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Simply better glycoproteins

Nature Biotechnology volume 32, pages 443–445 (2014)Cite this article

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Reducing the glycan heterogeneity of recombinant proteins may improve the efficacy of biopharmaceuticals.

Glycosylation is integral to more than half of eukaryotic proteins and influences many aspects of protein structure and function, including folding and stability, molecular recognition and immunogenicity1. Mammalian glycoproteins usually exist in many different glycoforms, and, in the context of protein therapeutics, this diversity can adversely affect drug potency and pharmacokinetics. In this issue, Meuris et al.2 present an elegant method to reduce the N-glycan heterogeneity of recombinant glycoproteins expressed in mammalian cells. By simplifying the N-glycosylation machinery, the authors expressed glycoproteins with smaller and more uniform glycan structures. This strategy opens the way for production of therapeutic glycoproteins of higher quality and efficacy.

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Figure 1: GlycoDelete system.

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Authors and Affiliations

  1. Department of Biomolecular Systems, Bernd Lepenies & Peter H. Seeberger are at the Max Planck Institute of Colloids and Interfaces, Potsdam, Germany,

    Bernd Lepenies & Peter H Seeberger

  2. Peter H. Seeberger is also at the Freie Universität Berlin, Institute of Chemistry and Biochemistry, Berlin, Germany.,

    Peter H Seeberger

Authors
  1. Bernd Lepenies
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  2. Peter H Seeberger
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Corresponding authors

Correspondence to Bernd Lepenies or Peter H Seeberger.

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The authors declare no competing financial interests.

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Lepenies, B., Seeberger, P. Simply better glycoproteins. Nat Biotechnol 32, 443–445 (2014). https://doi.org/10.1038/nbt.2893

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