메뉴 건너뛰기




Volumn 107, Issue 1, 2011, Pages 91-100

Expression of a KDEL-tagged dengue virus protein in cell suspension cultures of Nicotiana tabacum and Morinda citrifolia

Author keywords

Dengue virus; Envelope protein; Plant cell suspension culture; Recombinant protein; Stable expression

Indexed keywords

DENGUE VIRUS; ENVELOPE PROTEINS; PLANT CELL SUSPENSION CULTURES; RECOMBINANT PROTEIN; STABLE EXPRESSION;

EID: 80052819791     PISSN: 01676857     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11240-011-9960-4     Document Type: Article
Times cited : (12)

References (49)
  • 1
    • 0037163853 scopus 로고    scopus 로고
    • Recombinant dengue virus type 2 envelope/hepatitis B surface antigen hybrid protein expressed in Pichia pastoris can function as a bivalent immunogen
    • doi:10.1016/S0168-1656(02)00181-5
    • Bisht H, Chugh D, Raje M, Swaminathan S, Khanna N (2002) Recombinant dengue virus type 2 envelope/hepatitis B surface antigen hybrid protein expressed in Pichia pastoris can function as a bivalent immunogen. J Biotechnol 99: 97-110. doi: 10. 1016/S0168-1656(02)00181-5.
    • (2002) J Biotechnol , vol.99 , pp. 97-110
    • Bisht, H.1    Chugh, D.2    Raje, M.3    Swaminathan, S.4    Khanna, N.5
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 3
    • 77952551864 scopus 로고    scopus 로고
    • Overexpression and characterization of cyprosin B in transformed suspension cells of Cynara cardunculus
    • doi:10.1007/s11240-010-9690-z
    • De Sousa Sampaio P, Neto H, Poejo P, Serrazina S, Soares Pais M (2010) Overexpression and characterization of cyprosin B in transformed suspension cells of Cynara cardunculus. Plant Cell Tissue Organ Cult 101: 311-321. doi: 10. 1007/s11240-010-9690-z.
    • (2010) Plant Cell Tissue Organ Cult , vol.101 , pp. 311-321
    • de Sousa Sampaio, P.1    Neto, H.2    Poejo, P.3    Serrazina, S.4    Soares Pais, M.5
  • 4
    • 0028302115 scopus 로고
    • Analysis of C-terminally truncated dengue 2 and dengue 3 virus envelope glycoproteins: processing in insect cells and immunogenic properties in mice
    • doi:10.1099/0022-1317-75-7-1569
    • Delenda C, Staropoli I, Frenkiel M, Cabani L, Deubel V (1994) Analysis of C-terminally truncated dengue 2 and dengue 3 virus envelope glycoproteins: processing in insect cells and immunogenic properties in mice. J Gen Virol 75: 1569-1578. doi: 10. 1099/0022-1317-75-7-1569.
    • (1994) J Gen Virol , vol.75 , pp. 1569-1578
    • Delenda, C.1    Staropoli, I.2    Frenkiel, M.3    Cabani, L.4    Deubel, V.5
  • 5
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • doi:10.1006/jmbi.2000.3903
    • Emanuelsson O, Nielsen H, Brunak S, von Heijne G (2000) Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J Mol Biol 300: 1005-1016. doi: 10. 1006/jmbi. 2000. 3903.
    • (2000) J Mol Biol , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    von Heijne, G.4
  • 6
    • 14744298421 scopus 로고    scopus 로고
    • Protein modifications in the plant secretory pathway: current status and practical implications in molecular pharming
    • doi:10.1016/j.vaccine.2004.11.003
    • Faye L, Boulaflous A, Benchabane M, Gomord V, Michaud D (2005) Protein modifications in the plant secretory pathway: current status and practical implications in molecular pharming. Vaccine 23: 1770-1778. doi: 10. 1016/j. vaccine. 2004. 11. 003.
    • (2005) Vaccine , vol.23 , pp. 1770-1778
    • Faye, L.1    Boulaflous, A.2    Benchabane, M.3    Gomord, V.4    Michaud, D.5
  • 7
    • 0030731752 scopus 로고    scopus 로고
    • Optimization of scFv antibody production in transgenic plants
    • doi:10.1016/S1380-2933(97)00014-6
    • Fiedler U, Phillips J, Artsaenko O, Conrad U (1997) Optimization of scFv antibody production in transgenic plants. Immunotechnology 3(3): 205-216. doi: 10. 1016/S1380-2933(97)00014-6.
    • (1997) Immunotechnology , vol.3 , Issue.3 , pp. 205-216
    • Fiedler, U.1    Phillips, J.2    Artsaenko, O.3    Conrad, U.4
  • 8
    • 1542381015 scopus 로고    scopus 로고
    • Plant-based production of biopharmaceuticals
    • doi:10.1016/j.pbi.2004.01.007
    • Fischer R, Stoger E, Schillberg S, Christou P, Twyman R (2004) Plant-based production of biopharmaceuticals. Curr Opin Plant Biol 7(2): 152-158. doi: 10. 1016/j. pbi. 2004. 01. 007.
    • (2004) Curr Opin Plant Biol , vol.7 , Issue.2 , pp. 152-158
    • Fischer, R.1    Stoger, E.2    Schillberg, S.3    Christou, P.4    Twyman, R.5
  • 9
    • 77955248510 scopus 로고    scopus 로고
    • Plant-derived vaccines and other therapeutics produced in contained systems
    • doi:10.1586/erv.10.91
    • Franconi R, Demurtas O, Massa S (2010) Plant-derived vaccines and other therapeutics produced in contained systems. Expert Rev Vacc 9(8): 877-892. doi: 10. 1586/erv. 10. 91.
    • (2010) Expert Rev Vacc , vol.9 , Issue.8 , pp. 877-892
    • Franconi, R.1    Demurtas, O.2    Massa, S.3
  • 10
    • 0014276538 scopus 로고
    • Nutrient requirements of suspension cultures of soybean root cells
    • doi:10.1016/0014-4827(68)90403-5
    • Gamborg O, Miller R, Ojima K (1968) Nutrient requirements of suspension cultures of soybean root cells. Exp Cell Res 50(1): 151-158. doi: 10. 1016/0014-4827(68)90403-5.
    • (1968) Exp Cell Res , vol.50 , Issue.1 , pp. 151-158
    • Gamborg, O.1    Miller, R.2    Ojima, K.3
  • 11
    • 3442886589 scopus 로고    scopus 로고
    • Expression of the human milk protein sCD14 in tobacco plant cell culture
    • doi:10.1023/B:TICU.0000025667.46429.4d
    • Girard L, Bastin M, Courtois D (2004) Expression of the human milk protein sCD14 in tobacco plant cell culture. Plant Cell Tissue Organ Cult 78: 253-260. doi: 10. 1023/B: TICU. 0000025667. 46429. 4d.
    • (2004) Plant Cell Tissue Organ Cult , vol.78 , pp. 253-260
    • Girard, L.1    Bastin, M.2    Courtois, D.3
  • 12
    • 70450248470 scopus 로고    scopus 로고
    • Expression of hemagglutinin-neuraminidase glycoprotein of newcastle disease virus in agroinfiltrated Nicotiana benthamiana plants
    • doi:10.1016/j.jbiotec.2009.09.015
    • Gómez E, Chimeno Zoth S, Asurmendi Vázquez, Rovere C, Berinstein A (2009) Expression of hemagglutinin-neuraminidase glycoprotein of newcastle disease virus in agroinfiltrated Nicotiana benthamiana plants. J Biotechnol 144: 337-340. doi: 10. 1016/j. jbiotec. 2009. 09. 015.
    • (2009) J Biotechnol , vol.144 , pp. 337-340
    • Gómez, E.1    Chimeno Zoth, S.2    Asurmendi, V.3    Rovere, C.4    Berinstein, A.5
  • 13
    • 8344236780 scopus 로고    scopus 로고
    • Plant cell cultures for the production of recombinant proteins
    • doi:10.1038/nbt1027
    • Hellwig S, Drossar J, Twyman R, Fischer R (2004) Plant cell cultures for the production of recombinant proteins. Nat Biotechnol 22(11): 1415-1422. doi: 10. 1038/nbt1027.
    • (2004) Nat Biotechnol , vol.22 , Issue.11 , pp. 1415-1422
    • Hellwig, S.1    Drossar, J.2    Twyman, R.3    Fischer, R.4
  • 14
    • 43049109558 scopus 로고    scopus 로고
    • A strong endoplasmic reticulum retention signal in the stem-anchor region of envelope glycoprotein of dengue virus type 2 affects the production of virus-like particles
    • doi:10.1016/j.virol.2007.12.041
    • Hsieh S, Liu I, King C, Chang G, Wang W (2008) A strong endoplasmic reticulum retention signal in the stem-anchor region of envelope glycoprotein of dengue virus type 2 affects the production of virus-like particles. Virology 374(2): 338-350. doi: 10. 1016/j. virol. 2007. 12. 041.
    • (2008) Virology , vol.374 , Issue.2 , pp. 338-350
    • Hsieh, S.1    Liu, I.2    King, C.3    Chang, G.4    Wang, W.5
  • 15
    • 58249094041 scopus 로고    scopus 로고
    • Bioreactor strategies for improving production yield and functionality of a recombinant human protein in transgenic tobacco cell cultures
    • doi:10.1002/bit.22061
    • Huang T, Plesha M, Falk B, Dandekar A, McDonald K (2009) Bioreactor strategies for improving production yield and functionality of a recombinant human protein in transgenic tobacco cell cultures. Biotechnol Bioeng 102: 508-520. doi: 10. 1002/bit. 22061.
    • (2009) Biotechnol Bioeng , vol.102 , pp. 508-520
    • Huang, T.1    Plesha, M.2    Falk, B.3    Dandekar, A.4    McDonald, K.5
  • 16
    • 0034041013 scopus 로고    scopus 로고
    • Production and characterization of biologically active human GM-CSF secreted by genetically modified plant cells
    • doi:10.1006/prep.2000.1232
    • James E, Wang C, Wang Z, Reeves R, Shin J, Magnuson N, Lee J (2000) Production and characterization of biologically active human GM-CSF secreted by genetically modified plant cells. Protein Expr Purif 19: 131-138. doi: 10. 1006/prep. 2000. 1232.
    • (2000) Protein Expr Purif , vol.19 , pp. 131-138
    • James, E.1    Wang, C.2    Wang, Z.3    Reeves, R.4    Shin, J.5    Magnuson, N.6    Lee, J.7
  • 17
    • 70349765520 scopus 로고    scopus 로고
    • The production of biopharmaceuticals in plant systems
    • doi:10.1016/j.biotechadv.2009.07.002
    • Karg S, Kallio P (2009) The production of biopharmaceuticals in plant systems. Biotechnol Adv 27(6): 879-894. doi: 10. 1016/j. biotechadv. 2009. 07. 002.
    • (2009) Biotechnol Adv , vol.27 , Issue.6 , pp. 879-894
    • Karg, S.1    Kallio, P.2
  • 18
    • 0034702096 scopus 로고    scopus 로고
    • Purified dengue 2 virus envelope glycoprotein aggregates produced by baculovirus are immunogenic in mice
    • doi:10.1016/S0264-410X(00)00032-3
    • Kelly E, Greene J, King A, Innis B (2000) Purified dengue 2 virus envelope glycoprotein aggregates produced by baculovirus are immunogenic in mice. Vaccine 18(23): 2549-2559. doi: 10. 1016/S0264-410X(00)00032-3.
    • (2000) Vaccine , vol.18 , Issue.23 , pp. 2549-2559
    • Kelly, E.1    Greene, J.2    King, A.3    Innis, B.4
  • 19
    • 3442902015 scopus 로고    scopus 로고
    • Direct transfer and expression of human GM-CSF in tobacco suspension cell using Agrobacterium-mediated transfer system
    • doi:10.1023/B:TICU.0000022555.50772.09
    • Kim Y, Kwon T, Sik Y (2004) Direct transfer and expression of human GM-CSF in tobacco suspension cell using Agrobacterium-mediated transfer system. Plant Cell Tissue Organ Cult 78(2): 133-138. doi: 10. 1023/B: TICU. 0000022555. 50772. 09.
    • (2004) Plant Cell Tissue Organ Cult , vol.78 , Issue.2 , pp. 133-138
    • Kim, Y.1    Kwon, T.2    Sik, Y.3
  • 20
    • 33750570024 scopus 로고    scopus 로고
    • Expression of a cholera toxin B subunit in transgenic lettuce (Lactuca sativa L.) using Agrobacterium-mediated transformation system
    • Kim Y, Kim B, Kim T, Kang T, Yang M (2006) Expression of a cholera toxin B subunit in transgenic lettuce (Lactuca sativa L.) using Agrobacterium-mediated transformation system. Plant Cell Tissue Organ Cult 87: 203-210.
    • (2006) Plant Cell Tissue Organ Cult , vol.87 , pp. 203-210
    • Kim, Y.1    Kim, B.2    Kim, T.3    Kang, T.4    Yang, M.5
  • 21
    • 79957496315 scopus 로고    scopus 로고
    • Expression and assembly of ApxIIA toxin of Actinobacillus pleuropneumoniae fused with the enterotoxigenic E. coli heat-labile toxin B subunit in transgenic tobacco
    • doi: 10. 1007/s11240-010-9877-3
    • Kim M, Kim T, Yoo H, Yang M (2010a) Expression and assembly of ApxIIA toxin of Actinobacillus pleuropneumoniae fused with the enterotoxigenic E. coli heat-labile toxin B subunit in transgenic tobacco. Plant Cell Tissue Organ Cult. Online First. doi: 10. 1007/s11240-010-9877-3.
    • (2010) Plant Cell Tissue Organ Cult
    • Kim, M.1    Kim, T.2    Yoo, H.3    Yang, M.4
  • 22
    • 77957753828 scopus 로고    scopus 로고
    • Cholera toxin B subunit-domain III of dengue virus envelope glycoprotein E fusion protein production in transgenic plants
    • doi:10.1016/j.pep.2010.07.013
    • Kim T, Kim M, Yang M (2010b) Cholera toxin B subunit-domain III of dengue virus envelope glycoprotein E fusion protein production in transgenic plants. Protein Expr Purif 74(2): 236-241. doi: 10. 1016/j. pep. 2010. 07. 013.
    • (2010) Protein Expr Purif , vol.74 , Issue.2 , pp. 236-241
    • Kim, T.1    Kim, M.2    Yang, M.3
  • 23
    • 50849098592 scopus 로고    scopus 로고
    • Global spread and persistence of dengue
    • doi:10.1146/annurev.micro.62.081307.163005
    • Kyle J, Harris E (2008) Global spread and persistence of dengue. Annu Rev Microbiol 62: 71-92. doi: 10. 1146/annurev. micro. 62. 081307. 163005.
    • (2008) Annu Rev Microbiol , vol.62 , pp. 71-92
    • Kyle, J.1    Harris, E.2
  • 24
  • 26
    • 79952695566 scopus 로고    scopus 로고
    • Expression of the Escherichia coli heat-labile enterotoxin B subunit in transgenic watercress (Nasturtium officinale L.)
    • doi:10.1007/s11240-010-9835-0
    • Loc N, Song N, Tien N, Minh T, Nga P, Kim T, Yang M (2010) Expression of the Escherichia coli heat-labile enterotoxin B subunit in transgenic watercress (Nasturtium officinale L.). Plant Cell Tissue Organ Cult 105(1): 39-45. doi: 10. 1007/s11240-010-9835-0.
    • (2010) Plant Cell Tissue Organ Cult , vol.105 , Issue.1 , pp. 39-45
    • Loc, N.1    Song, N.2    Tien, N.3    Minh, T.4    Nga, P.5    Kim, T.6    Yang, M.7
  • 27
    • 24044482293 scopus 로고    scopus 로고
    • Expression of the antibody 14D9 in Nicotiana tabacum hairy roots
    • doi: 10. 2225/vol8-issue2-fulltext-10
    • Martínez C, Petruccelli S, Giulietti A, Álvarez M (2005) Expression of the antibody 14D9 in Nicotiana tabacum hairy roots. Electronic Journal of Biotechnology 8(2): 170-176. doi: 10. 2225/vol8-issue2-fulltext-10. http://www. ejbiotechnology. info/content/vol8/issue2/full/10/index. html.
    • (2005) Electronic Journal of Biotechnology , vol.8 , Issue.2 , pp. 170-176
    • Martínez, C.1    Petruccelli, S.2    Giulietti, A.3    Álvarez, M.4
  • 28
    • 77952239645 scopus 로고    scopus 로고
    • Exploring different strategies to express dengue virus envelope protein in a plant system
    • doi:10.1007/s10529-010-0236-6
    • Martínez C, Topal E, Giulietti A, Rodríguez Talou J, Mason H (2010) Exploring different strategies to express dengue virus envelope protein in a plant system. Biotechnol Lett 32: 867-875. doi: 10. 1007/s10529-010-0236-6.
    • (2010) Biotechnol Lett , vol.32 , pp. 867-875
    • Martínez, C.1    Topal, E.2    Giulietti, A.3    Rodríguez Talou, J.4    Mason, H.5
  • 29
    • 0344304516 scopus 로고    scopus 로고
    • Carboxy-terminally truncated Dengue 4 virus envelope glycoprotein expressed in Pichia pastoris induced neutralizing antibodies and resistance to Dengue 4 virus challenge in mice
    • doi:10.1007/s00705-003-0167-9
    • Muné M, Rodríguez R, Ramírez R, Soto Y, Sierra B, Rodríguez Roche R, Marquez G, Garcia J, Guillén G, Guzmán G (2003) Carboxy-terminally truncated Dengue 4 virus envelope glycoprotein expressed in Pichia pastoris induced neutralizing antibodies and resistance to Dengue 4 virus challenge in mice. Arch Virol 148: 2267-2273. doi: 10. 1007/s00705-003-0167-9.
    • (2003) Arch Virol , vol.148 , pp. 2267-2273
    • Muné, M.1    Rodríguez, R.2    Ramírez, R.3    Soto, Y.4    Sierra, B.5    Rodríguez Roche, R.6    Marquez, G.7    Garcia, J.8    Guillén, G.9    Guzmán, G.10
  • 30
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco tissue cultures
    • doi:10.1111/j.1399-3054.1962.tb08052.x
    • Murashige T, Skoog F (1962) A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiol Plant 15: 473-497. doi: 10. 1111/j. 1399-3054. 1962. tb08052. x.
    • (1962) Physiol Plant , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 31
    • 79251595840 scopus 로고    scopus 로고
    • Review of dengue virus and the development of a vaccine
    • doi:10.1016/j.biotechadv.2010.11.008
    • Murrell S, Wu S, Butler M (2011) Review of dengue virus and the development of a vaccine. Biotechnol Adv 29: 239-247. doi: 10. 1016/j. biotechadv. 2010. 11. 008.
    • (2011) Biotechnol Adv , vol.29 , pp. 239-247
    • Murrell, S.1    Wu, S.2    Butler, M.3
  • 32
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • doi:10.1093/protein/10.1.1
    • Nielsen H, Engelbrecht J, Brunak S, von Heijne G (1997) Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 10: 1-6. doi: 10. 1093/protein/10. 1. 1.
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 33
    • 0342900074 scopus 로고
    • Relation between primary and secondary metabolism in plant cell suspensions
    • doi:10.1007/BF00052164
    • Plas L, Eijkelboom C, Hagendoorn MJM (1995) Relation between primary and secondary metabolism in plant cell suspensions. Plant Cell Tissue Organ Cult 43(2): 111-116. doi: 10. 1007/BF00052164.
    • (1995) Plant Cell Tissue Organ Cult , vol.43 , Issue.2 , pp. 111-116
    • Plas, L.1    Eijkelboom, C.2    Hagendoorn, M.J.M.3
  • 34
    • 0038024238 scopus 로고    scopus 로고
    • Traditional and novel approaches to flavivirus vaccines
    • doi:10.1016/S0020-7519(03)00063-8
    • Pugachev K, Guirakhoo F, Trent D, Monath T (2003) Traditional and novel approaches to flavivirus vaccines. Int J Parasitol 33: 567-582. doi: 10. 1016/S0020-7519(03)00063-8.
    • (2003) Int J Parasitol , vol.33 , pp. 567-582
    • Pugachev, K.1    Guirakhoo, F.2    Trent, D.3    Monath, T.4
  • 35
    • 25144523093 scopus 로고    scopus 로고
    • New developments in flavivirus vaccines with special attention to yellow fever
    • doi:00001432-200510000-00004
    • Pugachev K, Guirakhoo F, Monath T (2005) New developments in flavivirus vaccines with special attention to yellow fever. Curr Opin Infect Dis 18: 387-394. doi: 00001432-200510000-00004.
    • (2005) Curr Opin Infect Dis , vol.18 , pp. 387-394
    • Pugachev, K.1    Guirakhoo, F.2    Monath, T.3
  • 37
    • 34547819753 scopus 로고    scopus 로고
    • Production of dengue 2 envelope domain III in plant using TMV-based vector system
    • doi:10.1016/j.vaccine.2007.06.029
    • Saejung W, Fujiyama K, Takasaki T, Ito M, Hori K, Malasit P, Watanabe Y, Kurane I, Seki T (2007) Production of dengue 2 envelope domain III in plant using TMV-based vector system. Vaccine 25(36): 6646-6654. doi: 10. 1016/j. vaccine. 2007. 06. 029.
    • (2007) Vaccine , vol.25 , Issue.36 , pp. 6646-6654
    • Saejung, W.1    Fujiyama, K.2    Takasaki, T.3    Ito, M.4    Hori, K.5    Malasit, P.6    Watanabe, Y.7    Kurane, I.8    Seki, T.9
  • 38
    • 0035007556 scopus 로고    scopus 로고
    • Production of spider silk proteins in tobacco and potato
    • doi:10.1038/89335
    • Scheller J, Gührs K, Grosse F, Conrad U (2001) Production of spider silk proteins in tobacco and potato. Nat Biotechnol 19(6): 573-577. doi: 10. 1038/89335.
    • (2001) Nat Biotechnol , vol.19 , Issue.6 , pp. 573-577
    • Scheller, J.1    Gührs, K.2    Grosse, F.3    Conrad, U.4
  • 39
    • 70349765665 scopus 로고    scopus 로고
    • Foreign protein production using plant cell and organ cultures: advantages and limitations
    • doi:10.1016/j.biotechadv.2009.05.009
    • Shih S, Doran P (2009) Foreign protein production using plant cell and organ cultures: advantages and limitations. Biotechnol Adv 27: 1036-1042. doi: 10. 1016/j. biotechadv. 2009. 05. 009.
    • (2009) Biotechnol Adv , vol.27 , pp. 1036-1042
    • Shih, S.1    Doran, P.2
  • 40
    • 0037418173 scopus 로고    scopus 로고
    • A plant signal peptide-hepatitis B surface antigen fusion protein with enhanced stability and immunogenicity expressed in plant cells
    • doi:10.1073_pnas.0438037100
    • Sojikul P, Buehner N, Mason H (2003) A plant signal peptide-hepatitis B surface antigen fusion protein with enhanced stability and immunogenicity expressed in plant cells. PNAS 100(5): 2209-2214. doi: 10. 1073_pnas. 0438037100.
    • (2003) Pnas , vol.100 , Issue.5 , pp. 2209-2214
    • Sojikul, P.1    Buehner, N.2    Mason, H.3
  • 41
    • 33845756751 scopus 로고    scopus 로고
    • Approaches to achieve high-level heterologous protein production in plants
    • doi:10.1111/j.1467-7652.2006.00216.x
    • Streatfield S (2007) Approaches to achieve high-level heterologous protein production in plants. Plant Biotechnol J 5: 2-15. doi: 10. 1111/j. 1467-7652. 2006. 00216. x.
    • (2007) Plant Biotechnol J , vol.5 , pp. 2-15
    • Streatfield, S.1
  • 42
    • 0031471296 scopus 로고    scopus 로고
    • The production of recombinant dengue virus E protein using Escherichia coli and Pichia pastoris
    • doi:10.1016/S0166-0934(97)00151-1
    • Sugrue R, Cui T, Xu Q, Fu J, Chan Y (1997) The production of recombinant dengue virus E protein using Escherichia coli and Pichia pastoris. J Virol Methods 69: 159-169. doi: 10. 1016/S0166-0934(97)00151-1.
    • (1997) J Virol Methods , vol.69 , pp. 159-169
    • Sugrue, R.1    Cui, T.2    Xu, Q.3    Fu, J.4    Chan, Y.5
  • 43
    • 12344325123 scopus 로고    scopus 로고
    • Recent developments in the use of transgenic plants for the production of human therapeutics and biopharmaceuticals
    • doi:10.1007/s11240-004-0653-0
    • Teli N, Timko M (2004) Recent developments in the use of transgenic plants for the production of human therapeutics and biopharmaceuticals. Plant Cell Tissue Organ Cult 79(2): 125-145. doi: 10. 1007/s11240-004-0653-0.
    • (2004) Plant Cell Tissue Organ Cult , vol.79 , Issue.2 , pp. 125-145
    • Teli, N.1    Timko, M.2
  • 44
    • 65349122388 scopus 로고    scopus 로고
    • Virus-specific read-through codon preference affects infectivity of chimeric cucumber green mottle mosaic viruses displaying a dengue virus epitope
    • Article ID 781712. doi: 10. 1155/2009/781712
    • Teoh P, Ooi A, AbuBakar S, Othman R (2009) Virus-specific read-through codon preference affects infectivity of chimeric cucumber green mottle mosaic viruses displaying a dengue virus epitope. J Biomed Biotechnol, Volume 2009, Article ID 781712. doi: 10. 1155/2009/781712.
    • (2009) J Biomed Biotechnol
    • Teoh, P.1    Ooi, A.2    AbuBakar, S.3    Othman, R.4
  • 45
    • 0033498455 scopus 로고    scopus 로고
    • Rice cell culture as an alternative production system for functional diagnostic and therapeutic antibodies
    • doi:10.1023/A:1008969031219
    • Torres E, Vaquero C, Nicholson L, Sack M, Stöger E, Drossard J, Christou P, Fischer R, Perrin Y (1999) Rice cell culture as an alternative production system for functional diagnostic and therapeutic antibodies. Transgenic Res 8(6): 441-449. doi: 10. 1023/A: 1008969031219.
    • (1999) Transgenic Res , vol.8 , Issue.6 , pp. 441-449
    • Torres, E.1    Vaquero, C.2    Nicholson, L.3    Sack, M.4    Stöger, E.5    Drossard, J.6    Christou, P.7    Fischer, R.8    Perrin, Y.9
  • 46
    • 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
    • doi:10.1111/j.1467-7652.2005.00137.x
    • Triguero A, Cabrera G, Cremata J, Yuen C, Wheeler J, Ramírez N (2005) 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(4): 449-457. doi: 10. 1111/j. 1467-7652. 2005. 00137. x.
    • (2005) Plant Biotechnol J , vol.3 , Issue.4 , pp. 449-457
    • Triguero, A.1    Cabrera, G.2    Cremata, J.3    Yuen, C.4    Wheeler, J.5    Ramírez, N.6
  • 47
    • 0242475327 scopus 로고    scopus 로고
    • Molecular farming in plants: host systems and expression technology
    • doi:10.1016/j.tibtech.2003.10.002
    • Twyman R, Stoger E, Schillberg S, Christou P, Fischer R (2003) Molecular farming in plants: host systems and expression technology. Trends Biotechnol 21(12): 570-578. doi: 10. 1016/j. tibtech. 2003. 10. 002.
    • (2003) Trends Biotechnol , vol.21 , Issue.12 , pp. 570-578
    • Twyman, R.1    Stoger, E.2    Schillberg, S.3    Christou, P.4    Fischer, R.5
  • 48
    • 70349977370 scopus 로고    scopus 로고
    • Progress towards a dengue vaccine
    • doi:10.1016/S1473-3099(09)70254-3
    • Webster D, Farrar J, Rowland-Jones S (2009) Progress towards a dengue vaccine. Lancet Infect Dis 9: 678-687. doi: 10. 1016/S1473-3099(09)70254-3.
    • (2009) Lancet Infect Dis , vol.9 , pp. 678-687
    • Webster, D.1    Farrar, J.2    Rowland-Jones, S.3
  • 49
    • 84867737732 scopus 로고    scopus 로고
    • Guidelines for the clinical evaluation of dengue vaccines in endemic areas
    • WHO (World Health Organization) WHO/IVB/08.12
    • WHO (World Health Organization) (2008) Guidelines for the clinical evaluation of dengue vaccines in endemic areas. Inmunization, vaccines and biologicals. WHO/IVB/08. 12. http://whqlibdoc. who. int/hq/2008/WHO_IVB_08. 12_eng. pdf.
    • (2008) Inmunization, vaccines and biologicals


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.