NDLI: Discovery and investigation of misincorporation of serine at asparagine positions in recombinant proteins expressed in Chinese hamster ovary cells.

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Discovery and investigation of misincorporation of serine at asparagine positions in recombinant proteins expressed in Chinese hamster ovary cells.

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Discovery and investigation of misincorporation of serine at asparagine positions in recombinant proteins expressed in Chinese hamster ovary cells.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gu, Sheng Dolnikova, Jana Su, Lihe Vecchi, Malgorzata M. Huang, Yao-ming Pederson, Nels Foley, Susan F. Wen, Dingyi Meier, Werner Garber, Ellen
Description	Author Affiliation: Wen D ( Biogen Idec Inc., 14 Cambridge Center, Cambridge, Massachusetts 02412, USA. dingyi.wen@biogenidec.com)
Abstract	Misincorporation of amino acids in proteins expressed in Escherichia coli has been well documented but not in proteins expressed in mammalian cells under normal recombinant protein production conditions. Here we report for the first time that Ser can be incorporated at Asn positions in proteins expressed in Chinese hamster ovary cells. This misincorporation was discovered as a result of intact mass measurement, peptide mapping analysis, and tandem mass spectroscopy sequencing. Our analyses showed that the substitution was not related to specific protein molecules or DNA codons and was not site-specific. We believe that the incorporation of Ser at sites coded for Asn was due to mischarging of tRNA(Asn) rather than to codon misreading. The rationale for substitution of Asn by Ser and not by other amino acids is also discussed. Further investigation indicated that the substitution was due to the starvation for Asn in the cell culture medium and that the substitution could be limited by using the Asn-rich feed. These observations demonstrate that the quality of expressed proteins should be closely monitored when altering cell culture conditions.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	47
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-11-20
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Asparagine Chemistry Recombinant Proteins Serine Animals CHO Cells Cloning, Molecular Cricetinae Cricetulus Escherichia Coli Metabolism Glycosylation Mass Spectrometry Models, Biological Peptide Mapping Peptides RNA, Transfer Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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