Engineered CHO cells for production of diverse, homogeneous glycoproteins

Zhang Yang; Shengjun Wang; Adnan Halim; Morten Alder Schulz; Morten Frodin; Shamim H. Rahman; Malene Bech Vester-Christensen; Carsten Behrens; Claus Kristensen; Sergey Y. Vakhrushev; Eric Paul Bennett; Hans H. Wandall; Henrik Clausen

doi:10.1038/nbt.3280

Engineered CHO cells for production of diverse, homogeneous glycoproteins

Zhang Yang, Shengjun Wang, Adnan Halim, Morten Alder Schulz, Morten Frodin, Shamim H. Rahman, Malene Bech Vester-Christensen, Carsten Behrens, Claus Kristensen, Sergey Y. Vakhrushev, Eric Paul Bennett, Hans H. Wandall, Henrik Clausen

Novo Nordisk Foundation Center for Biosustainability

Research output: Contribution to journal › Journal article › Research › peer-review

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 alpha 2,6-linked sialic acid capping. This engineering approach will aid the production of glycoproteins with improved properties and therapeutic potential.

Original language	English
Journal	Nature Biotechnology
Volume	33
Issue number	8
Pages (from-to)	842-844
Number of pages	3
ISSN	1087-0156
DOIs	https://doi.org/10.1038/nbt.3280
Publication status	Published - 2015

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title = "Engineered CHO cells for production of diverse, homogeneous glycoproteins",

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 alpha 2,6-linked sialic acid capping. This engineering approach will aid the production of glycoproteins with improved properties and therapeutic potential.",

author = "Zhang Yang and Shengjun Wang and Adnan Halim and Schulz, {Morten Alder} and Morten Frodin and Rahman, {Shamim H.} and Vester-Christensen, {Malene Bech} and Carsten Behrens and Claus Kristensen and Vakhrushev, {Sergey Y.} and Bennett, {Eric Paul} and Wandall, {Hans H.} and Henrik Clausen",

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T1 - Engineered CHO cells for production of diverse, homogeneous glycoproteins

AU - Yang, Zhang

AU - Wang, Shengjun

AU - Halim, Adnan

AU - Schulz, Morten Alder

AU - Frodin, Morten

AU - Rahman, Shamim H.

AU - Vester-Christensen, Malene Bech

AU - Behrens, Carsten

AU - Kristensen, Claus

AU - Vakhrushev, Sergey Y.

AU - Bennett, Eric Paul

AU - Wandall, Hans H.

AU - Clausen, Henrik

PY - 2015

Y1 - 2015

N2 - 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 alpha 2,6-linked sialic acid capping. This engineering approach will aid the production of glycoproteins with improved properties and therapeutic potential.

AB - 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 alpha 2,6-linked sialic acid capping. This engineering approach will aid the production of glycoproteins with improved properties and therapeutic potential.

U2 - 10.1038/nbt.3280

DO - 10.1038/nbt.3280

M3 - Journal article

C2 - 26192319

SN - 1087-0156

VL - 33

SP - 842

EP - 844

JO - Nature Biotechnology

JF - Nature Biotechnology

IS - 8

ER -

Engineered CHO cells for production of diverse, homogeneous glycoproteins

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