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

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Main Strategies of Plant Expression System Glycoengineering for Producing Humanized Recombinant Pharmaceutical Proteins. / Rozov, S. M.; Permyakova, N. V.; Deineko, E. V.

In: Biochemistry (Moscow), Vol. 83, No. 3, 01.03.2018, p. 215-232.

Research output: Contribution to journal › Review article › peer-review

Author

Rozov, S. M. ; Permyakova, N. V. ; Deineko, E. V. / Main Strategies of Plant Expression System Glycoengineering for Producing Humanized Recombinant Pharmaceutical Proteins. In: Biochemistry (Moscow). 2018 ; Vol. 83, No. 3. pp. 215-232.

BibTeX

@article{57101e28bfa94b7da3d676add136b53b,

title = "Main Strategies of Plant Expression System Glycoengineering for Producing Humanized Recombinant Pharmaceutical Proteins",

abstract = "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.",

keywords = "glycoengineering, glycosyltransferases, pharmaceutical proteins, plant expression systems, protein glycosylation",

author = "Rozov, {S. M.} and Permyakova, {N. V.} and Deineko, {E. V.}",

note = "Publisher Copyright: {\textcopyright} 2018, Pleiades Publishing, Ltd. Copyright: Copyright 2018 Elsevier B.V., All rights reserved. Publisher Copyright: {\textcopyright} 2018, Pleiades Publishing, Ltd.",

year = "2018",

month = mar,

day = "1",

doi = "10.1134/S0006297918030033",

language = "English",

volume = "83",

pages = "215--232",

journal = "Biochemistry (Moscow)",

issn = "0006-2979",

publisher = "Maik Nauka-Interperiodica Publishing",

number = "3",

}

RIS

TY - JOUR

T1 - Main Strategies of Plant Expression System Glycoengineering for Producing Humanized Recombinant Pharmaceutical Proteins

AU - Rozov, S. M.

AU - Permyakova, N. V.

AU - Deineko, E. V.

PY - 2018/3/1

Y1 - 2018/3/1

N2 - 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.

AB - 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.

KW - glycoengineering

KW - glycosyltransferases

KW - pharmaceutical proteins

KW - plant expression systems

KW - protein glycosylation

UR - http://www.scopus.com/inward/record.url?scp=85044237770&partnerID=8YFLogxK

U2 - 10.1134/S0006297918030033

DO - 10.1134/S0006297918030033

M3 - Review article

C2 - 29625542

AN - SCOPUS:85044237770

VL - 83

SP - 215

EP - 232

JO - Biochemistry (Moscow)

JF - Biochemistry (Moscow)

SN - 0006-2979

IS - 3

ER -

ID: 12178950