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Volumn 141, Issue 1-2, 2009, Pages 18-25

Production of chimeric monoclonal antibodies by genetically manipulated chickens

Author keywords

Chimeric monoclonal antibody; N linked oligosaccharide chain structure; Retroviral vector; Transgenic avian bioreactor

Indexed keywords

ANTIBODY PRODUCTIONS; ANTIGEN-BINDING ACTIVITIES; CHIMERIC ANTIBODIES; CHIMERIC MONOCLONAL ANTIBODY; EGG WHITES; HEAVY AND LIGHT CHAINS; N-LINKED OLIGOSACCHARIDE CHAIN STRUCTURE; RECOMBINANT ANTIBODIES; RETROVIRAL VECTOR; SEXUAL MATURATIONS; TRANSGENE; TRANSGENIC AVIAN BIOREACTOR;

EID: 64249173171     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2009.02.022     Document Type: Article
Times cited : (41)

References (44)
  • 1
    • 0037264969 scopus 로고    scopus 로고
    • Therapeutic antibodies for human diseases at the dawn of the twenty-first century
    • Brekke O.H., and Sandlie I. Therapeutic antibodies for human diseases at the dawn of the twenty-first century. Nat. Rev. Drug Discov. 2 (2003) 52-62
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 52-62
    • Brekke, O.H.1    Sandlie, I.2
  • 2
    • 0035313152 scopus 로고    scopus 로고
    • Therapeutic antibody expression technology
    • Chadd H.E., and Chamow S.M. Therapeutic antibody expression technology. Curr. Opin. Biotechnol. 12 (2001) 188-194
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 188-194
    • Chadd, H.E.1    Chamow, S.M.2
  • 3
    • 0041887181 scopus 로고    scopus 로고
    • Making recombinant proteins in animals-different systems, different applications
    • Dyck M.K., Lacroix D., Pothier F., and Sirard M.A. Making recombinant proteins in animals-different systems, different applications. Trends Biotechnol. 21 (2003) 394-399
    • (2003) Trends Biotechnol. , vol.21 , pp. 394-399
    • Dyck, M.K.1    Lacroix, D.2    Pothier, F.3    Sirard, M.A.4
  • 4
    • 0025997947 scopus 로고
    • The encephalomyocarditis virus internal ribosome entry site allows efficient coexpression of two genes from a recombinant provirus in cultured cells and in embryos
    • Ghattas I.R., Sanes J.R., and Majors J.E. The encephalomyocarditis virus internal ribosome entry site allows efficient coexpression of two genes from a recombinant provirus in cultured cells and in embryos. Mol. Cell. Biol. 11 (1991) 5848-5859
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5848-5859
    • Ghattas, I.R.1    Sanes, J.R.2    Majors, J.E.3
  • 5
    • 84924926133 scopus 로고
    • A series of normal stages in the development of the chick embryo
    • Hamburger V., and Hamilton H.L. A series of normal stages in the development of the chick embryo. J. Morphol. 88 (1951) 49-92
    • (1951) J. Morphol. , vol.88 , pp. 49-92
    • Hamburger, V.1    Hamilton, H.L.2
  • 7
    • 0028385758 scopus 로고
    • Versatile retroviral vectors for potential use in gene therapy
    • Hawley R.G., Lieu F.H.L., Fong A.Z.C., and Hawley T.S. Versatile retroviral vectors for potential use in gene therapy. Gene Ther. 1 (1994) 136-138
    • (1994) Gene Ther. , vol.1 , pp. 136-138
    • Hawley, R.G.1    Lieu, F.H.L.2    Fong, A.Z.C.3    Hawley, T.S.4
  • 9
    • 0037212233 scopus 로고    scopus 로고
    • Avian transgenesis: progress towards the promise
    • Ivarie R. Avian transgenesis: progress towards the promise. Trends Biotechnol. 21 (2003) 14-19
    • (2003) Trends Biotechnol. , vol.21 , pp. 14-19
    • Ivarie, R.1
  • 10
    • 23844504527 scopus 로고    scopus 로고
    • High-level expression of single-chain Fv-Fc fusion protein in serum and egg white of genetically manipulated chickens by using a retroviral vector
    • Kamihira M., Ono K., Esaka K., Nishijima K., Kigaku R., Komatsu H., Yamashita T., Kyogoku K., and Iijima S. High-level expression of single-chain Fv-Fc fusion protein in serum and egg white of genetically manipulated chickens by using a retroviral vector. J. Virol. 79 (2005) 10864-10874
    • (2005) J. Virol. , vol.79 , pp. 10864-10874
    • Kamihira, M.1    Ono, K.2    Esaka, K.3    Nishijima, K.4    Kigaku, R.5    Komatsu, H.6    Yamashita, T.7    Kyogoku, K.8    Iijima, S.9
  • 13
    • 1842836023 scopus 로고    scopus 로고
    • Generation of recombinant antibodies
    • Kipriyanov S.M., and Little M. Generation of recombinant antibodies. Mol. Biotechnol. 12 (1999) 173-201
    • (1999) Mol. Biotechnol. , vol.12 , pp. 173-201
    • Kipriyanov, S.M.1    Little, M.2
  • 15
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Köhler G., and Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256 (1975) 495-497
    • (1975) Nature , vol.256 , pp. 495-497
    • Köhler, G.1    Milstein, C.2
  • 16
    • 0019188771 scopus 로고
    • Immunoglobulin chain loss in hybridoma lines
    • Köhler G. Immunoglobulin chain loss in hybridoma lines. Proc. Natl. Acad. Sci. U.S.A. 77 (1980) 2197-2199
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 2197-2199
    • Köhler, G.1
  • 22
    • 0031835622 scopus 로고    scopus 로고
    • Characterization of a recombinant plant monoclonal secretory antibody and preventive immunotherapy in humans
    • Ma J.K., Hikmat B.Y., Wycoff K., Vine N.D., Chargelegue D., Yu L., Hein M.B., and Lehner T. Characterization of a recombinant plant monoclonal secretory antibody and preventive immunotherapy in humans. Nat. Med. 4 (1998) 601-606
    • (1998) Nat. Med. , vol.4 , pp. 601-606
    • Ma, J.K.1    Hikmat, B.Y.2    Wycoff, K.3    Vine, N.D.4    Chargelegue, D.5    Yu, L.6    Hein, M.B.7    Lehner, T.8
  • 24
    • 0034815057 scopus 로고    scopus 로고
    • Production of transgenic quails with high frequency of germ-line transmission using VSV-G pseudotyped retroviral vector
    • Mizuarai S., Ono K., Yamaguchi K., Nishijima K., Kamihira M., and Iijima S. Production of transgenic quails with high frequency of germ-line transmission using VSV-G pseudotyped retroviral vector. Biochem. Biophys. Res. Commun. 286 (2001) 456-463
    • (2001) Biochem. Biophys. Res. Commun. , vol.286 , pp. 456-463
    • Mizuarai, S.1    Ono, K.2    Yamaguchi, K.3    Nishijima, K.4    Kamihira, M.5    Iijima, S.6
  • 25
    • 0034170820 scopus 로고    scopus 로고
    • IRES-dependent second gene expression is significantly lower than cap-dependent first gene expression in a bicistronic vector
    • Mizuguchi H., Xu Z., Ishii-Watabe A., Uchida E., and Hayakawa T. IRES-dependent second gene expression is significantly lower than cap-dependent first gene expression in a bicistronic vector. Mol. Ther. 1 (2000) 376-382
    • (2000) Mol. Ther. , vol.1 , pp. 376-382
    • Mizuguchi, H.1    Xu, Z.2    Ishii-Watabe, A.3    Uchida, E.4    Hayakawa, T.5
  • 27
    • 0037370171 scopus 로고    scopus 로고
    • Development of transgenic chickens expressing bacterial β-galactosidase
    • Mozdziak P.E., Borwornpinyo S., McCoy D.W., and Petitte J.N. Development of transgenic chickens expressing bacterial β-galactosidase. Dev. Dyn. 226 (2003) 439-445
    • (2003) Dev. Dyn. , vol.226 , pp. 439-445
    • Mozdziak, P.E.1    Borwornpinyo, S.2    McCoy, D.W.3    Petitte, J.N.4
  • 28
    • 0034041010 scopus 로고    scopus 로고
    • Construction of recombinant monoclonal antibodies from a chicken hybridoma line secreting specific antibody
    • Nakamura N., Aoki Y., Horiuchi H., Furusawa S., Yamanaka H.I., Kitamoto T., and Matsuda H. Construction of recombinant monoclonal antibodies from a chicken hybridoma line secreting specific antibody. Cytotechnology 32 (2000) 191-198
    • (2000) Cytotechnology , vol.32 , pp. 191-198
    • Nakamura, N.1    Aoki, Y.2    Horiuchi, H.3    Furusawa, S.4    Yamanaka, H.I.5    Kitamoto, T.6    Matsuda, H.7
  • 31
    • 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.B., Borge S.M., and 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 (2000) 477-486
    • (2000) Glycobiology , vol.10 , pp. 477-486
    • Raju, T.S.1    Briggs, J.B.2    Borge, S.M.3    Jones, A.J.S.4
  • 32
    • 0142135386 scopus 로고    scopus 로고
    • Biologically active human interferon alpha-2b produced in the egg white of transgenic hens
    • Rapp J.C., Harvey A.J., Speksnijder G.L., Hu W., and Ivarie R. Biologically active human interferon alpha-2b produced in the egg white of transgenic hens. Transgenic Res. 12 (2003) 569-575
    • (2003) Transgenic Res. , vol.12 , pp. 569-575
    • Rapp, J.C.1    Harvey, A.J.2    Speksnijder, G.L.3    Hu, W.4    Ivarie, R.5
  • 33
    • 34247876138 scopus 로고    scopus 로고
    • Development trends for monoclonal antibody cancer therapeutics
    • Reichert J.M., and Valge-Archer V.E. Development trends for monoclonal antibody cancer therapeutics. Nat. Rev. Drug Discov. 6 (2007) 349-356
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 349-356
    • Reichert, J.M.1    Valge-Archer, V.E.2
  • 34
    • 2942722679 scopus 로고    scopus 로고
    • Antibodies and genetically engineered related molecules: production and purification
    • Roque A.C., Lowe C.R., and Taipa M.A. Antibodies and genetically engineered related molecules: production and purification. Biotechnol. Prog. 20 (2004) 639-654
    • (2004) Biotechnol. Prog. , vol.20 , pp. 639-654
    • Roque, A.C.1    Lowe, C.R.2    Taipa, M.A.3
  • 35
    • 0033198283 scopus 로고    scopus 로고
    • Biopharmaceutical production in transgenic livestock
    • Rudolph N.S. Biopharmaceutical production in transgenic livestock. Trends Biotechnol. 17 (1999) 367-374
    • (1999) Trends Biotechnol. , vol.17 , pp. 367-374
    • Rudolph, N.S.1
  • 36
    • 3543055751 scopus 로고    scopus 로고
    • Prospects for transgenesis in the chick
    • Sang H. Prospects for transgenesis in the chick. Mech. Dev. 121 (2004) 1179-1186
    • (2004) Mech. Dev. , vol.121 , pp. 1179-1186
    • Sang, H.1
  • 37
    • 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 M., and 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. 278 (2003) 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, M.11    Shitara, K.12
  • 38
    • 0023092177 scopus 로고
    • Comparative structural study of the N-linked oligosaccharides of human normal and pathological immunoglobulin G
    • Takahashi N., Ishii I., Ishihara H., Mori M., Tejima S., Jefferis R., Endo S., and Arata Y. Comparative structural study of the N-linked oligosaccharides of human normal and pathological immunoglobulin G. Biochemistry 26 (1987) 1137-1144
    • (1987) Biochemistry , vol.26 , pp. 1137-1144
    • Takahashi, N.1    Ishii, I.2    Ishihara, H.3    Mori, M.4    Tejima, S.5    Jefferis, R.6    Endo, S.7    Arata, Y.8
  • 39
    • 0028957151 scopus 로고
    • Three-dimensional elution mapping of pyridylaminated N-linked neutral and sialyl oligosaccharides
    • Takahashi N., Nakagawa H., Fujikawa K., Kawamura Y., and Tomiya N. Three-dimensional elution mapping of pyridylaminated N-linked neutral and sialyl oligosaccharides. Anal. Biochem. 226 (1995) 139-146
    • (1995) Anal. Biochem. , vol.226 , pp. 139-146
    • Takahashi, N.1    Nakagawa, H.2    Fujikawa, K.3    Kawamura, Y.4    Tomiya, N.5
  • 41
    • 1642291044 scopus 로고    scopus 로고
    • Transgenic livestock made easy
    • Whitelaw C.B. Transgenic livestock made easy. Trends Biotechnol. 22 (2004) 157-159
    • (2004) Trends Biotechnol. , vol.22 , pp. 157-159
    • Whitelaw, C.B.1
  • 42
    • 8344271026 scopus 로고    scopus 로고
    • Production of recombinant protein therapeutics in cultivated mammalian cells
    • Wurm F.M. Production of recombinant protein therapeutics in cultivated mammalian cells. Nat. Biotechnol. 22 (2004) 1393-1398
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1393-1398
    • Wurm, F.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.