability to patients, due to the strain it puts on national and private health budgets. The challenge in reducing cost of goods is that each antibody is unique, both in structure and function. Optimal clinical efficacy will require engineering of antibody genes to deliver products with enhanced activities produced by cell lines engineered to deliver antibody homogeneous for pre-selected post-translational modifications, that is, protein structures and glycoforms. A "universal" production vehicle cannot meet these demands and several production mammalian cells are now available, alternatives to mammalian cell lines are also reaching maturity. Advances in downstream processing also need to be realised whilst chemical changes during processing and storage must be minimised.
authors.affiliation: Immunity & Infection, University of Birmingham, UK.
authors.forename: Roy
authors.initials: R
authors.lastname: Jefferis
mesh_terms: D000906:Antibodies / Q000737:chemistry / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D000906:Antibodies; D011994:Recombinant Proteins