Posttranslational modification of therapeutic proteins in plants

被引:211
作者
Gomord, V [1 ]
Faye, L [1 ]
机构
[1] Univ Rouen, GDR 2590, IFRMP 23, CNRS,UMR 6037, F-76821 Mont St Aignan, France
关键词
D O I
10.1016/j.pbi.2004.01.015
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Plants have emerged as an alternative to current systems for the production of therapeutic proteins. The advantages of plants for the low-cost and large-scale production of safe and biologically active mammalian proteins have been documented recently. A major advantage of transgenic plants over production systems that are based on yeast or Escherichia coli is their ability to perform most of the posttranslational modifications (PTMs) that are required for the bioactivity and pharmacokinetics of recombinant therapeutic proteins. Furthermore, recent advances in the control of PTMs in transgenic plants have made it possible for plants to perform, at least to some extent, human-like modifications of recombinant proteins. Hence, plants have become a suitable alternative to animal cell factories for the production of therapeutic proteins.
引用
收藏
页码:171 / 181
页数:11
相关论文
共 48 条
[1]   Galactose-extended glycans of antibodies produced by transgenic plants [J].
Bakker, H ;
Bardor, M ;
Molthoff, JW ;
Gomord, V ;
Elbers, I ;
Stevens, LH ;
Jordi, W ;
Lommen, A ;
Faye, L ;
Lerouge, P ;
Bosch, D .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (05) :2899-2904
[2]   γ-glutamyl carboxylation:: An extracellular posttranslational modification that antedates the divergence of molluscs, arthropods, and chordates [J].
Bandyopadhyay, PK ;
Garrett, JE ;
Shetty, RP ;
Keate, T ;
Walker, CS ;
Olivera, BM .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (03) :1264-1269
[3]   Immunoreactivity in mammals of two typical plant glyco-epitopes, core α(1,3)-fucose and core xylose [J].
Bardor, M ;
Faveeuw, C ;
Fitchette, AC ;
Gilbert, D ;
Galas, L ;
Trottein, F ;
Faye, L ;
Lerouge, P .
GLYCOBIOLOGY, 2003, 13 (06) :427-434
[4]   Monoclonal C5-1 antibody produced in transgenic alfalfa plants exhibits a N-glycosylation that is homogenous and suitable for glyco-engineering into human-compatible structures [J].
Bardor, M ;
Loutelier-Bourhis, C ;
Paccalet, T ;
Cosette, P ;
Fitchette, AC ;
Vézina, LP ;
Trépanier, S ;
Dargis, M ;
Lemieux, R ;
Lange, C ;
Faye, L ;
Lerouge, P .
PLANT BIOTECHNOLOGY JOURNAL, 2003, 1 (06) :451-462
[5]  
BECKER GW, 1988, BIOTECHNOL APPL BIOC, V10, P326
[6]   N-glycosylation of a mouse IgG expressed in transgenic tobacco plants [J].
Cabanes-Macheteau, M ;
Fitchette-Lainé, AC ;
Loutelier-Bourhis, C ;
Lange, C ;
Vine, ND ;
Ma, JKC ;
Lerouge, P ;
Faye, L .
GLYCOBIOLOGY, 1999, 9 (04) :365-372
[7]   PROTEIN SORTING BY HIGH-PERFORMANCE LIQUID-CHROMATOGRAPHY .1. BIOMIMETIC INTERACTION CHROMATOGRAPHY OF RECOMBINANT HUMAN DEOXYRIBONUCLEASE-I ON POLYIONIC STATIONARY PHASES [J].
CACIA, J ;
QUAN, CP ;
VASSER, M ;
SLIWKOWSKI, MB ;
FRENZ, J .
JOURNAL OF CHROMATOGRAPHY, 1993, 634 (02) :229-239
[8]   POLYPEPTIDE LIGATION OCCURS DURING POST-TRANSLATIONAL MODIFICATION OF CONCANAVALIN-A [J].
CARRINGTON, DM ;
AUFFRET, A ;
HANKE, DE .
NATURE, 1985, 313 (5997) :64-67
[9]   A murine monoclonal antibody produced in transgenic plants with plant-specific glycans is not immunogenic in mice [J].
Chargelegue, D ;
Vine, ND ;
van Dolleweerd, CJ ;
Drake, PMW ;
Ma, JKC .
TRANSGENIC RESEARCH, 2000, 9 (03) :187-194
[10]   Reduction of CMP-N-acetylneuraminic acid hydroxylase activity in engineered Chinese hamster ovary cells using an antisense-RNA strategy [J].
Chenu, S ;
Grégoire, A ;
Malykh, Y ;
Visvikis, A ;
Monaco, L ;
Shaw, L ;
Schauer, R ;
Marc, A ;
Goergen, JL .
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 2003, 1622 (02) :133-144