W. Acosta, J. Ayala, M. C. Dolan, and C. L. Cramer, RTB Lectin: a novel receptor-independent delivery system for lysosomal enzyme replacement therapies, Sci. Rep, vol.5, p.14144, 2015.

S. Allmann, M. Mazet, N. Ziebart, G. Bouyssou, L. Fouillen et al., N-glycans of phaeodactylum tricornutum diatom and functional characterization of its Nacetylglucosaminyltransferase I enzyme, J. Biol. Chem, vol.9, pp.6152-6164, 2011.

H. Bakker, M. Bardor, J. W. Molthoff, V. Gomord, I. Elbers et al., Galactose-extended glycans of antibodies produced by transgenic plants, Proc. Natl. Acad. Sci. USA, vol.98, pp.2899-2904, 2001.

M. Bardor, Plant N-glycosylation: an engineered pathway for the production of therapeutical plant-derived glycoproteins, Comp. Biochem. Physiol. A: Mol. Integr. Physiol, vol.150, p.164, 2008.
URL : https://hal.archives-ouvertes.fr/hal-01848435

M. Bardor, C. Faveeuw, A. C. Fitchette, D. Gilbert, L. Galas et al., Immunoreactivity in mammals of two typical plant glycoepitopes, core alpha(1,3)-fucose and core xylose, Biotechnol. J, vol.13, pp.1473-1484, 2003.

R. J. Boado, Y. Zhang, C. F. Xia, Y. Wang, and W. M. Pardridge, Genetic engineering of a lysosomal enzyme fusion protein for targeted delivery across the human blood-brain barrier, Biotechnol. Bioeng, vol.99, pp.475-484, 2008.

S. A. Brooks, . Society, and F. E. Biology, Glycosylation in diverse cell systems: challenges and new frontiers in experimental biology, Essent. Rev. Exp. Biol, vol.4, pp.93-118, 2011.

C. H. Chen, K. R. Dellamaggiore, C. P. Ouellette, C. D. Sedano, M. Lizadjohry et al., Aptamer-based endocytosis of a lysosomal enzyme, Proc. Natl. Acad. Sci. USA, vol.105, pp.15908-15913, 2008.

R. S. Datia, J. K. Hammerlindl, B. Panchuk, L. E. Pelcher, and W. Keller, Modified binary plant transformation vectors with the wild-type gene encoding NPTII, Gene, vol.122, pp.383-384, 1992.

J. Dudek, S. Pfeffer, P. H. Lee, M. Jung, A. Cavalie et al., Protein transport into the human endoplasmic reticulum, J. Mol. Biol, vol.427, issue.6, pp.1159-1175, 2015.

,. Ele-ekouna, M. Boitel-conti, P. Lerouge, M. Bardor, and F. Guerineau, Enhanced production of recombinant human gastric lipase in turnip hairy roots, Plant Cell Tissue Organ Cult, vol.131, pp.601-610, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01777673

O. L. Gamborg, R. A. Miller, and K. Ojima, Nutrient requirements of suspension cultures of soybean root cells, Exp. Cell Res, vol.50, pp.151-158, 1968.

M. I. Georgiev, A. I. Pavlov, and T. Bley, Hairy root type plant in vitro systems as sources of bioactive substances, Appl. Microbiol. Biotechnol, vol.74, p.1175, 2007.

A. Giri and M. L. Narasu, Transgenic hairy roots, Biotechnol. Adv, vol.18, pp.1-22, 2000.

F. Guerineau, Tools for expressing foreign genes in plants, Plant Gene Transfer and Expression Protocols, pp.1-32, 1995.

S. Guillon, J. Tremouillaux-guiller, P. K. Pati, M. Rideau, and P. Gantet, Hairy root research: recent scenario and exciting prospects, Curr. Opin. Plant Biol, vol.3, pp.341-346, 2006.

S. Guillon, J. Tr-emouillaux-guiller, P. K. Pati, M. Rideau, and P. Gantet, Harnessing the potential of hairy roots: dawn of a new era, Trends Biotechnol, vol.24, pp.403-409, 2006.

X. He, T. Haselhorst, M. Von-itzstein, D. Kolarich, N. H. Packer et al., Production of a-L-iduronidase in maize for the ª 2018 The Authors, Plant Biotechnology Journal published by Society for Experimental Biology and The Association of Applied Biologists, vol.17, pp.505-516, 2012.

X. He, O. Pierce, T. Haselhorst, M. Von-itzstein, D. Kolarich et al., Characterization and downstream mannose phosphorylation of human recombinant a-L-iduronidase produced in Arabidopsis complex glycan-deficient (cgl) seeds, Plant Biotechnol. J, vol.11, pp.1034-1043, 2013.

S. C. Ho, M. Bardor, H. Feng, . Mariati, Y. W. Tong et al., IRES-mediated Tricistronic vectors for enhancing generation of high monoclonal antibody expressing CHO cell lines, J. Biotechnol, vol.157, pp.130-139, 2012.
URL : https://hal.archives-ouvertes.fr/hal-01844673

P. Hossler, S. F. Khattak, and Z. J. Li, Optimal and consistent protein glycosylation in mammalian cell culture, Glycobiology, vol.19, pp.936-949, 2009.

J. Hsu, D. Serrano, T. Bhowmick, K. Kumar, Y. Shen et al., Enhanced endothelial delivery and biochemical effects of alpha-galactosidase by ICAM-1-targeted nanocarriers for Fabry disease, J. Control. Release, vol.149, pp.323-331, 2011.

J. Hsu, L. Northrup, T. Bhowmick, and S. Muro, Enhanced delivery of alpha-glucosidase for Pompe disease by ICAM-1-targeted nanocarriers: comparative performance of a strategy for three distinct lysosomal storage disorders, Nanomedicine, vol.8, pp.731-739, 2012.

Y. Huet, J. P. Ekouna, A. Caron, K. Mezreb, M. Boitel-conti et al., Production and secretion of a heterologous protein by turnip hairy roots with superiority over tobacco hairy roots, Biotechnol. Lett, vol.36, pp.181-190, 2014.

G. Jung, M. Pabst, L. Neumann, A. Berger, and G. Lubec, Characterization of a-l-Iduronidase (Aldurazyme â ) and its complexes, 2013.

, Proteomics, vol.80, pp.26-33

E. D. Kakkis, A. Matynia, A. J. Jonas, and E. F. Neufeld, Overexpression of the human lysosomal enzyme a-L-iduronidase in Chinese hamster ovary cells, Protein Expr. Purif, vol.5, pp.225-232, 1994.

L. Kall, J. D. Canterbury, J. Weston, W. S. Noble, and M. J. Maccoss, Semi-supervised learning for peptide identification from shotgun proteomics datasets, Nat. Methods, vol.4, pp.923-925, 2007.

A. S. Karnoup, V. Turkelson, and W. H. Anderson, O-linked glycosylation in maize-expressed human IgA1, Glycobiology, vol.15, pp.965-981, 2005.

J. Kim, H. Park, B. T. Park, H. S. Hwang, J. I. Kim et al., O-glycans and O-glycosylation sites of recombinant human GM-CSF derived from suspension-cultured rice cells, and their structural role, Biochem. Biophys. Res. Comm, vol.479, pp.266-271, 2016.

L. Kober, C. Zehe, and J. Bode, Optimized signal peptides for the development of high expressing CHO cell lines, Biotechnol. Bioeng, vol.110, pp.1164-1173, 2013.

J. H. Lebowitz, J. H. Grubb, J. A. Maga, D. H. Schmiel, C. Vogler et al., Glycosylation-independent targeting enhances enzyme delivery to lysosomes and decreases storage in mucopolysaccharidosis type VII mice, Proc. Natl. Acad. Sci. USA, vol.101, pp.3083-3088, 2004.

N. Lingg, P. Zhang, Z. Song, and M. Bardor, The sweet tooth of biopharmaceuticals: Importance of recombinant protein glycosylation analysis, Biotechnol. J, vol.7, pp.1462-1472, 2012.
URL : https://hal.archives-ouvertes.fr/hal-01844671

C. Liu, M. J. Towler, G. Medrano, C. L. Cramer, and P. J. Weathers, Production of mouse interleukin-12 is greater in tobacco hairy roots grown in a mist reactor than in an airlift reactor, Biotechnol. Bioeng, vol.102, pp.1074-1086, 2009.

J. Z. Lu, R. J. Boado, E. K. Hui, Q. H. Zhou, and W. M. Pardridge, Expression in CHO cells and pharmacokinetics and brain uptake in the Rhesus monkey of an IgG-iduronate-2-sulfatase fusion protein, Biotechnol. Bioeng, vol.108, pp.1954-1964, 2011.

S. Markmann, M. Thelen, K. Cornils, M. Schweizer, N. Brocke-ahmadinejad et al., Lrp1/LDL receptor play critical roles in mannose 6-phosphate-independent lysosomal enzyme targeting, Traffic, vol.16, pp.743-759, 2015.

E. Mathieu-rivet, M. Scholz, C. Arias, F. Dardelle, S. Schulze et al., Exploring the N-glycosylation pathway in Chlamydomonas reinhardtii unravels novel complex structures, Mol. Cell Proteomics, vol.12, pp.3160-3183, 2013.
URL : https://hal.archives-ouvertes.fr/hal-00996460

F. Medina-bol-ivar and C. Cramer, Production of recombinant proteins by hairy roots cultured in plastic sleeve bioreactors, Recombinant Gene Expression: Reviews and Protocols, pp.351-363, 2004.

S. Muro, E. H. Schuchman, and V. R. Muzykantov, Lysosomal enzyme delivery by ICAM-1-targeted nanocarriers bypassing glycosylation-and clathrin-dependent endocytosis, Mol. Ther, vol.13, pp.135-141, 2006.

M. J. Osborn, R. T. Mcelmurry, B. Peacock, J. Tolar, and B. R. Blazar, Targeting of the CNS in MPS-IH using a nonviral transferrin-alpha-liduronidase fusion gene product, Mol. Ther, vol.16, pp.1459-1466, 2008.

L. Ou, T. L. Herzog, C. M. Wilmot, and C. B. Whitley, Standardization of alpha-L-iduronidase enzyme assay with Michaelis-Menten kinetics, Mol. Genet. Metab, vol.111, pp.113-115, 2014.

N. B. Pham, H. Schafer, and M. Wink, Production and secretion of recombinant thaumatin in tobacco hairy root cultures, Biotechnol. J, vol.7, pp.537-545, 2012.

O. M. Pierce, G. R. Mcnair, X. He, H. Kajiura, K. Fujiyama et al., N-glycan structures and downstream mannose-phosphorylation of plant recombinant human alpha-l-iduronidase: toward development of enzyme replacement therapy for mucopolysaccharidosis I, Plant Mol. Biol, vol.95, pp.593-606, 2017.

J. Pinkhasov, M. L. Alvarez, M. M. Rigano, K. Piensook, D. Larios et al., Recombinant plant-expressed tumour-associated MUC1 peptide is immunogenic and capable of breaking tolerance in MUC1.Tg mice, Plant Biotechnol. J, vol.9, pp.991-1001, 2011.

W. S. Prince, L. M. Mccormick, D. J. Wendt, P. A. Fitzpatrick, K. L. Schwartz et al., Lipoprotein receptor binding, cellular uptake, and lysosomal delivery of fusions between the receptor-associated protein (RAP) and a-l-iduronidase or acid a-glucosidase, J. Biol. Chem, vol.279, pp.35037-35046, 2004.

J. Schoberer and R. Strasser, Plant glyco-biotechnology, Semin. Cell Dev. Biol, vol.80, pp.133-141, 2017.

Y. Shaaltiel and Y. Tekoah, Plant specific N-glycans do not have proven adverse effects in humans, Nat. Biotechnol, vol.34, pp.706-708, 2016.

Y. Shaaltiel, G. Baum, S. Hashmueli, A. Lewkowicz, and D. Bartfeld, Plant cells expressing human glucocerebrosidase, 2015.

H. Sonoda, H. Morimoto, E. Yoden, Y. Koshimura, M. Kinoshita et al., A blood-brain-barrier-penetrating anti-human transferrin receptor antibody fusion protein for neuronopathic mucopolysaccharidosis II, Mol. Ther, vol.26, pp.1366-1374, 2018.

S. Srivastava and A. K. Srivastava, Hairy root culture for mass-production of high-value secondary metabolites, Crit. Rev. Biotechnol, vol.27, pp.29-43, 2007.

Y. Tekoah, Posttranslational modifications to plants -glycosylation, Encyclopedia of Genetics, 2006.

Y. Tekoah, S. Tzaban, T. Kizhner, M. Hainrichson, A. Gantman et al., Glycosylation and functionality of recombinant bglucocerebrosidase from various production systems, Biosci. Rep, vol.33, p.71, 2013.

G. Vanier, F. Hempel, P. Chan, M. Rodamer, D. Vaudry et al., Biochemical characterization of human anti-hepatitis B monoclonal antibody produced in the microalgae Phaeodactylum tricornutum, PLoS ONE, vol.10, p.139282, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01841078

G. Walsh and R. Jefferis, Post-translational modifications in the context of therapeutic proteins, Nat. Biotechnol, vol.24, pp.1241-1252, 2006.

R. Wongsamuth and P. M. Doran, Production of monoclonal antibodies by tobacco hairy roots, Biotechnol. Bioeng, vol.54, pp.401-415, 1997.

R. R. Woods, B. C. Geyer, and T. S. Mor, Hairy-root organ cultures for the production of human acetylcholinesterase, BMC Biotechnol, vol.8, p.95, 2008.

H. Xia, Q. Mao, and B. L. Davidson, The HIV Tat protein transduction domain improves the biodistribution of beta-glucuronidase expressed from recombinant viral vectors, Nat. Biotechnol, vol.19, pp.640-644, 2001.

X. Y. Zhang, A. Dinh, J. Cronin, S. C. Li, and J. Reiser, Cellular uptake and lysosomal delivery of galactocerebrosidase tagged with the HIV Tat protein transduction domain, J. Neurochem, vol.104, pp.1055-1064, 2008.

P. Zhang, T. Wang, M. Bardor, and Z. Song, Deciphering O-glycomics for the development and production of biopharmaceuticals, Pharm. Bioprocess, vol.1, pp.89-104, 2013.
URL : https://hal.archives-ouvertes.fr/hal-01846870

K. Zhao, K. F. Faull, E. D. Kakkis, and E. F. Neufeld, Carbohydrate structures of recombinant human a-l-iduronidase secreted by Chinese hamster ovary cells, J. Biol. Chem, vol.272, pp.22758-22765, 1997.

R. Zimmermann, S. Eyrisch, M. Ahmad, and V. Helms, Protein translocation across the ER membrane, Biochim. Biophys. Acta, vol.1808, pp.912-924, 2011.

, The Authors, hIDUA produced in Brassica rapa hairy root, vol.17, p.515, 2018.