Engineered CHO cells for production of diverse, homogeneous glycoproteins

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

University of Copenhagen
Danish Technical University
University of Copenhagen
Novo Nordisk A/S

Research output: Contribution to journal › Article › peer-review

225 Scopus citations

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.

Original language	English
Pages (from-to)	842-844
Number of pages	3
Journal	Nature Biotechnology
Volume	33
Issue number	8
DOIs	https://doi.org/10.1038/nbt.3280
State	Published - 10 Aug 2015
Externally published	Yes

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10.1038/nbt.3280

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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 α2,6-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 B.\} and Carsten Behrens and Claus Kristensen and Vakhrushev, \{Sergey Y.\} and Bennett, \{Eric Paul\} and Wandall, \{Hans H.\} and Henrik Clausen",

year = "2015",

month = aug,

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doi = "10.1038/nbt.3280",

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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 B.

AU - Behrens, Carsten

AU - Kristensen, Claus

AU - Vakhrushev, Sergey Y.

AU - Bennett, Eric Paul

AU - Wandall, Hans H.

AU - Clausen, Henrik

PY - 2015/8/10

Y1 - 2015/8/10

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 α2,6-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 α2,6-linked sialic acid capping. This engineering approach will aid the production of glycoproteins with improved properties and therapeutic potential.

UR - https://www.scopus.com/pages/publications/84938895840

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DO - 10.1038/nbt.3280

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AN - SCOPUS:84938895840

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

Abstract

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