Recombinant glycoproteins: The impact of cell lines and culture conditions on the generation of protein species

Journal of Proteomics
Julia RosenlöcherStephan Hinderlich

Abstract

Glycosylation is the most complex post-translational modification. Thus, it contributes to versatile chemical compositions of proteins, leading to high amounts of protein species. The structural heterogeneity of glycoproteins was also described by the definition of glycoforms. We therefore introduced a new term called "glycoprotein species" to join the two concepts from different fields of biology. In this study, we further determined the theoretical numbers of glycoprotein species of two recombinant glycoproteins - a therapeutical antibody and the human protease inhibitor alpha-1-antitrypsin (A1AT) - based on structural analysis of their N-glycans. Moreover, we showed that variations in the used cell lines and their cultivation conditions strongly influence the number of glycoprotein species in case of recombinant A1AT production. Protein glycosylation is a major source for the huge amount of protein species. This study extends the sight of protein species by the following contributions: 1) The new term "glycoprotein species" was defined to introduce the concept of glycoforms into the field. 2) An estimation of the number of potential glycoprotein species of two particular glycoproteins was given. 3) The influence of productio...Continue Reading

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Aug 15, 2015·Protein Expression and Purification·Julia RosenlöcherStephan Hinderlich

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Citations

Nov 22, 2016·European Journal of Pharmaceutics and Biopharmaceutics : Official Journal of Arbeitsgemeinschaft Für Pharmazeutische Verfahrenstechnik E.V·Agustina GugliottaMarcos Oggero
Dec 22, 2017·Critical Reviews in Biotechnology·Justin Bryan Goh, Say Kong Ng
Aug 1, 2018·Biotechnology and Bioengineering·Kelvin S NgJeffrey M Karp
Nov 30, 2015·Bioengineering·Julia RosenlöcherStephan Hinderlich

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