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Journal ArticleDOI

Engineered CHO cells for production of diverse, homogeneous glycoproteins.

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TLDR
An engineering approach will aid the production of glycoproteins with improved properties and therapeutic potential by constructing a design matrix that facilitates the generation of desired glycosylation, such as human-like α2,6-linked sialic acid capping.
Abstract
Production of glycoprotein therapeutics in Chinese hamster ovary (CHO) cells is limited by the cells' generic capacity for N-glycosylation, and production of glycoproteins with desirable homogeneous glycoforms remains a challenge. We conducted a comprehensive knockout screen of glycosyltransferase genes controlling N-glycosylation in CHO cells and constructed a design matrix that facilitates the generation of desired glycosylation, such as human-like α2,6-linked sialic acid capping. This engineering approach will aid the production of glycoproteins with improved properties and therapeutic potential.

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Journal ArticleDOI

Global view of human protein glycosylation pathways and functions

TL;DR: This work predicts that use of (single-cell) transcriptomics, genetic screens, genetic engineering of cellular glycosylation capacities and custom design of glycoprotein therapeutics are advancements that will ignite wider integration of gly cosylation in general cell biology.
Journal ArticleDOI

The art of CHO cell engineering: A comprehensive retrospect and future perspectives

TL;DR: This review provides a comprehensive summary of the most fundamental achievements in CHO cell engineering over the past three decades and discusses the potential of novel and innovative methodologies that might contribute to further enhancement of existing CHO based production platforms for biopharmaceutical manufacturing in the future.
Journal ArticleDOI

Therapeutic glycoprotein production in mammalian cells

TL;DR: The advance of "omics" technologies has recently given rise to new possibilities in improving these expression platforms and will significantly help developing new strategies, in particular for CHO (Chinese Hamster Ovary) cells.
Journal ArticleDOI

Global aspects of viral glycosylation.

TL;DR: It is underscored that glycans often pay important contributions to overall protein structure, function and immune recognition, and that glycANS represent a crucial determinant for vaccine design, to identify consensus glycosylation patterns for translational applications.
References
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Journal ArticleDOI

Biopharmaceutical benchmarks 2014

TL;DR: Monoclonal antibodies continue their march on the markets, and optimized so-called biobetter versions of existing biologics are also gaining ground, but the rate of biosimilar approvals has seen a dramatic slowdown in recent years.
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Establishment of FUT8 knockout Chinese hamster ovary cells: an ideal host cell line for producing completely defucosylated antibodies with enhanced antibody-dependent cellular cytotoxicity.

TL;DR: The results demonstrate that FUT8−/− cells are ideal host cell lines to stably produce completely defucosylated high‐ADCC antibodies with fixed quality and efficacy for therapeutic use.
Journal ArticleDOI

Humanization of Yeast to Produce Complex Terminally Sialylated Glycoproteins

TL;DR: Yeast is a widely used recombinant protein expression system expanded by engineering the yeast Pichia pastoris to secrete human glycoproteins with fully complex terminally sialylated N-glycans, allowing it to replicate the sequential steps of human glycosylation.
Journal ArticleDOI

Glycoengineering: The effect of glycosylation on the properties of therapeutic proteins

TL;DR: The discovery of darbepoetin alfa (DA), a hyperglycosylated analogue of erythropoietin that contains two additional N-linked carbohydrates, a threefold increase in serum half-life and increased in vivo activity compared to recombinant human ery Anthropo-EPO, is discussed.
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