REVIEW: Main Strategies of Plant Expression System Glycoengineering for Producing Humanized Recombinant Pharmaceutical Proteins

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S. M. Rozov^1,2*, N. V. Permyakova¹, and E. V. Deineko^1,3

¹Federal Research Center Institute of Cytology and Genetics, Siberian Branch of the Russian Academy of Sciences, 630090 Novosibirsk, Russia; E-mail: rozov@bionet.nsc.ru

²Novosibirsk State University, 630090 Novosibirsk, Russia

³National Tomsk State University, 634050 Tomsk, Russia

^* To whom correspondence should be addressed.

Received September 26, 2017; Revision received November 3, 2017

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Most the pharmaceutical proteins are derived not from their natural sources, rather their recombinant analogs are synthesized in various expression systems. Plant expression systems, unlike mammalian cell cultures, combine simplicity and low cost of procaryotic systems and the ability for posttranslational modifications inherent in eucaryotes. More than 50% of all human proteins and more than 40% of the currently used pharmaceutical proteins are glycosylated, that is, they are glycoproteins, and their biological activity, pharmacodynamics, and immunogenicity depend on the correct glycosylation pattern. This review examines in detail the similarities and differences between N- and O-glycosylation in plant and mammalian cells, as well as the effect of plant glycans on the activity, pharmacokinetics, immunity, and intensity of biosynthesis of pharmaceutical proteins. The main current strategies of glycoengineering of plant expression systems aimed at obtaining fully humanized proteins for pharmaceutical application are summarized.

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KEY WORDS: protein glycosylation, glycoengineering, pharmaceutical proteins, plant expression systems, glycosyltransferases

DOI: 10.1134/S0006297918030033

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