Abstract
BackgroundExpression 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.ResultsThe 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.ConclusionsThe 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.
Highlights
Expression of economically relevant proteins in alternative expression platforms, especially plant expression platforms, has gained significant interest in recent years
Two other Granulocyte-Colony Stimulating Factor (G-CSF) variants were built, which would target the recombinant protein to the cytosol and as ER-derived protein bodies
All of the G-CSF variant constructs-containing Agrobacterium strains were co-infiltrated with an Agrobacterium strain containing the p19 construct, a post-transcriptional gene silencing suppressor from Cymbidium ringspot tombusvirus (CymRSV) [40]
Summary
Expression of economically relevant proteins in alternative expression platforms, especially plant expression platforms, has gained significant interest in recent years. Plants have emerged as alternative expression systems for the production of pharmaceutical proteins [1,2,3,4]. While there are several advantages to using plants as expression systems, such as low cost of production and maintenance, fast scalability, biological safety, and proper protein folding and assembly [1,2,3, 5], there are some limitations concerning bioactivity or quality of the produced proteins [6]. Further maturation of the plant core N-glycan typically results in a biantennary structure, occasionally with terminal Lewis A epitopes. Terminal Lewis A epitopes are rarely observed in human proteins, but are widely distributed in plant glycoproteins.
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