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Background  Expression of economically relevant proteins in alternative expression platforms, especially plant expression platforms, has gained significant interest in recent years. A special interest in working with plants as bioreactors for the production of pharmaceutical proteins is related to low production costs, product safety and quality. Among the different properties that plants can also offer for the production of recombinant proteins, protein glycosylation is crucial since it may have an impact on pharmaceutical functionality and/or stability.    Results  The pharmaceutical glycoprotein human Granulocyte-Colony Stimulating Factor was transiently expressed in  Nicotiana benthamiana  plants and subjected to mammalian-specific mucin-type  O -glycosylation by co-expressing the pharmaceutical protein together with the glycosylation machinery responsible for such post-translational modification.    Conclusions  The pharmaceutical glycoprotein human Granulocyte-Colony Stimulating Factor can be expressed in  N. benthamiana  plants via agroinfiltration with its native mammalian-specific mucin-type  O -glycosylation.    Electronic supplementary material  The online version of this article (10.1186/s13007-018-0363-y) contains supplementary material, which is available to authorized users.

plant methods

Transient co-expression with three O-glycosylation enzymes allows production of GalNAc-O-glycosylated Granulocyte-Colony Stimulating Factor in N. benthamiana