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Volumn 153, Issue 3-4, 2011, Pages 160-166

Insect cells for antibody production: Evaluation of an efficient alternative

Author keywords

" High Five" cells; Baculovirus; Insect cells; Monoclonal antibodies; N linked glycosylation

Indexed keywords

'' HIGH FIVE'' CELLS; ANTIBODY PRODUCTION; ANTIGEN BINDING; BACULOVIRUS; CHINESE HAMSTER OVARY CELLS; GLYCOFORMS; HEAVY CHAIN; INSECT CELL LINES; INSECT CELL SYSTEMS; INSECT CELLS; MAMMALIAN CELLS; N-GLYCANS; N-LINKED; N-LINKED GLYCOSYLATION; OLIGOSACCHARIDE STRUCTURE; PRODUCT YIELDS; SPODOPTERA FRUGIPERDA; THERAPEUTIC MONOCLONAL ANTIBODIES; TRANSIENT EXPRESSION; TRICHOPLUSIA NI;

EID: 79955775743     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2011.02.009     Document Type: Article
Times cited : (30)

References (35)
  • 1
    • 33846187538 scopus 로고    scopus 로고
    • The role of protein glycosylation in allergy
    • Altmann F. The role of protein glycosylation in allergy. Int. Arch. Allergy Immunol. 2007, 142:99-115.
    • (2007) Int. Arch. Allergy Immunol. , vol.142 , pp. 99-115
    • Altmann, F.1
  • 3
    • 65649154135 scopus 로고    scopus 로고
    • Short-hairpin-RNA-mediated silencing of fucosyltransferase 8 in Chinese-hamster ovary cells for the production of antibodies with enhanced antibody immune effector function
    • Beuger V., Kunkele K.P., Koll H., Gartner A., Bahner M., Burtscher H., Klein C. Short-hairpin-RNA-mediated silencing of fucosyltransferase 8 in Chinese-hamster ovary cells for the production of antibodies with enhanced antibody immune effector function. Biotechnol. Appl. Biochem. 2009, 53:31-37.
    • (2009) Biotechnol. Appl. Biochem. , vol.53 , pp. 31-37
    • Beuger, V.1    Kunkele, K.P.2    Koll, H.3    Gartner, A.4    Bahner, M.5    Burtscher, H.6    Klein, C.7
  • 5
    • 0021760375 scopus 로고
    • Assembly of functional antibodies from immunoglobulin heavy and light chains synthesised in E. coli
    • Boss M., Kenten J., Wood C., Emtage J. Assembly of functional antibodies from immunoglobulin heavy and light chains synthesised in E. coli. Nucleic Acids Res. 1984, 12:3791-3806.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 3791-3806
    • Boss, M.1    Kenten, J.2    Wood, C.3    Emtage, J.4
  • 6
    • 0035817416 scopus 로고    scopus 로고
    • Improved glycosylation of a foreign protein by Tn-5B1-4 cells engineered to express mammalian glycosyltransferases
    • Breitbach K., Jarvis D.L. Improved glycosylation of a foreign protein by Tn-5B1-4 cells engineered to express mammalian glycosyltransferases. Biotechnol. Bioeng. 2001, 74:230-239.
    • (2001) Biotechnol. Bioeng. , vol.74 , pp. 230-239
    • Breitbach, K.1    Jarvis, D.L.2
  • 10
    • 33846126638 scopus 로고    scopus 로고
    • Antibody production with yeasts and filamentous fungi: on the road to large scale?
    • Gasser B., Mattanovich D. Antibody production with yeasts and filamentous fungi: on the road to large scale?. Biotechnol. Lett. 2007, 29:201-212.
    • (2007) Biotechnol. Lett. , vol.29 , pp. 201-212
    • Gasser, B.1    Mattanovich, D.2
  • 11
    • 2242455924 scopus 로고    scopus 로고
    • Engineering the protein N-glycosylation pathway in insect cells for production of biantennary, complex N-glycans
    • Hollister J., Grabenhorst E., Nimtz M., Conradt H., Jarvis D.L. Engineering the protein N-glycosylation pathway in insect cells for production of biantennary, complex N-glycans. Biochemistry 2002, 41:15093-15104.
    • (2002) Biochemistry , vol.41 , pp. 15093-15104
    • Hollister, J.1    Grabenhorst, E.2    Nimtz, M.3    Conradt, H.4    Jarvis, D.L.5
  • 12
    • 31844447560 scopus 로고    scopus 로고
    • Impact of variable domain glycosylation on antibody clearance: an LC/MS characterization
    • Huang L., Biolsi S., Bales K.R., Kuchibhotla U. Impact of variable domain glycosylation on antibody clearance: an LC/MS characterization. Anal. Biochem. 2006, 349:197-207.
    • (2006) Anal. Biochem. , vol.349 , pp. 197-207
    • Huang, L.1    Biolsi, S.2    Bales, K.R.3    Kuchibhotla, U.4
  • 13
    • 79952202624 scopus 로고    scopus 로고
    • Maximizing productivity of CHO cell-based fed-batch culture using chemically defined media conditions and typical manufacturing equipment
    • Huang Y.M., Hu W., Rustandi E., Chang K., Yusuf-Makagiansar H., Ryll T. Maximizing productivity of CHO cell-based fed-batch culture using chemically defined media conditions and typical manufacturing equipment. Biotechnol. Prog. 2010, 26:1400-1410.
    • (2010) Biotechnol. Prog. , vol.26 , pp. 1400-1410
    • Huang, Y.M.1    Hu, W.2    Rustandi, E.3    Chang, K.4    Yusuf-Makagiansar, H.5    Ryll, T.6
  • 14
    • 71549150895 scopus 로고    scopus 로고
    • Baculovirus-insect cell expression systems
    • Jarvis D.L. Baculovirus-insect cell expression systems. Methods Enzymol. 2009, 463:191-222.
    • (2009) Methods Enzymol. , vol.463 , pp. 191-222
    • Jarvis, D.L.1
  • 15
    • 0032190659 scopus 로고    scopus 로고
    • Engineering N-glycosylation pathways in the baculovirus-insect cell system
    • Jarvis D.L., Kawar Z.S., Hollister J.R. Engineering N-glycosylation pathways in the baculovirus-insect cell system. Curr. Opin. Biotechnol. 1998, 9:528-533.
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 528-533
    • Jarvis, D.L.1    Kawar, Z.S.2    Hollister, J.R.3
  • 16
    • 67649394336 scopus 로고    scopus 로고
    • Recombinant antibody therapeutics: the impact of glycosylation on mechanisms of action
    • Jefferis R. Recombinant antibody therapeutics: the impact of glycosylation on mechanisms of action. Trends Pharmacol. Sci. 2009, 30:356-362.
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 356-362
    • Jefferis, R.1
  • 17
    • 0037013743 scopus 로고    scopus 로고
    • Interaction sites on human IgG-Fc for FcgammaR: current models
    • Jefferis R., Lund J. Interaction sites on human IgG-Fc for FcgammaR: current models. Immunol. Lett. 2002, 82:57-65.
    • (2002) Immunol. Lett. , vol.82 , pp. 57-65
    • Jefferis, R.1    Lund, J.2
  • 18
    • 33845590523 scopus 로고    scopus 로고
    • Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: the high-mannose, hybrid, and complex types
    • Kanda Y., Yamada T., Mori K., Okazaki A., Inoue M., Kitajima-Miyama K., Kuni-Kamochi R., Nakano R., Yano K., Kakita S., Shitara K., Satoh M. Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: the high-mannose, hybrid, and complex types. Glycobiology 2007, 17:104-118.
    • (2007) Glycobiology , vol.17 , pp. 104-118
    • Kanda, Y.1    Yamada, T.2    Mori, K.3    Okazaki, A.4    Inoue, M.5    Kitajima-Miyama, K.6    Kuni-Kamochi, R.7    Nakano, R.8    Yano, K.9    Kakita, S.10    Shitara, K.11    Satoh, M.12
  • 19
    • 77953655955 scopus 로고    scopus 로고
    • Industrialization of mAb production technology: the bioprocessing industry at a crossroads
    • Kelley B. Industrialization of mAb production technology: the bioprocessing industry at a crossroads. MAbs 2009, 1:443-452.
    • (2009) MAbs , vol.1 , pp. 443-452
    • Kelley, B.1
  • 20
    • 1842836023 scopus 로고    scopus 로고
    • Generation of recombinant antibodies
    • Kipriyanov S., Little M. Generation of recombinant antibodies. Mol. Biotechnol. 1999, 12:173-201.
    • (1999) Mol. Biotechnol. , vol.12 , pp. 173-201
    • Kipriyanov, S.1    Little, M.2
  • 22
    • 22844450442 scopus 로고    scopus 로고
    • Baculovirus as versatile vectors for protein expression in insect and mammalian cells
    • Kost T.A., Condreay J.P., Jarvis D.L. Baculovirus as versatile vectors for protein expression in insect and mammalian cells. Nat. Biotechnol. 2005, 23:567-575.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 567-575
    • Kost, T.A.1    Condreay, J.P.2    Jarvis, D.L.3
  • 24
    • 0027378859 scopus 로고
    • Baculovirus systems for the expression of human gene products
    • Luckow V.A. Baculovirus systems for the expression of human gene products. Curr. Opin. Biotechnol. 1993, 4:564-572.
    • (1993) Curr. Opin. Biotechnol. , vol.4 , pp. 564-572
    • Luckow, V.A.1
  • 25
    • 34147112902 scopus 로고    scopus 로고
    • Scalable transient gene expression in Chinese hamster ovary cells in instrumented and non-instrumented cultivation systems
    • Muller N., Derouazi M., Van Tilborgh F., Wulhfard S., Hacker D.L., Jordan M., Wurm F.M. Scalable transient gene expression in Chinese hamster ovary cells in instrumented and non-instrumented cultivation systems. Biotechnol. Lett. 2007, 29:703-711.
    • (2007) Biotechnol. Lett. , vol.29 , pp. 703-711
    • Muller, N.1    Derouazi, M.2    Van Tilborgh, F.3    Wulhfard, S.4    Hacker, D.L.5    Jordan, M.6    Wurm, F.M.7
  • 26
    • 33751322142 scopus 로고    scopus 로고
    • Compensation of endogenous IgG mediated inhibition of antibody-dependent cellular cytotoxicity by glyco-engineering of therapeutic antibodies
    • Nechansky A., Schuster M., Jost W., Siegl P., Wiederkum S., Gorr G., Kircheis R. Compensation of endogenous IgG mediated inhibition of antibody-dependent cellular cytotoxicity by glyco-engineering of therapeutic antibodies. Mol. Immunol. 2007, 44:1815-1817.
    • (2007) Mol. Immunol. , vol.44 , pp. 1815-1817
    • Nechansky, A.1    Schuster, M.2    Jost, W.3    Siegl, P.4    Wiederkum, S.5    Gorr, G.6    Kircheis, R.7
  • 28
    • 37149040344 scopus 로고    scopus 로고
    • Adaptation of the " in-gel release method" to N-glycome analysis of low-milligram amounts of material
    • Rendić D., Wilson I.B., Lubec G., Gutternigg M., Altmann F., Léonard R. Adaptation of the " in-gel release method" to N-glycome analysis of low-milligram amounts of material. Electrophoresis 2007, 28:4484-4492.
    • (2007) Electrophoresis , vol.28 , pp. 4484-4492
    • Rendić, D.1    Wilson, I.B.2    Lubec, G.3    Gutternigg, M.4    Altmann, F.5    Léonard, R.6
  • 29
    • 0004136246 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press, New York, USA
    • Sambrook J., Russel D.W. Molecular Cloning 2001, Cold Spring Harbor Laboratory Press, New York, USA. Third edition.
    • (2001) Molecular Cloning
    • Sambrook, J.1    Russel, D.W.2
  • 30
    • 33750835115 scopus 로고    scopus 로고
    • Non-fucosylated therapeutic antibodies as next-generation therapeutic antibodies
    • Satoh M., Iida S., Shitara K. Non-fucosylated therapeutic antibodies as next-generation therapeutic antibodies. Expert Opin. Biol. Ther. 2006, 6:1161-1173.
    • (2006) Expert Opin. Biol. Ther. , vol.6 , pp. 1161-1173
    • Satoh, M.1    Iida, S.2    Shitara, K.3
  • 31
    • 0037474276 scopus 로고    scopus 로고
    • The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity
    • Shinkawa T., Nakamura K., Yamane N., Shoji-Hosaka E., Kanda Y., Sakurada M., Uchida K., Anazawa H., Satoh M., Yamasaki M., Hanai N., Shitara K. The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. J. Biol. Chem. 2003, 278:3466-3473.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3466-3473
    • Shinkawa, T.1    Nakamura, K.2    Yamane, N.3    Shoji-Hosaka, E.4    Kanda, Y.5    Sakurada, M.6    Uchida, K.7    Anazawa, H.8    Satoh, M.9    Yamasaki, M.10    Hanai, N.11    Shitara, K.12
  • 34
    • 0001962451 scopus 로고
    • A manual of methods for baculovirus vectors and insect cell culture procedures
    • Summers M.D., Smith G.E. A manual of methods for baculovirus vectors and insect cell culture procedures. Texas Agric. Exp. Station Bull. 1987, 1555.
    • (1987) Texas Agric. Exp. Station Bull. , pp. 1555
    • Summers, M.D.1    Smith, G.E.2
  • 35
    • 0027338531 scopus 로고
    • Optimization of growth methods and recombinant protein production in BTI-Tn-5B1-4 insect cells using the baculovirus expression system
    • Wickham T.J., Nemerow G.R. Optimization of growth methods and recombinant protein production in BTI-Tn-5B1-4 insect cells using the baculovirus expression system. Biotechnol. Prog. 1993, 9:25-30.
    • (1993) Biotechnol. Prog. , vol.9 , pp. 25-30
    • Wickham, T.J.1    Nemerow, G.R.2


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