메뉴 건너뛰기




Volumn 107, Issue 2, 2009, Pages 165-172

Change in glycosylation pattern with extension of endoplasmic reticulum retention signal sequence of mouse antibody produced by suspension-cultured tobacco BY2 cells

Author keywords

Antibody; Endoplasmic reticulum (ER); Glycosylation; KDEL; Tobacco

Indexed keywords

ENDOPLASMIC RETICULUM (ER); FUCOSYLATION; GLYCAN STRUCTURES; GLYCANS; KDEL; RECOMBINANT PROTEINS; RETRIEVAL SYSTEMS; SIGNAL SEQUENCES; SUGAR CHAIN STRUCTURES; SUGAR CHAINS; SUSPENSION-CULTURED; TOBACCO BY-2 CELLS; TRANSGENIC PLANTS; TYPE STRUCTURES; XYLOSYLATION;

EID: 60949091047     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2008.09.016     Document Type: Article
Times cited : (14)

References (36)
  • 1
    • 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., and 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 (1998) 101-109
    • (1998) Plant Mol. Biol. , vol.38 , pp. 101-109
    • Conrad, U.1    Fiedler, U.2
  • 2
    • 2442590941 scopus 로고    scopus 로고
    • Plant molecular farming: systems and products
    • Horn M.E., Woodard S.L., and Howard J.A. Plant molecular farming: systems and products. Plant Cell Rep. 22 (2004) 711-720
    • (2004) Plant Cell Rep. , vol.22 , pp. 711-720
    • Horn, M.E.1    Woodard, S.L.2    Howard, J.A.3
  • 4
    • 33745685217 scopus 로고    scopus 로고
    • N-Linked glycan structures of a mouse monoclonal antibody produced from tobacco BY2 suspension-cultured cells
    • Fujiyama K., Misaki R., Katsura A., Tanaka T., Furukawa A., Omasa T., and Seki T. N-Linked glycan structures of a mouse monoclonal antibody produced from tobacco BY2 suspension-cultured cells. J. Biosci. Bioeng. 101 (2006) 212-218
    • (2006) J. Biosci. Bioeng. , vol.101 , pp. 212-218
    • Fujiyama, K.1    Misaki, R.2    Katsura, A.3    Tanaka, T.4    Furukawa, A.5    Omasa, T.6    Seki, T.7
  • 5
    • 0034570433 scopus 로고    scopus 로고
    • N-glycosylation of recombinant pharmaceutical glycoproteins produced in transgenic plants: towards an humanisation of plant N-glycans
    • Lerouge P., Bardor M., Pagny S., Gomord V., and Faye L. N-glycosylation of recombinant pharmaceutical glycoproteins produced in transgenic plants: towards an humanisation of plant N-glycans. Curr. Pharm. Biotechnol. 1 (2000) 347-354
    • (2000) Curr. Pharm. Biotechnol. , vol.1 , pp. 347-354
    • Lerouge, P.1    Bardor, M.2    Pagny, S.3    Gomord, V.4    Faye, L.5
  • 6
    • 26944477789 scopus 로고    scopus 로고
    • Biopharmaceutical production in plants: problems, solutions and opportunities
    • Gomord V., Chamberlain P., Jefferis R., and Faye L. Biopharmaceutical production in plants: problems, solutions and opportunities. Trends Biotechnol. 23 (2005) 559-565
    • (2005) Trends Biotechnol. , vol.23 , pp. 559-565
    • Gomord, V.1    Chamberlain, P.2    Jefferis, R.3    Faye, L.4
  • 7
    • 0034958453 scopus 로고    scopus 로고
    • Analysis of Asn-linked glycans from vegetable foodstuffs: widespread occurrence of Lewis a, core alpha1,3-linked fucose and xylose substitutions
    • Wilson I.B., Zeleny R., Kolarich D., Staudacher E., Stroop C.J., Kamerling J.P., and Altmann F. Analysis of Asn-linked glycans from vegetable foodstuffs: widespread occurrence of Lewis a, core alpha1,3-linked fucose and xylose substitutions. Glycobiology 11 (2001) 261-274
    • (2001) Glycobiology , vol.11 , pp. 261-274
    • Wilson, I.B.1    Zeleny, R.2    Kolarich, D.3    Staudacher, E.4    Stroop, C.J.5    Kamerling, J.P.6    Altmann, F.7
  • 8
    • 2942606516 scopus 로고    scopus 로고
    • Specificity of IgG and IgE antibodies against plant and insect glycoprotein glycans determined with artificial glycoforms of human transferrin
    • Bencurova M., Hemmer W., Focke-Tejkl M., Wilson I.B., and Altmann F. Specificity of IgG and IgE antibodies against plant and insect glycoprotein glycans determined with artificial glycoforms of human transferrin. Glycobiology 14 (2004) 457-466
    • (2004) Glycobiology , vol.14 , pp. 457-466
    • Bencurova, M.1    Hemmer, W.2    Focke-Tejkl, M.3    Wilson, I.B.4    Altmann, F.5
  • 10
    • 33645109820 scopus 로고    scopus 로고
    • Immunoglobulin G specifically binding plant N-glycans with high affinity could be generated in rabbits but not in mice
    • Jin C., Bencúrová M., Borth N., Ferko B., Jensen-Jarolin E., Altmann F., and Hantusch B. Immunoglobulin G specifically binding plant N-glycans with high affinity could be generated in rabbits but not in mice. Glycobiology 16 (2006) 349-357
    • (2006) Glycobiology , vol.16 , pp. 349-357
    • Jin, C.1    Bencúrová, M.2    Borth, N.3    Ferko, B.4    Jensen-Jarolin, E.5    Altmann, F.6    Hantusch, B.7
  • 11
    • 0028830782 scopus 로고
    • Oligosaccharide-protein interactions in IgG can modulate recognition by Fc receptors
    • Lund J., Takahashi N., Pound J.D., Goodall M., Nakagawa H., and Jefferis R. Oligosaccharide-protein interactions in IgG can modulate recognition by Fc receptors. FASEB J. 9 (1995) 115-119
    • (1995) FASEB J. , vol.9 , pp. 115-119
    • Lund, J.1    Takahashi, N.2    Pound, J.D.3    Goodall, M.4    Nakagawa, H.5    Jefferis, R.6
  • 15
    • 2142707181 scopus 로고    scopus 로고
    • Transgenic tobacco cells producing the human monoclonal antibody to hepatitis B virus surface antigen
    • Yano A., Maeda F., and Takekoshi M. Transgenic tobacco cells producing the human monoclonal antibody to hepatitis B virus surface antigen. J. Med. Virol. 73 (2004) 208-215
    • (2004) J. Med. Virol. , vol.73 , pp. 208-215
    • Yano, A.1    Maeda, F.2    Takekoshi, M.3
  • 19
    • 0347478147 scopus 로고    scopus 로고
    • Expression and characterization of an anti-(hepatitis B surface antigen) glycosylated mouse antibody in transgenic tobacco (Nicotiana tabacum) plants and its use in the immunopurification of its target antigen
    • Ramirez N., Rodriguez M., Ayala M., Cremata J., Perez M., Martinez A., Linares M., Hevia Y., Paez R., Valdes R., Gavilondo J.V., and Selman-Housein G. Expression and characterization of an anti-(hepatitis B surface antigen) glycosylated mouse antibody in transgenic tobacco (Nicotiana tabacum) plants and its use in the immunopurification of its target antigen. Biotechnol. Appl. Biochem. 38 (2003) 223-230
    • (2003) Biotechnol. Appl. Biochem. , vol.38 , pp. 223-230
    • Ramirez, N.1    Rodriguez, M.2    Ayala, M.3    Cremata, J.4    Perez, M.5    Martinez, A.6    Linares, M.7    Hevia, Y.8    Paez, R.9    Valdes, R.10    Gavilondo, J.V.11    Selman-Housein, G.12
  • 20
    • 33646842291 scopus 로고    scopus 로고
    • Plant-derived mouse IgG monoclonal antibody fused to KDEL endoplasmic reticulum-retention signal is N-glycosylated homogeneously throughout the plant with mostly high-mannose-type N-glycans
    • Triguero A., Cabrera G., Cremata J.A., Yuen C.T., Wheeler J., and Ramírez N.I. Plant-derived mouse IgG monoclonal antibody fused to KDEL endoplasmic reticulum-retention signal is N-glycosylated homogeneously throughout the plant with mostly high-mannose-type N-glycans. Plant Biotechnol. J. 3 (2005) 449-457
    • (2005) Plant Biotechnol. J. , vol.3 , pp. 449-457
    • Triguero, A.1    Cabrera, G.2    Cremata, J.A.3    Yuen, C.T.4    Wheeler, J.5    Ramírez, N.I.6
  • 21
    • 5644303930 scopus 로고    scopus 로고
    • Recombinant anti-hCG antibodies retained in the endoplasmic reticulum of transformed plants lack core-xylose and core-α(1,3)-fucose residues
    • Sriraman R., Bardor M., Sack M., Vaquero C., Faye L., Fischer R., Finnern R., and Lerouge P. Recombinant anti-hCG antibodies retained in the endoplasmic reticulum of transformed plants lack core-xylose and core-α(1,3)-fucose residues. Plant Biotechnol. J. 2 (2004) 279-287
    • (2004) Plant Biotechnol. J. , vol.2 , pp. 279-287
    • Sriraman, R.1    Bardor, M.2    Sack, M.3    Vaquero, C.4    Faye, L.5    Fischer, R.6    Finnern, R.7    Lerouge, P.8
  • 22
    • 0027014897 scopus 로고
    • New plant binary vectors with selectable markers located proximal to the left T-DNA border
    • Becker D., Kemper E., Schell J., and Masterson R. New plant binary vectors with selectable markers located proximal to the left T-DNA border. Plant Mol. Biol. 20 (1992) 1195-1197
    • (1992) Plant Mol. Biol. , vol.20 , pp. 1195-1197
    • Becker, D.1    Kemper, E.2    Schell, J.3    Masterson, R.4
  • 24
    • 0029139008 scopus 로고
    • Analysis of conditions for Agrobacterium-mediated transformation of tobacco cells in suspension
    • Rempel H.C., and Nelson L.M. Analysis of conditions for Agrobacterium-mediated transformation of tobacco cells in suspension. Transgenic Res. 4 (1995) 199-207
    • (1995) Transgenic Res. , vol.4 , pp. 199-207
    • Rempel, H.C.1    Nelson, L.M.2
  • 26
    • 0025477749 scopus 로고
    • Improved method for fluorescence labeling of sugar chains with sialic acid residues
    • Kondo A., Suzuki J., Kuraya N., Hase S., Kato I., and Ikenaka T. Improved method for fluorescence labeling of sugar chains with sialic acid residues. Agric. Biol. Chem. 54 (1990) 2169-2170
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 2169-2170
    • Kondo, A.1    Suzuki, J.2    Kuraya, N.3    Hase, S.4    Kato, I.5    Ikenaka, T.6
  • 27
    • 0042878233 scopus 로고    scopus 로고
    • Characterization of almond α-mannosidase and its application for structure analysis of sugar chain
    • Misaki R., Fujiyama K., Yokoyama H., Ido Y., Miyauchi K., Yoshida T., and Seki T. Characterization of almond α-mannosidase and its application for structure analysis of sugar chain. J. Biosci. Bioeng. 96 (2003) 187-192
    • (2003) J. Biosci. Bioeng. , vol.96 , pp. 187-192
    • Misaki, R.1    Fujiyama, K.2    Yokoyama, H.3    Ido, Y.4    Miyauchi, K.5    Yoshida, T.6    Seki, T.7
  • 29
    • 0025797046 scopus 로고
    • The structure of a neural specific carbohydrate epitope of horseradish peroxidase recognized by anti-horseradish peroxidase antiserum
    • Kurosaka A., Yano A., Itoh N., Kuroda Y., Nakagawa T., and Kawasaki T. The structure of a neural specific carbohydrate epitope of horseradish peroxidase recognized by anti-horseradish peroxidase antiserum. J. Biol. Chem. 266 (1991) 4168-4172
    • (1991) J. Biol. Chem. , vol.266 , pp. 4168-4172
    • Kurosaka, A.1    Yano, A.2    Itoh, N.3    Kuroda, Y.4    Nakagawa, T.5    Kawasaki, T.6
  • 30
    • 0032602265 scopus 로고    scopus 로고
    • Structures of N-linked oligosaccharides of glycoproteins from tobacco BY2 suspension cultured cells
    • Palacpac N.Q., Kimura Y., Fujiyama K., Yoshida T., and Seki T. Structures of N-linked oligosaccharides of glycoproteins from tobacco BY2 suspension cultured cells. Biosci. Biotechnol. Biochem. 63 (1999) 35-39
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 35-39
    • Palacpac, N.Q.1    Kimura, Y.2    Fujiyama, K.3    Yoshida, T.4    Seki, T.5
  • 32
    • 33747116052 scopus 로고    scopus 로고
    • Mannan binding lectin and its interaction with immunoglobulins in health and in disease
    • Arnold J.N., Dwek R.A., Rudd P.M., and Sim R.B. Mannan binding lectin and its interaction with immunoglobulins in health and in disease. Immunol. Lett. 106 (2006) 103-110
    • (2006) Immunol. Lett. , vol.106 , pp. 103-110
    • Arnold, J.N.1    Dwek, R.A.2    Rudd, P.M.3    Sim, R.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.