메뉴 건너뛰기




Volumn 7, Issue 4, 2012, Pages

Sweetbac: A new approach for the production of mammalianised glycoproteins in insect cells

Author keywords

[No Author keywords available]

Indexed keywords

3D6 ANTIBODY; AGGLUTININ; BETA 1,4 GALACTOSYLTRANSFERASE 1; GALACTOSE; GALACTOSYLTRANSFERASE; GLYCOPROTEIN; GLYCOPROTEIN GP 41; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; N ACETYLGLUCOSAMINYLTRANSFERASE; UNCLASSIFIED DRUG; BETA 1,3 GALACTOSYL 0 GLYCOSYL GLYCOPROTEIN BETA 1,3 N ACETYLGLUCOSAMINYLTRANSFERASE; BETA-1,3-GALACTOSYL-0-GLYCOSYL-GLYCOPROTEIN BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE; CAENORHABDITIS ELEGANS PROTEIN; FC RECEPTOR; RECOMBINANT PROTEIN;

EID: 84859237513     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0034226     Document Type: Article
Times cited : (80)

References (32)
  • 1
    • 49749105995 scopus 로고    scopus 로고
    • An update of prophylactic human papillomavirus L1 virus-like particle vaccine clinical trial results
    • Schiller JT, Castellsagué X, Villa LL, Hildesheim A, (2008) An update of prophylactic human papillomavirus L1 virus-like particle vaccine clinical trial results. Vaccine 26 (Suppl 10): K53-61.
    • (2008) Vaccine , vol.26 , Issue.SUPPL. 10
    • Schiller, J.T.1    Castellsagué, X.2    Villa, L.L.3    Hildesheim, A.4
  • 3
    • 0017475358 scopus 로고
    • The establishment of two cell lines from the insect Spodoptera frugiperda (Lepidoptera; Noctuidae)
    • Vaughn JL, Goodwin RH, Tompkins GJ, McCawley P, (1977) The establishment of two cell lines from the insect Spodoptera frugiperda (Lepidoptera; Noctuidae). In Vitro 13: 213-217.
    • (1977) In Vitro , vol.13 , pp. 213-217
    • Vaughn, J.L.1    Goodwin, R.H.2    Tompkins, G.J.3    McCawley, P.4
  • 4
    • 0027338531 scopus 로고
    • Optimization of growth methods and recombinant protein production in BTI-Tn-5B1-4 insect cells using the baculovirus expression system
    • Wickham TJ, Nemerow GR, (1993) Optimization of growth methods and recombinant protein production in BTI-Tn-5B1-4 insect cells using the baculovirus expression system. Biotechnol Prog 9: 25-30.
    • (1993) Biotechnol Prog , vol.9 , pp. 25-30
    • Wickham, T.J.1    Nemerow, G.R.2
  • 5
    • 77954146431 scopus 로고    scopus 로고
    • Ao38, a new cell line from eggs of the black witch moth, Ascalapha odorata (Lepidoptera: Noctuidae), is permissive for AcMNPV infection and produces high levels of recombinant proteins
    • Hashimoto Y, Zhang S, Blissard GW, (2010) Ao38, a new cell line from eggs of the black witch moth, Ascalapha odorata (Lepidoptera: Noctuidae), is permissive for AcMNPV infection and produces high levels of recombinant proteins. BMC Biotechnol 10: 50.
    • (2010) BMC Biotechnol , vol.10 , pp. 50
    • Hashimoto, Y.1    Zhang, S.2    Blissard, G.W.3
  • 6
    • 0032848027 scopus 로고    scopus 로고
    • Insect cells as hosts for the expression of recombinant glycoproteins
    • Altmann F, Staudacher E, Wilson IBH, März L, (1999) Insect cells as hosts for the expression of recombinant glycoproteins. Glycoconj J 16: 109-123.
    • (1999) Glycoconj J , vol.16 , pp. 109-123
    • Altmann, F.1    Staudacher, E.2    Wilson, I.B.H.3    März, L.4
  • 7
    • 0029933189 scopus 로고    scopus 로고
    • Elongation of the N-glycans of fowl plague virus hemagglutinin expressed in Spodoptera frugiperda (Sf9) cells by coexpression of human β1,2-N-acetylglucosaminyltransferase I
    • Wagner R, Liedtke S, Kretzschmar E, Geyer H, Geyer R, et al. (1996) Elongation of the N-glycans of fowl plague virus hemagglutinin expressed in Spodoptera frugiperda (Sf9) cells by coexpression of human β1,2-N-acetylglucosaminyltransferase I. Glycobiology 6: 165-175.
    • (1996) Glycobiology , vol.6 , pp. 165-175
    • Wagner, R.1    Liedtke, S.2    Kretzschmar, E.3    Geyer, H.4    Geyer, R.5
  • 8
    • 0029769504 scopus 로고    scopus 로고
    • Modifying the insect cell N-glycosylation pathway with immediate early baculovirus expression vectors
    • Jarvis DL, Finn EE, (1996) Modifying the insect cell N-glycosylation pathway with immediate early baculovirus expression vectors. Nat Biotechnol 14: 1288-1292.
    • (1996) Nat Biotechnol , vol.14 , pp. 1288-1292
    • Jarvis, D.L.1    Finn, E.E.2
  • 9
    • 0031775473 scopus 로고    scopus 로고
    • Stable expression of mammalian β1,4-galactosyltransferase extends the N-glycosylation pathway in insect cells
    • Hollister JR, Shaper JH, Jarvis DL, (1998) Stable expression of mammalian β1,4-galactosyltransferase extends the N-glycosylation pathway in insect cells. Glycobiology 8: 473-480.
    • (1998) Glycobiology , vol.8 , pp. 473-480
    • Hollister, J.R.1    Shaper, J.H.2    Jarvis, D.L.3
  • 10
    • 0035817416 scopus 로고    scopus 로고
    • Improved glycosylation of a foreign protein by Tn-5B1-4 cells engineered to express mammalian glycosyltransferases
    • Breitbach K, Jarvis DL, (2001) Improved glycosylation of a foreign protein by Tn-5B1-4 cells engineered to express mammalian glycosyltransferases. Biotechnol Bioeng 74: 230-239.
    • (2001) Biotechnol Bioeng , vol.74 , pp. 230-239
    • Breitbach, K.1    Jarvis, D.L.2
  • 11
    • 0035093068 scopus 로고    scopus 로고
    • Engineering lepidopteran insect cells for sialoglycoprotein production by genetic transformation with mammalian β1,4-galactosyltransferase and α2,6-sialyltransferase genes
    • Hollister JR, Jarvis DL, (2001) Engineering lepidopteran insect cells for sialoglycoprotein production by genetic transformation with mammalian β1,4-galactosyltransferase and α2,6-sialyltransferase genes. Glycobiology 11: 1-9.
    • (2001) Glycobiology , vol.11 , pp. 1-9
    • Hollister, J.R.1    Jarvis, D.L.2
  • 12
    • 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 DL, (2002) Engineering the protein N-glycosylation pathway in insect cells for production of biantennary, complex N-glycans. Biochemistry 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
  • 13
    • 0038243176 scopus 로고    scopus 로고
    • A transgenic insect cell line engineered to produce CMP-sialic acid and sialylated glycoproteins
    • Aumiller J, Hollister J, Jarvis D, (2003) A transgenic insect cell line engineered to produce CMP-sialic acid and sialylated glycoproteins. Glycobiology 13: 497-507.
    • (2003) Glycobiology , vol.13 , pp. 497-507
    • Aumiller, J.1    Hollister, J.2    Jarvis, D.3
  • 14
    • 84856298339 scopus 로고    scopus 로고
    • A new glycoengineered insect cell line with an inducibly-mammalianized protein N-glycosylation pathway
    • Aumiller JJ, Mabashi-Asazuma H, Hillar A, Shi X, Jarvis DL, (2012) A new glycoengineered insect cell line with an inducibly-mammalianized protein N-glycosylation pathway. Glycobiology.
    • (2012) Glycobiology
    • Aumiller, J.J.1    Mabashi-Asazuma, H.2    Hillar, A.3    Shi, X.4    Jarvis, D.L.5
  • 15
    • 77954951040 scopus 로고    scopus 로고
    • Trichoplusia ni cells (High Five) are highly efficient for the production of influenza A virus-like particles: a comparison of two insect cell lines as production platforms for influenza vaccines
    • Krammer F, Schinko T, Palmberger D, Tauer C, Messner P, et al. (2010) Trichoplusia ni cells (High Five) are highly efficient for the production of influenza A virus-like particles: a comparison of two insect cell lines as production platforms for influenza vaccines. Mol Biotechnol 45: 226-234.
    • (2010) Mol Biotechnol , vol.45 , pp. 226-234
    • Krammer, F.1    Schinko, T.2    Palmberger, D.3    Tauer, C.4    Messner, P.5
  • 17
    • 11144340226 scopus 로고    scopus 로고
    • Baculovirus expression system for heterologous multiprotein complexes
    • Berger I, Fitzgerald DJ, Richmond TJ, (2004) Baculovirus expression system for heterologous multiprotein complexes. Nat Biotechnol 22: 1583-1587.
    • (2004) Nat Biotechnol , vol.22 , pp. 1583-1587
    • Berger, I.1    Fitzgerald, D.J.2    Richmond, T.J.3
  • 19
    • 75749152978 scopus 로고    scopus 로고
    • MultiBac: multigene baculovirus-based eukaryotic protein complex production
    • Unit 5.20
    • Bieniossek C, Richmond TJ, Berger I, (2008) MultiBac: multigene baculovirus-based eukaryotic protein complex production. Curr Protoc Protein Sci Chapter 5: Unit 5.20.
    • (2008) Curr Protoc Protein Sci Chapter , vol.5
    • Bieniossek, C.1    Richmond, T.J.2    Berger, I.3
  • 20
    • 77955962894 scopus 로고    scopus 로고
    • New baculovirus expression tools for recombinant protein complex production
    • Trowitzsch S, Bieniossek C, Nie Y, Garzoni F, Berger I, (2010) New baculovirus expression tools for recombinant protein complex production. J Struct Biol 172: 45-54.
    • (2010) J Struct Biol , vol.172 , pp. 45-54
    • Trowitzsch, S.1    Bieniossek, C.2    Nie, Y.3    Garzoni, F.4    Berger, I.5
  • 22
    • 0025160356 scopus 로고
    • Nucleotide sequences of the cDNAs encoding the V-regions of H- and L-chains of a human monoclonal antibody specific to HIV-1-gp41
    • Felgenhauer M, Kohl J, Rüker F, (1990) Nucleotide sequences of the cDNAs encoding the V-regions of H- and L-chains of a human monoclonal antibody specific to HIV-1-gp41. Nucleic Acids Res 18: 4927.
    • (1990) Nucleic Acids Res , vol.18 , pp. 4927
    • Felgenhauer, M.1    Kohl, J.2    Rüker, F.3
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 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 IBH, Lubec G, Gutternigg M, Altmann F, et al. (2007) Adaptation of the "in-gel release method" to N-glycome analysis of low-milligram amounts of material. Electrophoresis 28: 4484-4492.
    • (2007) Electrophoresis , vol.28 , pp. 4484-4492
    • Rendić, D.1    Wilson, I.B.H.2    Lubec, G.3    Gutternigg, M.4    Altmann, F.5
  • 25
    • 59749086716 scopus 로고    scopus 로고
    • Specificity analysis of lectins and antibodies using remodeled glycoproteins
    • Iskratsch T, Braun A, Paschinger K, Wilson IBH, (2009) Specificity analysis of lectins and antibodies using remodeled glycoproteins. Anal Biochem 386: 133-146.
    • (2009) Anal Biochem , vol.386 , pp. 133-146
    • Iskratsch, T.1    Braun, A.2    Paschinger, K.3    Wilson, I.B.H.4
  • 26
    • 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, et al. (2007) Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: the high-mannose, hybrid, and complex types. Glycobiology 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
  • 27
    • 31844447560 scopus 로고    scopus 로고
    • Impact of variable domain glycosylation on antibody clearance: an LC/MS characterization
    • Huang L, Biolsi S, Bales KR, Kuchibhotla U, (2006) Impact of variable domain glycosylation on antibody clearance: an LC/MS characterization. Anal Biochem 349: 197-207.
    • (2006) Anal Biochem , vol.349 , pp. 197-207
    • Huang, L.1    Biolsi, S.2    Bales, K.R.3    Kuchibhotla, U.4
  • 28
    • 67649394336 scopus 로고    scopus 로고
    • Recombinant antibody therapeutics: the impact of glycosylation on mechanisms of action
    • Jefferis R, (2009) Recombinant antibody therapeutics: the impact of glycosylation on mechanisms of action. Trends Pharmacol Sci 30: 356-362.
    • (2009) Trends Pharmacol Sci , vol.30 , pp. 356-362
    • Jefferis, R.1
  • 30
    • 77953655955 scopus 로고    scopus 로고
    • Industrialization of mAb production technology: the bioprocessing industry at a crossroads
    • Kelley B, (2009) Industrialization of mAb production technology: the bioprocessing industry at a crossroads. MAbs 1: 443-452.
    • (2009) MAbs , vol.1 , pp. 443-452
    • Kelley, B.1
  • 31
    • 40849142102 scopus 로고    scopus 로고
    • Cetuximab-induced anaphylaxis and IgE specific for galactose- α -1,3-galactose
    • Chung CH, Mirakhur B, Chan E, Le QT, Berlin J, et al. (2008) Cetuximab-induced anaphylaxis and IgE specific for galactose- α-1,3-galactose. N Engl J Med 358: 1109-1117.
    • (2008) N Engl J Med , vol.358 , pp. 1109-1117
    • Chung, C.H.1    Mirakhur, B.2    Chan, E.3    Le, Q.T.4    Berlin, J.5
  • 32
    • 12244295475 scopus 로고    scopus 로고
    • Improvement of glycosylation in insect cells with mammalian glycosyltransferases
    • Netherlands
    • Chang GD, Chen CJ, Lin CY, Chen HC, Chen H, (2003) Improvement of glycosylation in insect cells with mammalian glycosyltransferases. pp. 61-71 J Biotechnol. Netherlands.
    • (2003) J Biotechnol , pp. 61-71
    • Chang, G.D.1    Chen, C.J.2    Lin, C.Y.3    Chen, H.C.4    Chen, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.