Impact of host cell line choice on glycan profile

被引：161

作者：

Goh, Justin Bryan ^{[1
]}

Ng, Say Kong ^{[1
]}

机构：

[1] ASTAR, Bioproc Technol Inst, Singapore, Singapore

来源：

CRITICAL REVIEWS IN BIOTECHNOLOGY | 2018年 / 38卷 / 06期

基金：

新加坡国家研究基金会;

关键词：

Glycosylation; expression system; immunoglobulin G (IgG); coagulation factor VII (FVII); erythropoietin (EPO); alpha-1 antitrypsin (A1AT); N-LINKED OLIGOSACCHARIDES; HAMSTER OVARY CELLS; GLCNAC-GLYCOPEPTIDE BETA-4-N-ACETYLGLUCOSAMINYLTRANSFERASE-III; RECOMBINANT THERAPEUTIC PROTEINS; ENGINEERED NICOTIANA-BENTHAMIANA; NONHUMAN SIALIC-ACID; FACTOR-VII RFVIIA; GLYCOLYLNEURAMINIC ACID; HUMAN IGG1; STRUCTURAL-CHARACTERIZATION;

D O I：

10.1080/07388551.2017.1416577

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

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.

引用

页码：851 / 867

页数：17

共 161 条

[1]

ADAMSON JW, 1990, ANNU REV MED, V41, P349

[2] Increased serum clearance of oligomannose species present on a human IgG1 molecule [J].