Production systems for recombinant antibodies
Autor: | Michael Hust, Thomas Schirrmann, Stefan Dübel, Laila Al-Halabi |
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Rok vydání: | 2008 |
Předmět: |
Glycosylation
Gram-negative bacteria Recombinant Fusion Proteins Gram-Positive Bacteria Protein Engineering Antibodies Cell Physiological Phenomena law.invention Animals Genetically Modified chemistry.chemical_compound law Gram-Negative Bacteria Animals Cloning Molecular biology Immunogenicity Fungi Protein engineering Plants Genetically Modified biology.organism_classification Fusion protein Recombinant Proteins Yeast chemistry Biochemistry Antibody Formation Recombinant DNA biology.protein Antibody Genetic Engineering |
Zdroj: | Frontiers in Bioscience. :4576 |
ISSN: | 1093-4715 1093-9946 |
DOI: | 10.2741/3024 |
Popis: | Recombinant antibodies are the fastest growing class of therapeutic proteins. Furthermore, antibodies are key detection reagents in research and diagnostics. The increasing demand for antibodies with regards to amount and quality resulted in the development of a variety of recombinant production systems employing gram-negative and gram-positive bacteria, yeast and filamentous fungi, insect cell lines as well as mammalian cell lines. More recently, antibodies were also successfully produced in transgenic plants and animals. Currently, the production of recombinant antibodies for therapy is performed in mammalian cell lines to reduce the risk of immunogenicity caused by non-human post-translational modifications, in particular glycosylation. However, novel strategies already allow human-like glycosylation patterns in yeast, insect cell lines and transgenic plants. Furthermore, therapeutic strategies not requiring glycosylation of the Fc portion have been conceived, most prominently using bispecific antibodies or scFv fusion proteins, which can be produced in bacteria. Here, we review all current antibody production systems considering their advantages and limitations with respect to intended applications. |
Databáze: | OpenAIRE |
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