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Advances in the Expression of Humanized Glycoprotein in Yeast |
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Abstract Compared with complex glycoproteins in humans, therapeutic proteins produced in yeast expression systems typically carry high-mannose sugar chains which can lead to rapid clearance, enhanced immunogenicity and poor pharmacokinetic behaviour in clinical application. After the recreation of the N-glycosylation pathways by eliminating endogenous glycosylation reactions, introducing mammalian glycosyltransferases and expressing some sugar transporters, human-like complex glycoproteins with terminal sialic acids could be produced. This review summarizes yeast N-linked glycosylation processes, the heterogeneity of glycosylation, the genetic engineering of yeast glycosylation pathways to produce fully humanized glycoproteins and the application of endo-β-N-acetylglucosaminidase for in vitro synthesis of complex glycoproteins in recent years. Moreover, existing problems and future development directions are discussed.
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Received: 20 December 2006
Published: 25 April 2007
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