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In vivo deglycosylation of recombinant proteins in plants by co-expression with bacterial PNGase F. | LitMetric

AI Article Synopsis

Article Abstract

At present, several eukaryotic expression systems including yeast, insect and mammalian cells and plants are used for the production of recombinant proteins. Proteins with potential N-glycosylation sites are efficiently glycosylated when expressed in these systems. However, the ability of the eukaryotic expression systems to glycosylate may be not desirable for some proteins. If target proteins that do not carry N-linked glycans in the native host contain potential N-linked glycosylation sites, they can be aberrantly glycosylated in the eukaryotic expression systems, thus, potentially impairing biological activity. Recently, we have developed a strategy of enzymatic deglycosylation of proteins in vivo by co-introducing bacterial PNGase F via agroinfiltration followed by transient expression in plants. (1) Here, we summarize our work on this topic and its potential implications.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3813534PMC
http://dx.doi.org/10.4161/bioe.23449DOI Listing

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