ArticleThe Journal of biological chemistry2009
Discovery and investigation of misincorporation of serine at asparagine positions in recombinant proteins expressed in Chinese hamster ovary cells.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 68 citations in OpenAlex.
- Sequence Variant Analysis During Cell Line Selection via High-Throughput Peptide Mapping.Advances in experimental medicine and biology · 2026Article
- Transfer RNAs: diversity in form and function.RNA biology · 2021Review
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- Identification of Lysine Misincorporation at Asparagine Position in Recombinant Insulin Analogs Produced in E. coli.Pharmaceutical research · 2019Article
- Macro- and Micro-Heterogeneity of Natural and Recombinant IgG Antibodies.Antibodies (Basel, Switzerland) · 2019Review
- Evolution of a comprehensive, orthogonal approach to sequence variant analysis for biotherapeutics.mAbs · 2019Review
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- Advancement in bioprocess technology: parallels between microbial natural products and cell culture biologics.Journal of industrial microbiology & biotechnology · 2017Review
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- Reduced amino acid specificity of mammalian tyrosyl-tRNA synthetase is associated with elevated mistranslation of Tyr codons.The Journal of biological chemistry · 2014Article
- Review
- Frameshifting dynamics.Biopolymers · 2013Review
- Adaptive translation as a mechanism of stress response and adaptation.Annual review of genetics · 2013Review
- Analytical tools for characterizing biopharmaceuticals and the implications for biosimilars.Nature reviews. Drug discovery · 2012Review
- Glycine to glutamic acid misincorporation observed in a recombinant protein expressed by Escherichia coli cells.Protein science : a publication of the Protein Society · 2012Article
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Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.