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      Impact of host cell line choice on glycan profile

      1 , 1
      Critical Reviews in Biotechnology
      Informa UK Limited

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          Abstract

          Protein glycosylation is post-translational modification (PTM) which is important for pharmacokinetics and immunogenicity of recombinant glycoprotein therapeutics. As a result of variations in monosaccharide composition, glycosidic linkages and glycan branching, glycosylation introduces considerable complexity and heterogeneity to therapeutics. The host cell line used to produce the glycoprotein has a strong influence on the glycosylation because different host systems may express varying repertoire of glycosylation enzymes and transporters that contributes to specificity and heterogeneity in glycosylation profiles. In this review, we discuss the types of host cell lines currently used for recombinant therapeutic production, their glycosylation potential and the resultant impact on glycoprotein properties. In addition, we compare the reported glycosylation profiles of four recombinant glycoproteins: immunoglobulin G (IgG), coagulation factor VII (FVII), erythropoietin (EPO) and alpha-1 antitrypsin (A1AT) produced in different mammalian cells to establish the influence of mammalian host cell lines on glycosylation.

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          Most cited references108

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          Characteristics of a Human Cell Line Transformed by DNA from Human Adenovirus Type 5

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            Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins.

            Ajit Varki (2007)
            All cells in nature are covered by a dense and complex array of carbohydrates. Given their prominence on cell surfaces, it is not surprising that these glycans mediate and/or modulate many cellular interactions. Proteins that bind sialic acid, a sugar that is found on the surface of the cell and on secreted proteins in vertebrates, are involved in a broad range of biological processes, including intercellular adhesion, signalling and microbial attachment. Studying the roles of such proteins in vertebrates has improved our understanding of normal physiology, disease and human evolution.
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              CHO cells in biotechnology for production of recombinant proteins: current state and further potential.

              Recombinant Chinese hamster ovary cells (rCHO) cells have been the most commonly used mammalian host for large-scale commercial production of therapeutic proteins. Recent advances in cell culture technology for rCHO cells have achieved significant improvement in protein production leading to titer of more than 10 g/L to meet the huge demand from market needs. This achievement is associated with progression in the establishment of high and stable producer and the optimization of culture process including media development. In this review article, we focus on current strategies and achievements in cell line development, mainly in vector engineering and cell engineering, for high and stable protein production in rCHO cells. The approaches that manipulate various DNA elements for gene targeting by site-specific integration and cis-acting elements to augment and stabilize gene expression are reviewed here. The genetic modulation strategy by "direct" cell engineering with growth-promoting and/or productivity-enhancing factors and omics-based approaches involved in transcriptomics, proteomics, and metabolomics to pursue cell engineering are also presented.
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                Author and article information

                Journal
                Critical Reviews in Biotechnology
                Critical Reviews in Biotechnology
                Informa UK Limited
                0738-8551
                1549-7801
                December 27 2017
                August 18 2018
                December 20 2017
                August 18 2018
                : 38
                : 6
                : 851-867
                Affiliations
                [1 ] Bioprocessing Technology Institute, Agency for Science, Technology and Research (A*STAR), Singapore, Singapore
                Article
                10.1080/07388551.2017.1416577
                29262720
                1f49bbc0-317f-4a98-9587-a1643fb740a6
                © 2018
                History

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