دورية أكاديمية
أعرض في EDS

Glycoengineering of Mammalian Expression Systems on a Cellular Level.

التفاصيل البيبلوغرافية
العنوان: Glycoengineering of Mammalian Expression Systems on a Cellular Level.
المؤلفون: Heffner KM; Department of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, MD, USA., Wang Q; Department of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, MD, USA., Hizal DB; Department of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, MD, USA., Can Ö; Department of Medical Engineering, Acibadem Mehmet Ali Aydinlar University, Istanbul, Turkey., Betenbaugh MJ; Department of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, MD, USA. beten@jhu.edu.
المصدر: Advances in biochemical engineering/biotechnology [Adv Biochem Eng Biotechnol] 2021; Vol. 175, pp. 37-69.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Springer Verlag Country of Publication: Germany NLM ID: 8307733 Publication Model: Print Cited Medium: Print ISSN: 0724-6145 (Print) Linking ISSN: 07246145 NLM ISO Abbreviation: Adv Biochem Eng Biotechnol Subsets: MEDLINE
أسماء مطبوعة: Publication: Heidelberg : Springer Verlag
Original Publication: Berlin ; New York : Springer-Verlag, [1983-
مواضيع طبية MeSH: Glycoproteins*/genetics , Glycoproteins*/metabolism, Animals ; CHO Cells ; Cricetinae ; Cricetulus ; Glycosylation ; Recombinant Proteins/genetics
مستخلص: Mammalian expression systems such as Chinese hamster ovary (CHO), mouse myeloma (NS0), and human embryonic kidney (HEK) cells serve a critical role in the biotechnology industry as the production host of choice for recombinant protein therapeutics. Most of the recombinant biologics are glycoproteins that contain complex oligosaccharide or glycan attachments representing a principal component of product quality. Both N-glycans and O-glycans are present in these mammalian cells, but the engineering of N-linked glycosylation is of critical interest in industry and many efforts have been directed to improve this pathway. This is because altering the N-glycan composition can change the product quality of recombinant biotherapeutics in mammalian hosts. In addition, sialylation and fucosylation represent components of the glycosylation pathway that affect circulatory half-life and antibody-dependent cellular cytotoxicity, respectively. In this chapter, we first offer an overview of the glycosylation, sialylation, and fucosylation networks in mammalian cells, specifically CHO cells, which are extensively used in antibody production. Next, genetic engineering technologies used in CHO cells to modulate glycosylation pathways are described. We provide examples of their use in CHO cell engineering approaches to highlight these technologies further. Specifically, we describe efforts to overexpress glycosyltransferases and sialyltransfereases, and efforts to decrease sialidase cleavage and fucosylation. Finally, this chapter covers new strategies and future directions of CHO cell glycoengineering, such as the application of glycoproteomics, glycomics, and the integration of 'omics' approaches to identify, quantify, and characterize the glycosylated proteins in CHO cells. Graphical Abstract.
(© 2018. Springer International Publishing AG.)
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فهرسة مساهمة: Keywords: CHO; CRISPR/Cas9; Chinese hamster ovary; Fucosylation; Glycoengineering; Glycomics; Glycoproteomics; Mammalian expression systems; N-linked glycosylation; O-linked glycosylation; Sialylation; TALEN; ZFN
المشرفين على المادة: 0 (Glycoproteins)
0 (Recombinant Proteins)
تواريخ الأحداث: Date Created: 20180314 Date Completed: 20210728 Latest Revision: 20210728
رمز التحديث: 20221213
DOI: 10.1007/10_2017_57
PMID: 29532110
قاعدة البيانات: MEDLINE
الوصف
تدمد:0724-6145
DOI:10.1007/10_2017_57