메뉴 건너뛰기




Volumn 4, Issue 10, 2003, Pages 794-805

The production of recombinant pharmaceutical proteins in plants

Author keywords

[No Author keywords available]

Indexed keywords

AUTOANTIGEN; AVICIDIN; CAPSID PROTEIN; CARORX; CHOLERA TOXIN; CHOLERA TOXIN A2 SUBUNIT; CHOLERA TOXIN B SUBUNIT; ENTEROTOXIN; ESCHERICHIA COLI ENTEROTOXIN; HEPATITIS B SURFACE ANTIGEN; HEPATITIS E ANTIGEN; MONOCLONAL ANTIBODY T84.66; PORCINE TRANSMISSIBLE GASTROENTERITIS VIRUS GLYCOPROTEIN S; RECOMBINANT ANTIBODY; RECOMBINANT PROTEIN; ROTAVIRUS ENTEROTOXIN; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN; WATER;

EID: 0141706699     PISSN: 14710056     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrg1177     Document Type: Review
Times cited : (797)

References (111)
  • 1
    • 0035313153 scopus 로고    scopus 로고
    • Advances in Escherichia coli production of therapeutic proteins
    • Schwartz, J. R. Advances in Escherichia coli production of therapeutic proteins. Curr. Opin. Biotechnol. 12, 195-201 (2001).
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 195-201
    • Schwartz, J.R.1
  • 2
    • 0035313635 scopus 로고    scopus 로고
    • Industrial choices for protein production by large-scale cell culture
    • Chu, L. & Robinson, D. K. Industrial choices for protein production by large-scale cell culture. Curr. Opin. Biotechnol. 12, 180-187 (2001).
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 180-187
    • Chu, L.1    Robinson, D.K.2
  • 3
    • 0033672657 scopus 로고    scopus 로고
    • Transgenic animal bioreactors
    • Houdebaine, L. M. Transgenic animal bioreactors. Transgenic Res. 9, 305-320 (2000).
    • (2000) Transgenic Res. , vol.9 , pp. 305-320
    • Houdebaine, L.M.1
  • 4
    • 0033667765 scopus 로고    scopus 로고
    • Molecular farming of pharmaceutical proteins
    • Fischer, R. & Emans, N. Molecular farming of pharmaceutical proteins. Transgenic Res. 9, 279-299 (2000).
    • (2000) Transgenic Res. , vol.9 , pp. 279-299
    • Fischer, R.1    Emans, N.2
  • 5
    • 0035477961 scopus 로고    scopus 로고
    • Transgenic plants as protein factories
    • Giddings, G. Transgenic plants as protein factories. Curr. Opin. Biotechnol. 12, 450-454 (2001)
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 450-454
    • Giddings, G.1
  • 6
    • 0001081886 scopus 로고
    • The expression of a nopaline synthase human growth hormone chimaeric gene in transformed tobacco and sunflower callus tissue
    • Barta, A. et al. The expression of a nopaline synthase human growth hormone chimaeric gene in transformed tobacco and sunflower callus tissue. Plant Mol. Biol. 6, 347-357 (1986).
    • (1986) Plant Mol. Biol. , vol.6 , pp. 347-357
    • Barta, A.1
  • 7
    • 0024959945 scopus 로고
    • Production of antibodies in transgenic plants
    • Hiatt, A., Cafferkey, R. & Bowdish, K. Production of antibodies in transgenic plants. Nature 342, 76-78 (1989).
    • (1989) Nature , vol.342 , pp. 76-78
    • Hiatt, A.1    Cafferkey, R.2    Bowdish, K.3
  • 8
    • 0027048769 scopus 로고
    • Expression of hepatitis B surface antigen in transgenic plants
    • Mason, H. S., Lam, D. M. K. & Arntzen, C. J. Expression of hepatitis B surface antigen in transgenic plants. Proc. Natl Acad. Sci. USA 89, 11745-11749 (1992)
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 11745-11749
    • Mason, H.S.1    Lam, D.M.K.2    Arntzen, C.J.3
  • 10
    • 0141644652 scopus 로고    scopus 로고
    • Criteria for high-level expression of a fungal laccase gene in transgenic maize
    • Hood, E. E. et al. Criteria for high-level expression of a fungal laccase gene in transgenic maize. Plant Biotechnol. J. 1, 129-140 (2003).
    • (2003) Plant Biotechnol. J. , vol.1 , pp. 129-140
    • Hood, E.E.1
  • 11
    • 0000217415 scopus 로고    scopus 로고
    • Commercial production of avidin from transgenic maize: Characterization of transformant, production, processing, extraction and purification
    • Hood, E. E. et al. Commercial production of avidin from transgenic maize: characterization of transformant, production, processing, extraction and purification. Mol. Breeding 3, 291-306 (1997).
    • (1997) Mol. Breeding , vol.3 , pp. 291-306
    • Hood, E.E.1
  • 12
    • 0031194819 scopus 로고    scopus 로고
    • Expression of the human milk protein β-casein in transgenic potato plants
    • Chong, D. K. X. et al. Expression of the human milk protein β-casein in transgenic potato plants. Transgenic Res. 6, 289-296 (1997).
    • (1997) Transgenic Res. , vol.6 , pp. 289-296
    • Chong, D.K.X.1
  • 13
    • 0034598976 scopus 로고    scopus 로고
    • Triple helix assembly and processing of human collagen produced in transgenic tobacco plants
    • Ruggiero, F. et al. Triple helix assembly and processing of human collagen produced in transgenic tobacco plants. FEBS Lett. 469, 132-136 (2000).
    • (2000) FEBS Lett. , vol.469 , pp. 132-136
    • Ruggiero, F.1
  • 14
    • 0034016818 scopus 로고    scopus 로고
    • High-yield production of a human therapeutic protein in tobacco chloroplasts
    • Staub, J. M. et al. High-yield production of a human therapeutic protein in tobacco chloroplasts. Nature Biotechnol. 18, 333-338 (2000). This report shows that the secreted human protein somatotropin is soluble and biologically active when expressed in tobacco chloroplasts and has correctly formed disulphide bonds.
    • (2000) Nature Biotechnol. , vol.18 , pp. 333-338
    • Staub, J.M.1
  • 15
    • 85169106486 scopus 로고    scopus 로고
    • A chloroplast transgenic approach to hyper-express and purify human serum albumin, a protein highly susceptible to proteolytic degradation
    • Fernandez-San Millan, A., Mingo-Castel, A., Miller, M. & Daniell, H. A chloroplast transgenic approach to hyper-express and purify human serum albumin, a protein highly susceptible to proteolytic degradation. Plant Biotechnol 1, 77-79 (2003).
    • (2003) Plant Biotechnol , vol.1 , pp. 77-79
    • Fernandez-San Millan, A.1    Mingo-Castel, A.2    Miller, M.3    Daniell, H.4
  • 16
    • 0141533545 scopus 로고    scopus 로고
    • Oil bodies and associated proteins as affinity matrices. US Patent 6,509,453 (2003)
    • Moloney, M., Boothe, J. & Van Rooijen, G. Oil bodies and associated proteins as affinity matrices. US Patent 6,509,453 (2003).
    • Moloney, M.1    Boothe, J.2    Van Rooijen, G.3
  • 17
    • 0035313152 scopus 로고    scopus 로고
    • Therapeutic antibody expression technology
    • Chadd, H. E. & Chamow, S. M. Therapeutic antibody expression technology. Curr. Opin. Biotechnol. 12, 188-194 (2001).
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 188-194
    • Chadd, H.E.1    Chamow, S.M.2
  • 18
    • 0029035201 scopus 로고
    • Generation and assembly of secretory antibodies in plants
    • Ma, J. K. et al. Generation and assembly of secretory antibodies in plants. Science 268, 716-719 (1995). This study shows for the first time that secretory antibodies, with 10 polypeptide chains that represent the products of four genes, can be assembled correctly in transgenic plants. Two rounds of crossing, which involved four singly-transgenic lines, were required to stack all four transgenes in the same plant.
    • (1995) Science , vol.268 , pp. 716-719
    • Ma, J.K.1
  • 19
    • 0033758177 scopus 로고    scopus 로고
    • Production of hepatitis B surface antigen in transgenic plants for oral immunization
    • Richter, L. J., Thanavala, Y., Arntzen, C. J. & Mason, H. S. Production of hepatitis B surface antigen in transgenic plants for oral immunization. Nature Biotechnol. 18, 1167-1171 (2000).
    • (2000) Nature Biotechnol. , vol.18 , pp. 1167-1171
    • Richter, L.J.1    Thanavala, Y.2    Arntzen, C.J.3    Mason, H.S.4
  • 20
    • 0032863164 scopus 로고    scopus 로고
    • A plant-derived edible vaccine against hepatitis B virus
    • Kapusta, J. et al. A plant-derived edible vaccine against hepatitis B virus. FASEB J. 13, 1796-1799 (1999).
    • (1999) FASEB J. , vol.13 , pp. 1796-1799
    • Kapusta, J.1
  • 21
    • 0031863854 scopus 로고    scopus 로고
    • Immunogenicity in humans of a recombinant bacterial-antigen delivered in a transgenic potato
    • Tacket, C. O. et al. Immunogenicity in humans of a recombinant bacterial-antigen delivered in a transgenic potato. Nature Med. 4, 607-609 (1998).
    • (1998) Nature Med. , vol.4 , pp. 607-609
    • Tacket, C.O.1
  • 22
    • 0013651896 scopus 로고    scopus 로고
    • Human immune responses to a novel Norwalk virus vaccine delivered in transgenic potatoes
    • Tacket, C. O. et al. Human immune responses to a novel Norwalk virus vaccine delivered in transgenic potatoes. J. Infect. Dis. 182, 302-305 (2000).
    • (2000) J. Infect. Dis. , vol.182 , pp. 302-305
    • Tacket, C.O.1
  • 23
    • 0034030703 scopus 로고    scopus 로고
    • Expression of full-length bioactive antimicrobial human lactoferrin in potato plants
    • Chong, D. K. X. & Langridge, W. H. R. Expression of full-length bioactive antimicrobial human lactoferrin in potato plants. Transgenic Res. 9, 71-78 (2000).
    • (2000) Transgenic Res. , vol.9 , pp. 71-78
    • Chong, D.K.X.1    Langridge, W.H.R.2
  • 24
    • 0030447028 scopus 로고    scopus 로고
    • Expression of an environmentally friendly synthetic protein-based polymer in transgenic tobacco plants
    • Zhang, X. Urry, D. W. & Daniell, H. Expression of an environmentally friendly synthetic protein-based polymer in transgenic tobacco plants. Plant Cell Reps. 16, 174-179 (1996)
    • (1996) Plant Cell Reps. , vol.16 , pp. 174-179
    • Zhang, X.1    Urry, D.W.2    Daniell, H.3
  • 25
    • 0033984413 scopus 로고    scopus 로고
    • Stable expression of a biodegradable protein-based polymer in stable tobacco chloroplasts
    • Guda, C., Lee, S. B. & Daniell, H. Stable expression of a biodegradable protein-based polymer in stable tobacco chloroplasts. Plant Cell Reps. 19, 257-262 (2000).
    • (2000) Plant Cell Reps. , vol.19 , pp. 257-262
    • Guda, C.1    Lee, S.B.2    Daniell, H.3
  • 26
    • 0037181489 scopus 로고    scopus 로고
    • Hydroxylated human homotrimeric collagen I in Agrobacterium tumefaciens-mediated transient expression and in transgenic tobacco plant
    • Merle, C. et al. Hydroxylated human homotrimeric collagen I in Agrobacterium tumefaciens-mediated transient expression and in transgenic tobacco plant. FEBS Lett. 515, 114-118 (2002).
    • (2002) FEBS Lett. , vol.515 , pp. 114-118
    • Merle, C.1
  • 27
    • 0035007556 scopus 로고    scopus 로고
    • Production of spider silk proteins in tobacco and potato
    • Scheller, J., Guhrs, K. H., Grosse, F. & Conrad, U. Production of spider silk proteins in tobacco and potato Nature Biotechnol. 19, 573-577 (2001).
    • (2001) Nature Biotechnol. , vol.19 , pp. 573-577
    • Scheller, J.1    Guhrs, K.H.2    Grosse, F.3    Conrad, U.4
  • 28
    • 0021919918 scopus 로고
    • Identification of DNA sequences required for activity of the cauliflower mosaic virus 35S promoter
    • O'Dell, J. T., Nagy, F. & Chua, N. H. Identification of DNA sequences required for activity of the cauliflower mosaic virus 35S promoter. Nature 313, 810-812 (1985).
    • (1985) Nature , vol.313 , pp. 810-812
    • O'Dell, J.T.1    Nagy, F.2    Chua, N.H.3
  • 29
    • 0001354961 scopus 로고
    • Expression of a soybean β-conclycinin gene under the control of the cauliflower mosaic virus 35S and 19S promoters in transformed petunia tissues
    • Lawton, M. A. et al. Expression of a soybean β-conclycinin gene under the control of the cauliflower mosaic virus 35S and 19S promoters in transformed petunia tissues. Plant Mol. Biol. 9, 315-324 (1987).
    • (1987) Plant Mol. Biol. , vol.9 , pp. 315-324
    • Lawton, M.A.1
  • 30
    • 0023236892 scopus 로고
    • Duplication of CaMV- 35S promoter sequences creates a strong enhancer for plant genes
    • Kay, R., Chan, A. Daly, M. & McPherson, J. Duplication of CaMV-35S promoter sequences creates a strong enhancer for plant genes. Science 236, 1299-1302 (1987).
    • (1987) Science , vol.236 , pp. 1299-1302
    • Kay, R.1    Chan, A.2    Daly, M.3    McPherson, J.4
  • 31
    • 0030138945 scopus 로고    scopus 로고
    • Ubiquitin promoter-based vectors for high-level expression of selectable and/or screenable marker genes in monocotyledonous plants
    • Christensen, A. H. & Quail, P. H. Ubiquitin promoter-based vectors for high-level expression of selectable and/or screenable marker genes in monocotyledonous plants. Transgenic Res. 5, 213-218 (1996).
    • (1996) Transgenic Res. , vol.5 , pp. 213-218
    • Christensen, A.H.1    Quail, P.H.2
  • 32
    • 0030066414 scopus 로고    scopus 로고
    • Intron-mediated enhancement of gene expression in maize (Zea mays L.) and bluegrass (Poa pratensis L.)
    • Vain, P., Finer, K. R., Engler, D. E., Pratt, R. C. & Flner, J. J. Intron-mediated enhancement of gene expression in maize (Zea mays L.) and bluegrass (Poa pratensis L.). Plant Cell Rep. 15, 489-494 (1996).
    • (1996) Plant Cell Rep. , vol.15 , pp. 489-494
    • Vain, P.1    Finer, K.R.2    Engler, D.E.3    Pratt, R.C.4    Flner, J.J.5
  • 33
    • 0342748410 scopus 로고    scopus 로고
    • Cereal crops as viable production and storage systems for pharmaceutical scFv antibodies
    • Stoger E. et al. Cereal crops as viable production and storage systems for pharmaceutical scFv antibodies. Plant Mol. Biol. 42, 583-590 (2000).
    • (2000) Plant Mol. Biol. , vol.42 , pp. 583-590
    • Stoger, E.1
  • 35
    • 0037394628 scopus 로고    scopus 로고
    • Chemically regulated gene expression in plants
    • Padidam, M. Chemically regulated gene expression in plants. Curr. Opin. Plant Biol. 6, 169-177 (2003).
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 169-177
    • Padidam, M.1
  • 36
    • 0013057023 scopus 로고    scopus 로고
    • Chemical-inducible, ecdysone receptor-based gene expression system for plants
    • Padidam, M., Gore, M., Lu, D. L. & Smirnova, O. Chemical-inducible, ecdysone receptor-based gene expression system for plants. Transgenic Res. 12, 101-109 (2003).
    • (2003) Transgenic Res. , vol.12 , pp. 101-109
    • Padidam, M.1    Gore, M.2    Lu, D.L.3    Smirnova, O.4
  • 37
    • 0032952346 scopus 로고    scopus 로고
    • Transgenic plants for therapeutic proteins: Linking upstream and downstream technologies
    • Cramer C. L., Boothe, J. G. & Oishi, K. K. Transgenic plants for therapeutic proteins: linking upstream and downstream technologies. Curr. Top. Microbiol. Immunol. 240, 95-118 (1999).
    • (1999) Curr. Top. Microbiol. Immunol. , vol.240 , pp. 95-118
    • Cramer, C.L.1    Boothe, J.G.2    Oishi, K.K.3
  • 38
    • 0033178118 scopus 로고    scopus 로고
    • Apoplastic and cytosolic expression of full-size antibodies and antibody fragments in Nicotiana tabacum
    • Schillberg, S., Zimmermann, S., Voss, A. & Fischer, R. Apoplastic and cytosolic expression of full-size antibodies and antibody fragments in Nicotiana tabacum. Transgenic Res. 8, 255-263 (1999). This paper compares the stability of identical scFv antibodies that are targeted to different compartments, and shows that the secretory pathway is generally much more suitable for antibody accumulation than the cytosol.
    • (1999) Transgenic Res. , vol.8 , pp. 255-263
    • Schillberg, S.1    Zimmermann, S.2    Voss, A.3    Fischer, R.4
  • 39
    • 0002440028 scopus 로고    scopus 로고
    • High-level accumulation of single-chain variable fragments in the cytosol of transgenic Petunia hybrida
    • De Jaeger, G. et al. High-level accumulation of single-chain variable fragments in the cytosol of transgenic Petunia hybrida. Eur. J. Biochem. 259, 1-10 (1998).
    • (1998) Eur. J. Biochem. , vol.259 , pp. 1-10
    • De Jaeger, G.1
  • 40
    • 0037205497 scopus 로고    scopus 로고
    • Formation of disulfide bridges by a single-chain Fv antibody in the reducing ectopic environment of the plant cytosol
    • Schouten, A., Rossien, J., Bakker, J. & Schots, A. Formation of disulfide bridges by a single-chain Fv antibody in the reducing ectopic environment of the plant cytosol. J. Biol Chem 277, 19339-19345 (2002).
    • (2002) J. Biol Chem. , vol.277 , pp. 19339-19345
    • Schouten, A.1    Rossien, J.2    Bakker, J.3    Schots, A.4
  • 41
    • 0032168897 scopus 로고    scopus 로고
    • Compartment-specific accumulation of recombinant immunoglobulins in plant cells: An essential tool for antibody production and immunomodulation of physiological functions and pathogen activity
    • Conrad, U. & Fiedler, U. Compartment-specific accumulation of recombinant immunoglobulins in plant cells: an essential tool for antibody production and immunomodulation of physiological functions and pathogen activity. Plant Mol. Biol. 38, 101-109 (1998).
    • (1998) Plant Mol. Biol. , vol.38 , pp. 101-109
    • Conrad, U.1    Fiedler, U.2
  • 43
    • 0032573210 scopus 로고    scopus 로고
    • A viral suppressor of gene silencing in plants
    • Anandalakshmi, R. et al. A viral suppressor of gene silencing in plants. Proc. Natl Acad. Sci. USA 95, 13079-13084 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 13079-13084
    • Anandalakshmi, R.1
  • 44
    • 0037337257 scopus 로고    scopus 로고
    • Agrobacterium-mediated plant transformation: The biology behind the "gene-jockeying" tool
    • Gelvin, S. B. Agrobacterium-mediated plant transformation: the biology behind the "gene-jockeying" tool. Microbiol. Mol. Biol. Rev. 67, 16-23 (2003).
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 16-23
    • Gelvin, S.B.1
  • 45
    • 0013187276 scopus 로고    scopus 로고
    • Re-engineering plant gene targeting
    • Britt, A. B. & May, G. D. Re-engineering plant gene targeting. Trends Plant Sci. 8, 90-95 (2003).
    • (2003) Trends Plant Sci. , vol.8 , pp. 90-95
    • Britt, A.B.1    May, G.D.2
  • 46
    • 0141644651 scopus 로고    scopus 로고
    • The current status of plant transformation technologies
    • Veluthambi, K., Gupta, A. K. & Sharma, A. The current status of plant transformation technologies. Curr. Sci. India 84, 368-380 (2003).
    • (2003) Curr. Sci. India , vol.84 , pp. 368-380
    • Veluthambi, K.1    Gupta, A.K.2    Sharma, A.3
  • 47
    • 0030440711 scopus 로고    scopus 로고
    • Transformation technology
    • Christou, P. Transformation technology. Trends Plant Sci. 1, 423-431 (1996).
    • (1996) Trends Plant Sci. , vol.1 , pp. 423-431
    • Christou, P.1
  • 50
    • 0033197809 scopus 로고    scopus 로고
    • A simple method to enrich an Agrobacterium-transformed population for plants containing only T-DNA sequences
    • Hanson, B. et al. A simple method to enrich an Agrobacterium-transformed population for plants containing only T-DNA sequences. Plant J. 19, 727-734 (1999).
    • (1999) Plant J. , vol.19 , pp. 727-734
    • Hanson, B.1
  • 51
    • 0034112666 scopus 로고    scopus 로고
    • Linear transgene constructs lacking vector backbone sequences generate low-copy-number transgenic plants with simple integration patterns
    • Fu, X. et al. Linear transgene constructs lacking vector backbone sequences generate low-copy-number transgenic plants with simple integration patterns. Transgenic Res. 9, 11-19 (2000).
    • (2000) Transgenic Res. , vol.9 , pp. 11-19
    • Fu, X.1
  • 52
    • 0034570433 scopus 로고    scopus 로고
    • N-glycosylation of recombinant pharmaceutical glycoproteins produced in transgenic plants: Towards humanisation of plant N-glycans
    • Lerouge, P., Bardor, M., Pagny, S., Gomord, V. & Faye, L. N-glycosylation of recombinant pharmaceutical glycoproteins produced in transgenic plants: towards humanisation of plant N-glycans. Curr. Pharmaceutical Biotech. 1, 347-354 (2000).
    • (2000) Curr. Pharmaceutical Biotech. , vol.1 , pp. 347-354
    • Lerouge, P.1    Bardor, M.2    Pagny, S.3    Gomord, V.4    Faye, L.5
  • 53
    • 0038581900 scopus 로고    scopus 로고
    • Immunoreactivity in mammals of two typical plant glyco-epitopes: Core α(1,3)-fucose and core xylose
    • Bardor, M. et al. Immunoreactivity in mammals of two typical plant glyco-epitopes: core α(1,3)-fucose and core xylose. Glycobiology 13, 427-434 (2003).
    • (2003) Glycobiology , vol.13 , pp. 427-434
    • Bardor, M.1
  • 54
    • 0033805614 scopus 로고    scopus 로고
    • A murine monoclonal antibody produced in transgenic plants with plant-specific glycans is not immunogenic in mice
    • Chargelegue, D., Vine, N. D., van Dolleweerd, C. J., Drake, P. M. & Ma, J. K. A murine monoclonal antibody produced in transgenic plants with plant-specific glycans is not immunogenic in mice. Transgenic Res. 9, 187-194 (2000). The first published paper that discusses the immunogenicity of a plant-derived glycosylated recombinant protein.
    • (2000) Transgenic Res. , vol.9 , pp. 187-194
    • Chargelegue, D.1    Vine, N.D.2    Van Dolleweerd, C.J.3    Drake, P.M.4    Ma, J.K.5
  • 55
    • 0004055174 scopus 로고    scopus 로고
    • (eds Ernst, B., Hart, G. W. & Sanay, P.) (Wiley, New York)
    • Warner, T. G. in Carbohydrates in Chemistry and Biology (eds Ernst, B., Hart, G. W. & Sanay, P.) 1043-1064 (Wiley, New York, 2000).
    • (2000) Carbohydrates in Chemistry and Biology , pp. 1043-1064
    • Warner, T.G.1
  • 56
    • 0037157167 scopus 로고    scopus 로고
    • Efficient chemoenzymatic synthesis of O-linked sialyl oligosaccharides
    • Blixt, O., Allin, K., Pereira, L., Datta, A. & Paulson, J. C. Efficient chemoenzymatic synthesis of O-linked sialyl oligosaccharides. J. Am. Chem. Soc. 124, 5739-5746 (2002).
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5739-5746
    • Blixt, O.1    Allin, K.2    Pereira, L.3    Datta, A.4    Paulson, J.C.5
  • 57
    • 0035956939 scopus 로고    scopus 로고
    • Galactose-extended glycans of antibodies produced by transgenic plants
    • Bakker, H. et al. Galactose-extended glycans of antibodies produced by transgenic plants. Proc Natl Acad. Sci. USA 98, 2899-2904 (2001). In this study, a transgenic tobacco line that expressed the heavy and light chains of a murine antibody was crossed with a line that expressed human β-1,4-galactosyltransferase. The progeny produced antibodies ∼30% of which had partially galactosylated N-glycans, which provided a useful approach for the 'humanization' of plant glycans.
    • (2001) Proc Natl Acad. Sci. USA , vol.98 , pp. 2899-2904
    • Bakker, H.1
  • 58
    • 0034050074 scopus 로고    scopus 로고
    • Species-specific variation in glycosylation of IgG: Evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics
    • Raju, T. S., Briggs, J., Borge, S. M. & Jones, A. J. S. Species-specific variation in glycosylation of IgG: evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics. Glycobiology 10, 477-486 (2000). In this study, cell-specific glycosylation of immunoglobulins was studied by mass spectrometry and capillary electrophoresis/laser-induced fluorescence in 13 different animal systems. The glycan patterns were found to be unique in different species, which indicated that some might be more suitable than others for the production of human therapeutic proteins. The same might apply to plant systems, which were not considered in this paper.
    • (2000) Glycobiology , vol.10 , pp. 477-486
    • Raju, T.S.1    Briggs, J.2    Borge, S.M.3    Jones, A.J.S.4
  • 59
    • 0032916112 scopus 로고    scopus 로고
    • Production of recombinant proteins in plant root exudates
    • Borisjuk, N. V. et al. Production of recombinant proteins in plant root exudates. Nature Biotechnol. 17, 466-469 (1999).
    • (1999) Nature Biotechnol. , vol.17 , pp. 466-469
    • Borisjuk, N.V.1
  • 61
    • 0037703161 scopus 로고    scopus 로고
    • Rhizosecretion of a monoclonal antibody protein complex from transgenic tobacco roots
    • Drake, P. M. W. et al. Rhizosecretion of a monoclonal antibody protein complex from transgenic tobacco roots. Plant Mol. Biol. 52, 233-241 (2003).
    • (2003) Plant Mol. Biol. , vol.52 , pp. 233-241
    • Drake, P.M.W.1
  • 62
    • 0036008774 scopus 로고    scopus 로고
    • Engineering the plastid genome of higher plants
    • Maliga, P. Engineering the plastid genome of higher plants. Curr. Opin. Plant Biol. 5, 164-17212002).
    • (2002) Curr. Opin. Plant Biol. , vol.5 , pp. 164-1721
    • Maliga, P.1
  • 63
    • 0036481848 scopus 로고    scopus 로고
    • Milestones in chloroplast genetic engineering: An environmentally friendly era in biotechnology
    • Daniell, H., Khan, M. S. & Allison, L. Milestones in chloroplast genetic engineering: an environmentally friendly era in biotechnology. Trends Plant Sci. 7, 84-91 (2002).
    • (2002) Trends Plant Sci. , vol.7 , pp. 84-91
    • Daniell, H.1    Khan, M.S.2    Allison, L.3
  • 64
    • 0037440739 scopus 로고    scopus 로고
    • Expression of tetanus toxin fragment C in tobacco chloroplasts
    • Tregoning, J. S. et al. Expression of tetanus toxin fragment C in tobacco chloroplasts. Nucleic Acids Res. 31, 1174-1179 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , pp. 1174-1179
    • Tregoning, J.S.1
  • 65
    • 0035979785 scopus 로고    scopus 로고
    • Expression of the native cholera B toxin subunit gene and assembly as functional oligomers in transgenic tobacco chloroplasts
    • Daniell, H., Lee, S. B., Panchal, T. & Wiebe, P. O. Expression of the native cholera B toxin subunit gene and assembly as functional oligomers in transgenic tobacco chloroplasts J. Mol. Biol. 311, 1001-1009 (2001).
    • (2001) J. Mol. Biol. , vol.311 , pp. 1001-1009
    • Daniell, H.1    Lee, S.B.2    Panchal, T.3    Wiebe, P.O.4
  • 66
    • 0032852381 scopus 로고    scopus 로고
    • Fluorescent antibiotic resistance marker for tracking plastid transformation in higher plants
    • Khan, M. S. & Maliga, P. Fluorescent antibiotic resistance marker for tracking plastid transformation in higher plants. Nature Biotechnol. 17, 910-915 (1999).
    • (1999) Nature Biotechnol. , vol.17 , pp. 910-915
    • Khan, M.S.1    Maliga, P.2
  • 67
    • 0032846881 scopus 로고    scopus 로고
    • Towards molecular farming in the future: Using plant-cell-suspension cultures as bioreactors
    • Fischer, R., Emans, N., Schuster, F., Hellwig, S. & Drossard, J. Towards molecular farming in the future: using plant-cell-suspension cultures as bioreactors. Biotechnol. Appl. Biochem. 30, 109-112 (1999).
    • (1999) Biotechnol. Appl. Biochem. , vol.30 , pp. 109-112
    • Fischer, R.1    Emans, N.2    Schuster, F.3    Hellwig, S.4    Drossard, J.5
  • 68
    • 0036355659 scopus 로고    scopus 로고
    • Practical considerations for pharmaceutical antibody production in different crop systems
    • Stöger, E. et al. Practical considerations for pharmaceutical antibody production in different crop systems. Mol. Breeding 9, 149-158 (2002). This paper considers in detail the factors that should be evaluated when choosing a crop system for the production of pharmaceutical proteins. The same scFv is expressed in many species to compare intrinsic yields, and features such as storage, distribution and biosafety are discussed, as well as economic factors.
    • (2002) Mol. Breeding , vol.9 , pp. 149-158
    • Stöger, E.1
  • 69
    • 0011977387 scopus 로고    scopus 로고
    • Commercial production of β-glucuronidase (GUS): A model system for the procluction of proteins in plants
    • Witcher, D. et al. Commercial production of β-glucuronidase (GUS): a model system for the procluction of proteins in plants. Mol. Breeding 4, 301-312 (1998).
    • (1998) Mol. Breeding , vol.4 , pp. 301-312
    • Witcher, D.1
  • 70
    • 0036901079 scopus 로고    scopus 로고
    • Monoclonal antibody manufacturing in transgenic plants - Myths and realities
    • Hood, E. E., Woodard, S. L. & Horn, M. E. Monoclonal antibody manufacturing in transgenic plants - myths and realities. Curr. Opin. Biotechnol. 13, 630-635 (2002).
    • (2002) Curr. Opin. Biotechnol. , vol.13 , pp. 630-635
    • Hood, E.E.1    Woodard, S.L.2    Horn, M.E.3
  • 71
    • 0037070490 scopus 로고    scopus 로고
    • From green plants to industnal enzymes
    • Hood, E. E. From green plants to industnal enzymes. Enzyme Microbial. Technol. 30, 279-283 (2002).
    • (2002) Enzyme Microbial. Technol. , vol.30 , pp. 279-283
    • Hood, E.E.1
  • 72
    • 0031790556 scopus 로고    scopus 로고
    • A humanized monoclonal antibody produced in transgenic plants for immunoprotection of the vagina against genital herpes
    • Zeitlin, L. et al. A humanized monoclonal antibody produced in transgenic plants for immunoprotection of the vagina against genital herpes. Nature Biotechnol. 16, 1361-1364 (1998).
    • (1998) Nature Biotechnol. , vol.16 , pp. 1361-1364
    • Zeitlin, L.1
  • 73
    • 0033587793 scopus 로고    scopus 로고
    • Production of a diagnostic monoclonal antibody in perennial alfalfa plants
    • Khoudi, H. et al. Production of a diagnostic monoclonal antibody in perennial alfalfa plants. Biotechnol Bioeng 64, 135-143 (1999).
    • (1999) Biotechnol. Bioeng , vol.64 , pp. 135-143
    • Khoudi, H.1
  • 74
    • 0033772176 scopus 로고    scopus 로고
    • Transgenic pea seeds as bioreactors for the production of a single-chain Fv fragment (scFV) antibody used in cancer diagnosis and therapy
    • Perrin, Y. et al. Transgenic pea seeds as bioreactors for the production of a single-chain Fv fragment (scFV) antibody used in cancer diagnosis and therapy. Mol. Breeding 6, 345-352 (2000).
    • (2000) Mol. Breeding , vol.6 , pp. 345-352
    • Perrin, Y.1
  • 75
    • 0036383059 scopus 로고    scopus 로고
    • Expression of antibodies and Fab fragments in transgenic potato plants: A case study for bulk production in crop plants
    • De Wilde, C., Peeters, K., Jacobs, A. Peck, I. & Depicker, A. Expression of antibodies and Fab fragments in transgenic potato plants: a case study for bulk production in crop plants. Mol. Breeding 9, 2871-282 (2002).
    • (2002) Mol. Breeding , vol.9 , pp. 2871-2282
    • De Wilde, C.1    Peeters, K.2    Jacobs, A.3    Peck, I.4    Depicker, A.5
  • 76
    • 0036342361 scopus 로고    scopus 로고
    • Biopharming the Simpli-RED™ HIV diagnostic reagent in barley, potato and tobacco
    • Schunmann, P. H. D., Coia, G. & Waterhouse, P. M. Biopharming the Simpli-RED™ HIV diagnostic reagent in barley, potato and tobacco. Mol. Breeding 9, 113-121 (2002).
    • (2002) Mol. Breeding , vol.9 , pp. 113-121
    • Schunmann, P.H.D.1    Coia, G.2    Waterhouse, P.M.3
  • 77
    • 0028863460 scopus 로고
    • Expression of the rabies virus glycoprotein in transgenic tomatoes
    • McGarvey, P. B. et al. Expression of the rabies virus glycoprotein in transgenic tomatoes. Biotechnology 13, 1484-1487 (1995)
    • (1995) Biotechnology , vol.13 , pp. 1484-1487
    • McGarvey, P.B.1
  • 78
    • 0037472387 scopus 로고    scopus 로고
    • Vaccine antigen production in transgenic plants: Strategies gene constructs and perspectives
    • Sala, F. et al. Vaccine antigen production in transgenic plants: strategies, gene constructs and perspectives Vaccine 21, 803-808 (2003)
    • (2003) Vaccine , vol.21 , pp. 803-808
    • Sala, F.1
  • 79
    • 0041602667 scopus 로고    scopus 로고
    • The biosafety of molecular farming in plants
    • ABN 110
    • Commandeur, U., Twyman, R. M. & Fischer, R. The biosafety of molecular farming in plants AgBiotechNet 5, ABN 110 (2003).
    • (2003) AgBiotechNet , vol.5
    • Commandeur, U.1    Twyman, R.M.2    Fischer, R.3
  • 80
    • 0035984713 scopus 로고    scopus 로고
    • Excision of selectable marker genes from transgenic plants
    • Hare, P. D. & Chua, N.-H. Excision of selectable marker genes from transgenic plants. Nature Biotechnol. 20, 575-579 (2002).
    • (2002) Nature Biotechnol. , vol.20 , pp. 575-579
    • Hare, P.D.1    Chua, N.-H.2
  • 81
    • 0036537227 scopus 로고    scopus 로고
    • Marker-free transformation: Increasing transformation frequency by the use of regeneration-promoting genes
    • Zuo, J. R., Niu, Q. W., Ikeda, Y. & Chua, N. H. Marker-free transformation: increasing transformation frequency by the use of regeneration-promoting genes. Curr. Opin. Biotechnol. 13, 173-180 (2002).
    • (2002) Curr. Opin. Biotechnol. , vol.13 , pp. 173-180
    • Zuo, J.R.1    Niu, Q.W.2    Ikeda, Y.3    Chua, N.H.4
  • 83
    • 0036307494 scopus 로고    scopus 로고
    • In situ transfer of antibiotic resistance genes from transgenic (transplastomic) tobacco plants to bacteria
    • Kay, E., Vogel, T. M., Bertolla, F., Nalin, R. & Simonet, P. In situ transfer of antibiotic resistance genes from transgenic (transplastomic) tobacco plants to bacteria. Appl. Environ. Microbiol. 68, 3345-3351 (2002).
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3345-3351
    • Kay, E.1    Vogel, T.M.2    Bertolla, F.3    Nalin, R.4    Simonet, P.5
  • 85
    • 0042750509 scopus 로고    scopus 로고
    • Product differentiation alternatives: Identity preservation, segregation and traceability
    • Smyth, S & Phillips, R. W. B. Product differentiation alternatives: identity preservation, segregation and traceability. AgBioForum 5, 30-42 (2002).
    • (2002) AgBioForum , vol.5 , pp. 30-42
    • Smyth, S.1    Phillips, R.W.B.2
  • 86
    • 0037362471 scopus 로고    scopus 로고
    • Molecular farming of recombinant antibodies in plants
    • Schillberg, S., Fischer, R. & Emans, N. Molecular farming of recombinant antibodies in plants. Cell. Mol. Life Sci. 60, 433-445 (2003). This is a comprehensive discussion of the technical issues concerning the production of antibodies in plants, which is treated in much more detail than is possible in the present review.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 433-445
    • Schillberg, S.1    Fischer, R.2    Emans, N.3
  • 88
    • 0033582277 scopus 로고    scopus 로고
    • Rapid production of specific vaccines for lymphoma by expression of the tumor-derived single-chain Fv epitopes in tobacco plants
    • McCormick, A. A. et al. Rapid production of specific vaccines for lymphoma by expression of the tumor-derived single-chain Fv epitopes in tobacco plants. Proc. Natl Acad. Sci. USA 96, 703-708 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 703-708
    • McCormick, A.A.1
  • 89
    • 0034825803 scopus 로고    scopus 로고
    • Production of secretory IgA antibodies in plants
    • Larrick, J. W., Yu, L., Naftzger, C., Jaiswat, S. & Wycoff, K. Production of secretory IgA antibodies in plants. Biomolecular Eng. 18, 87-94 (2001). This paper presents a useful summary of recent advances in the plant-based production of secretory IgAs with a discussion of purification methods and production costs.
    • (2001) Biomolecular Eng. , vol.18 , pp. 87-94
    • Larrick, J.W.1    Yu, L.2    Naftzger, C.3    Jaiswat, S.4    Wycoff, K.5
  • 90
    • 0031835622 scopus 로고    scopus 로고
    • Characterization of a recombinant plant monoclonal secretory antibody and preventive immunotherapy in humans
    • Ma, J. K. et al. Characterization of a recombinant plant monoclonal secretory antibody and preventive immunotherapy in humans. Nature Med. 4, 601-605 (1998).
    • (1998) Nature Med. , vol.4 , pp. 601-605
    • Ma, J.K.1
  • 91
    • 0036515168 scopus 로고    scopus 로고
    • A carcinoembryonic antigen-specific diabody produced in tobacco
    • Vaquero, C. et al. A carcinoembryonic antigen-specific diabody produced in tobacco. FASEB J. 16, 408-410 (2002).
    • (2002) FASEB J. , vol.16 , pp. 408-410
    • Vaquero, C.1
  • 92
    • 0035988504 scopus 로고    scopus 로고
    • Efficacy of plant-produced recombinant antibodies against HCG
    • Kathuria, S. et al. Efficacy of plant-produced recombinant antibodies against HCG. Human Reproduction 17, 2054-2061 (2002).
    • (2002) Human Reproduction , vol.17 , pp. 2054-2061
    • Kathuria, S.1
  • 93
    • 0031081649 scopus 로고    scopus 로고
    • Plants as bioreactors for pharmaceuticals: Regulatory considerations
    • Miele, L. Plants as bioreactors for pharmaceuticals: regulatory considerations. Trends Biotechnol. 15, 45-50 (1997).
    • (1997) Trends Biotechnol. , vol.15 , pp. 45-50
    • Miele, L.1
  • 94
    • 0038769415 scopus 로고    scopus 로고
    • (eds Hood, E. E. & Howard, J.) (Kluwer Academic, New York
    • Emlay, D. in Plants as Factories for Protein Production (eds Hood, E. E. & Howard, J.) 175-180 (Kluwer Academic, New York, 2002).
    • (2002) Plants as Factories for Protein Production , pp. 175-180
    • Emlay, D.1
  • 97
    • 0033779268 scopus 로고    scopus 로고
    • Plasma membrane display of anti-viral single chain Fv fragments confers resistance to tobacco mosaic virus
    • Schillberg, S., Zimmermann, S., Findlay, K. & Fischer, R. Plasma membrane display of anti-viral single chain Fv fragments confers resistance to tobacco mosaic virus. Mol. Breeding 6, 317-326 (2000).
    • (2000) Mol. Breeding , vol.6 , pp. 317-326
    • Schillberg, S.1    Zimmermann, S.2    Findlay, K.3    Fischer, R.4
  • 98
    • 0025271471 scopus 로고
    • Production of correctly processed human serum albumin in transgenic plants
    • Sijmons, P. C. et al. Production of correctly processed human serum albumin in transgenic plants. Biotechnology 8, 217-221 (1990).
    • (1990) Biotechnology , vol.8 , pp. 217-221
    • Sijmons, P.C.1
  • 99
    • 0006878489 scopus 로고
    • Expression of human α-interferon in plants
    • Zhu, Z. et al. Expression of human α-interferon in plants. Virology 172, 213-222 (1994).
    • (1994) Virology , vol.172 , pp. 213-222
    • Zhu, Z.1
  • 100
    • 0029257224 scopus 로고
    • Characterisation of a human glycoprotein (erythropoetin) produced in cultured tobacco cells
    • Matsumoto, S., Ikura, K, Ueda, M. & Sasaki, R. Characterisation of a human glycoprotein (erythropoetin) produced in cultured tobacco cells. Plant Mol. Biol. 27, 1163-1172 (1995).
    • (1995) Plant Mol. Biol. , vol.27 , pp. 1163-1172
    • Matsumoto, S.1    Ikura, K.2    Ueda, M.3    Sasaki, R.4
  • 102
    • 0033498455 scopus 로고    scopus 로고
    • Rice cell culture as an alternative production system for functional diagnostic and therapeutic antibodies
    • Torres, E. et al. Rice cell culture as an alternative production system for functional diagnostic and therapeutic antibodies. Transgenic Res. 8, 441-449 (1999).
    • (1999) Transgenic Res. , vol.8 , pp. 441-449
    • Torres, E.1
  • 103
    • 0032695258 scopus 로고    scopus 로고
    • Production of functional human α1-antitrypsin by plant cell culture
    • Terashima, M. et al. Production of functional human α1-antitrypsin by plant cell culture. Appl. Microbiol. Biotechnol. 52, 516-523 (1999).
    • (1999) Appl. Microbiol. Biotechnol. , vol.52 , pp. 516-523
    • Terashima, M.1
  • 104
    • 0025477259 scopus 로고
    • Synthesis and self-assembly of a functional monoclonal antibody in transgenic Nicotiana tabacum
    • Düring, K., Hippe, S., Kreuzaler, F. & Schell, J. Synthesis and self-assembly of a functional monoclonal antibody in transgenic Nicotiana tabacum. Plant Mol. Biol. 15, 281-293 (1990).
    • (1990) Plant Mol. Biol. , vol.15 , pp. 281-293
    • Düring, K.1    Hippe, S.2    Kreuzaler, F.3    Schell, J.4
  • 105
    • 0029035201 scopus 로고
    • Generation and assembly of secretory antibodies in plants
    • Ma, J. K.-C. et al. Generation and assembly of secretory antibodies in plants. Science 268, 716-719 (1995).
    • (1995) Science , vol.268 , pp. 716-719
    • Ma, J.K.-C.1
  • 106
    • 0031239836 scopus 로고    scopus 로고
    • Expression and characterization of bryodin 1 and a bryodin 1-based single-chain immunotoxin from tobacco cell culture
    • Francisco, J. A. et al. Expression and characterization of bryodin 1 and a bryodin 1-based single-chain immunotoxin from tobacco cell culture. Bioconjug. Chem. 8, 708-713 (1997).
    • (1997) Bioconjug. Chem. , vol.8 , pp. 708-713
    • Francisco, J.A.1
  • 107
    • 0037457888 scopus 로고    scopus 로고
    • Expression and assembly of a fully active antibody in algae
    • Mayfield, S. P. et al. Expression and assembly of a fully active antibody in algae. Proc. Natl Acad. Sci. USA 100, 438-442 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 438-442
    • Mayfield, S.P.1
  • 108
    • 0035925713 scopus 로고    scopus 로고
    • Plant-based vaccines: Unique advantages
    • Streatfield, S. J. et al. Plant-based vaccines: unique advantages. Vaccine 19, 2742-2748 (2001).
    • (2001) Vaccine , vol.19 , pp. 2742-2748
    • Streatfield, S.J.1
  • 109
    • 0030791484 scopus 로고    scopus 로고
    • Transgenic plants expressing autoantigens fed to mice to induce oral immune tolerance
    • Ma, S. W. et al. Transgenic plants expressing autoantigens fed to mice to induce oral immune tolerance. Nature Med. 3, 793-796 (1997).
    • (1997) Nature Med. , vol.3 , pp. 793-796
    • Ma, S.W.1
  • 110
    • 0035018196 scopus 로고    scopus 로고
    • A plant-based multicomponent vaccine protects mice from enteric diseases
    • Yu, J. & Langridge, W. H. A plant-based multicomponent vaccine protects mice from enteric diseases. Nature Biotechnol. 19, 548-552 (2001).
    • (2001) Nature Biotechnol. , vol.19 , pp. 548-552
    • Yu, J.1    Langridge, W.H.2
  • 111
    • 0037073630 scopus 로고    scopus 로고
    • Delivery of subunit vaccines in maize seed
    • Lamphear, B. J. et al. Delivery of subunit vaccines in maize seed. J. Control Release 83, 169-180 (2002).
    • (2002) J. Control Release , vol.83 , pp. 169-180
    • Lamphear, B.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.