Appropriate glycosylation of recombinant proteins for human use |
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Authors: | Susan A Brooks |
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Institution: | (1) School of Biological and Molecular Sciences, Oxford Brookes University, Gipsy Lane, OX3 0BP Headington, Oxford, UK |
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Abstract: | One of the commonest and least well understood posttranslational modifications of proteins is their glycosylation. Human glycoproteins
are glycosylated with a bewilderingly heterogeneous array of complex N- and O-linked glycans, which are the product of the coordinated activity of enzymes resident in the endoplasmic reticulum and Golgi
apparatus of the cell. Glycosylation of proteins is highly regulated and changes during differentiation, development, under
different physiological—and cell culture—conditions and in disease. The glycosylation of recombinant proteins, especially
those destined for potential administration to human subjects, is of critical importance. Glycosylation profoundly affects
biological activity, function, clearance from circulation, and crucially, antigenicity. The cells of nonhuman species do not
glycosylate their proteins in the same way as human cells do. In many cases, the differences are profound. Overall, the species
most distant to humans in evolutionary terms, such as bacteria, yeasts, fungi, insects and plants—the species used most commonly
in expression systems—have glycosylation repertoires least like our own. This review gives a brief overview of human N- and
O-linked protein glycosylation, summarizes what is known of the glycosylation potential of the cells of nonhuman species,
and presents the implications for the biotechnology industry. |
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Keywords: | Expression systems biotechnology glycosylation oligosaccharides posttranslational modification of proteins |
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