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Volumn 9, Issue 8, 2010, Pages 859-876

Transient expression systems for plant-derived biopharmaceuticals

Author keywords

Agrobacterium; monoclonal antibodies; plant virus; transient expression; vaccine; virus peptide display; virus like particles

Indexed keywords

BETA GLUCURONIDASE; GREEN FLUORESCENT PROTEIN; HYDROPHOBIN; IMMUNOGLOBULIN FC FRAGMENT; MONOCLONAL ANTIBODY; VIRUS VECTOR; RECOMBINANT VACCINE;

EID: 77955260676     PISSN: 14760584     EISSN: 17448395     Source Type: Journal    
DOI: 10.1586/erv.10.85     Document Type: Review
Times cited : (141)

References (157)
  • 1
  • 3
    • 67849122688 scopus 로고    scopus 로고
    • Chloroplast-derived vaccine antigens and biopharmaceuticals: Expression, folding, assembly and functionality
    • Chebolu S, Daniell H. Chloroplast-derived vaccine antigens and biopharmaceuticals: expression, folding, assembly and functionality. Curr. Top. Microbiol. Immunol. 332, 33-54 (2009).
    • (2009) Curr. Top. Microbiol. Immunol. , vol.332 , pp. 33-54
    • Chebolu, S.1    Daniell, H.2
  • 4
    • 62849111312 scopus 로고    scopus 로고
    • A plant-derived recombinant human glucocerebrosidase enzyme - A preclinical and Phase i investigation
    • Aviezer D, Brill-Almon E, Shaaltiel Y et al. A plant-derived recombinant human glucocerebrosidase enzyme - a preclinical and Phase I investigation. PLoS One 4, e4792 (2009).
    • (2009) PLoS One , vol.4
    • Aviezer, D.1    Brill-Almon, E.2    Shaaltiel, Y.3
  • 5
    • 48249120731 scopus 로고    scopus 로고
    • Plant-produced idiotype vaccines for the treatment of non-Hodgkin's lymphoma: Safety and immunogenicity in a Phase i clinical study
    • McCormick AA, Reddy S, Reinl SJ et al. Plant-produced idiotype vaccines for the treatment of non-Hodgkin's lymphoma: safety and immunogenicity in a Phase I clinical study. Proc. Natl Acad. Sci. USA 105, 10131-10136 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 10131-10136
    • McCormick, A.A.1    Reddy, S.2    Reinl, S.J.3
  • 6
    • 77953964469 scopus 로고    scopus 로고
    • The production of hemagglutinin- based virus-like particles in plants: A rapid, efficient and safe response to pandemic influenza
    • D-Aoust MA, Couture MM, Charland N et al. The production of hemagglutinin- based virus-like particles in plants: a rapid, efficient and safe response to pandemic influenza. Plant Biotechnol. J. 8, 607-619 (2010).
    • (2010) Plant Biotechnol. J. , vol.8 , pp. 607-619
    • D'Aoust, M.A.1    Couture, M.M.2    Charland, N.3
  • 8
    • 14844293838 scopus 로고    scopus 로고
    • Magnifection - A new platform for expressing recombinant vaccines in plants
    • Gleba Y, Klimyuk V, Marillonnet S. Magnifection - a new platform for expressing recombinant vaccines in plants. Vaccine 23, 2042-2048 (2005).
    • (2005) Vaccine , vol.23 , pp. 2042-2048
    • Gleba, Y.1    Klimyuk, V.2    Marillonnet, S.3
  • 10
    • 46049083590 scopus 로고    scopus 로고
    • Viral vectors for production of recombinant proteins in plants
    • Lico C, Chen Q, Santi L. Viral vectors for production of recombinant proteins in plants. J. Cell Physiol. 216, 366-377 (2008).
    • (2008) J. Cell Physiol. , vol.216 , pp. 366-377
    • Lico, C.1    Chen, Q.2    Santi, L.3
  • 11
    • 69449107844 scopus 로고    scopus 로고
    • Plant-based strategies aimed at expressing HIV antigens and neutralizing antibodies at high levels. Nef as a case study
    • Marusic C, Vitale A, Pedrazzini E et al. Plant-based strategies aimed at expressing HIV antigens and neutralizing antibodies at high levels. Nef as a case study. Transgenic Res. 18, 499-512 (2009).
    • (2009) Transgenic Res. , vol.18 , pp. 499-512
    • Marusic, C.1    Vitale, A.2    Pedrazzini, E.3
  • 12
    • 40549102456 scopus 로고    scopus 로고
    • Genetically engineered tobacco mosaic virus as nanoparticle vaccines
    • McCormick AA, Palmer KE. Genetically engineered tobacco mosaic virus as nanoparticle vaccines. Expert Rev. Vaccines 7, 33-41 (2008).
    • (2008) Expert Rev. Vaccines , vol.7 , pp. 33-41
    • McCormick, A.A.1    Palmer, K.E.2
  • 13
    • 58149112262 scopus 로고    scopus 로고
    • Plant-produced vaccines: Promise and reality
    • Rybicki EP. Plant-produced vaccines: promise and reality. DrugDiscov. Today 14, 16-24 (2009).
    • (2009) DrugDiscov. Today , vol.14 , pp. 16-24
    • Rybicki, E.P.1
  • 15
    • 53849112341 scopus 로고    scopus 로고
    • Recent progress in the development of plant derived vaccines
    • Yusibov, V, Rabindran S. Recent progress in the development of plant derived vaccines. Expert Rev. Vaccines 7, 1173-1183 (2008).
    • (2008) Expert Rev. Vaccines , vol.7 , pp. 1173-1183
    • Yusibov, V.1    Rabindran, S.2
  • 16
    • 60549093038 scopus 로고    scopus 로고
    • A case study for plant-made pharmaceuticals comparing different plant expression and production systems
    • Vancanneyt G, Dubald M, Schroder W, Peters J, Botterman J. A case study for plant-made pharmaceuticals comparing different plant expression and production systems. Methods Mol. Biol. 483, 209-221 (2009).
    • (2009) Methods Mol. Biol. , vol.483 , pp. 209-221
    • Vancanneyt, G.1    Dubald, M.2    Schroder, W.3    Peters, J.4    Botterman, J.5
  • 17
    • 37249076430 scopus 로고    scopus 로고
    • Current status of binary vectors and superbinary vectors
    • Komori T, Imayama T, Kato N et al. Current status of binary vectors and superbinary vectors. Plant Physiol. 145, 1155-1160 (2007).
    • (2007) Plant Physiol. , vol.145 , pp. 1155-1160
    • Komori, T.1    Imayama, T.2    Kato, N.3
  • 18
    • 38949207311 scopus 로고    scopus 로고
    • T-DNA binary vectors and systems
    • Lee LY, Gelvin SB. T-DNA binary vectors and systems. Plant Physiol. 146, 325-332 (2008).
    • (2008) Plant Physiol. , vol.146 , pp. 325-332
    • Lee, L.Y.1    Gelvin, S.B.2
  • 19
    • 49449105359 scopus 로고    scopus 로고
    • Nicotiana benthamiana: Its history and future as a model for plant- pathogen interactions
    • Goodin MM, Zaitlin D, Naidu RA, Lommel SA. Nicotiana benthamiana: its history and future as a model for plant- pathogen interactions. Mol. Plant Microbe Interact. 21, 1015-1026 (2008).
    • (2008) Mol. Plant Microbe Interact. , vol.21 , pp. 1015-1026
    • Goodin, M.M.1    Zaitlin, D.2    Naidu, R.A.3    Lommel, S.A.4
  • 20
    • 69449106537 scopus 로고    scopus 로고
    • Optimization of conditions for transient Agrobacterium- mediated gene expression assays in Arabidopsis
    • Kim MJ, Baek K, Park CM. Optimization of conditions for transient Agrobacterium- mediated gene expression assays in Arabidopsis. Plant Cell Rep. 28, 1159-1167 (2009).
    • (2009) Plant Cell Rep. , vol.28 , pp. 1159-1167
    • Kim, M.J.1    Baek, K.2    Park, C.M.3
  • 21
    • 33745252002 scopus 로고    scopus 로고
    • Transient expression assay by agroinfiltration of leaves
    • Lee MW, Yang Y. Transient expression assay by agroinfiltration of leaves. Methods Mol. Biol. 323, 225-229 (2006).
    • (2006) Methods Mol. Biol. , vol.323 , pp. 225-229
    • Lee, M.W.1    Yang, Y.2
  • 22
    • 21444444551 scopus 로고    scopus 로고
    • Highly efficient transient expression of functional recombinant antibodies in lettuce
    • Negrouk V, Eisner G, Lee H et al. Highly efficient transient expression of functional recombinant antibodies in lettuce. Plant Sci. 169, 433-438 (2005).
    • (2005) Plant Sci. , vol.169 , pp. 433-438
    • Negrouk, V.1    Eisner, G.2    Lee, H.3
  • 23
    • 60549101719 scopus 로고    scopus 로고
    • Rapid system for evaluating bioproduction capacity complex pharmaceutical proteins in plants
    • Medrano G, Reidy MJ, Liu J et al. Rapid system for evaluating bioproduction capacity complex pharmaceutical proteins in plants. Methods Mol. Biol. 483, 51-67 (2009).
    • (2009) Methods Mol. Biol. , vol.483 , pp. 51-67
    • Medrano, G.1    Reidy, M.J.2    Liu, J.3
  • 24
    • 60349102014 scopus 로고    scopus 로고
    • A model of Agrobacterium tumefaciens vacuum infiltration into harvested leaf tissue and subsequent in planta transgene transient expression
    • Simmons CW, VanderGheynst JS, Upadhyaya SK et al. A model of Agrobacterium tumefaciens vacuum infiltration into harvested leaf tissue and subsequent in planta transgene transient expression. Biotechnol. Bioeng. 102, 965-970 (2009).
    • (2009) Biotechnol. Bioeng. , vol.102 , pp. 965-970
    • Simmons, C.W.1    Vandergheynst, J.S.2    Upadhyaya, S.K.3
  • 25
    • 33745226469 scopus 로고    scopus 로고
    • In planta Agrobacterium-mediated transformation by vacuum infiltration
    • Tague BW, Mantis J. In planta Agrobacterium-mediated transformation by vacuum infiltration. Methods Mol. Biol. 323, 215-223 (2006).
    • (2006) Methods Mol. Biol. , vol.323 , pp. 215-223
    • Tague, B.W.1    Mantis, J.2
  • 26
    • 33846805740 scopus 로고    scopus 로고
    • Amplicon-plus targeting technology (APTT) for rapid production of a highly unstable vaccine protein in tobacco plants
    • Azhakanandam K, Weissinger SM, Nicholson JS, Qu R, Weissinger AK. Amplicon-plus targeting technology (APTT) for rapid production of a highly unstable vaccine protein in tobacco plants. Plant Mol. Biol. 63, 393-404 (2007).
    • (2007) Plant Mol. Biol. , vol.63 , pp. 393-404
    • Azhakanandam, K.1    Weissinger, S.M.2    Nicholson, J.S.3    Qu, R.4    Weissinger, A.K.5
  • 27
    • 24944498904 scopus 로고    scopus 로고
    • Systemic Agrobacterium tumefaciens-mediated transfection of viral replicons for efficient transient expression in plants
    • Marillonnet S, Thoeringer C, Kandzia R, Klimyuk V, Gleba Y. Systemic Agrobacterium tumefaciens-mediated transfection of viral replicons for efficient transient expression in plants. Nat. Biotechnol. 23, 718-723 (2005).
    • (2005) Nat. Biotechnol. , vol.23 , pp. 718-723
    • Marillonnet, S.1    Thoeringer, C.2    Kandzia, R.3    Klimyuk, V.4    Gleba, Y.5
  • 28
    • 71549120129 scopus 로고    scopus 로고
    • High-level HIV-1 Nef transient expression in Nicotiana benthamiana using the P19 gene silencing suppressor protein of Artichoke mottledcrinckle virus
    • Lombardi R, Circelli P, Villani ME et al. High-level HIV-1 Nef transient expression in Nicotiana benthamiana using the P19 gene silencing suppressor protein of Artichoke mottledcrinckle virus. BMC Biotechnol. 96, 1-11 (2009).
    • (2009) BMC Biotechnol. , vol.96 , pp. 1-11
    • Lombardi, R.1    Circelli, P.2    Villani, M.E.3
  • 29
    • 67650422005 scopus 로고    scopus 로고
    • Boosted expression of the SARS-CoV nucleocapsid protein in tobacco and its immunogenicity in mice
    • Zheng N, Xia R, Yang C et al. Boosted expression of the SARS-CoV nucleocapsid protein in tobacco and its immunogenicity in mice. Vaccine 27, 5001-5007 (2009).
    • (2009) Vaccine , vol.27 , pp. 5001-5007
    • Zheng, N.1    Xia, R.2    Yang, C.3
  • 30
    • 41549141202 scopus 로고    scopus 로고
    • A simple and effective system for foreign gene expression in plants via root absorption of agrobacterial suspension
    • Yang L, Wang H, Liu J et al. A simple and effective system for foreign gene expression in plants via root absorption of agrobacterial suspension. J. Biotechnol. 134, 320-324 (2008).
    • (2008) J. Biotechnol. , vol.134 , pp. 320-324
    • Yang, L.1    Wang, H.2    Liu, J.3
  • 31
    • 13244262550 scopus 로고    scopus 로고
    • Conformational analysis of hepatitis B surface antigen fusions in an Agrobacterium-mediated transient expression system
    • Huang Z, Mason HS. Conformational analysis of hepatitis B surface antigen fusions in an Agrobacterium-mediated transient expression system. Plant Biotechnol. J. 2, 241-249 (2004).
    • (2004) Plant Biotechnol. J. , vol.2 , pp. 241-249
    • Huang, Z.1    Mason, H.S.2
  • 32
    • 35348872523 scopus 로고    scopus 로고
    • Assessing the expression of chicken anemia virus proteins in plants
    • Lacorte C, Lohuis H, Goldbach R, Prins M. Assessing the expression of chicken anemia virus proteins in plants. Virus Res. 129, 80-86 (2007).
    • (2007) Virus Res. , vol.129 , pp. 80-86
    • Lacorte, C.1    Lohuis, H.2    Goldbach, R.3    Prins, M.4
  • 33
    • 75949109975 scopus 로고    scopus 로고
    • Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamiana
    • Joensuu JJ, Conley AJ, Lienemann M et al. Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamiana. Plant Physiol. 152, 622-633 (2009).
    • (2009) Plant Physiol. , vol.152 , pp. 622-633
    • Joensuu, J.J.1    Conley, A.J.2    Lienemann, M.3
  • 34
    • 70450248470 scopus 로고    scopus 로고
    • Expression of hemagglutinin-neuraminidase glycoprotein of newcastle disease virus in agroinfiltrated Nicotiana benthamiana plants
    • Gomez E, Zoth SC, Asurmendi S et al. Expression of hemagglutinin- neuraminidase glycoprotein of newcastle disease virus in agroinfiltrated Nicotiana benthamiana plants. J. Biotechnol. 337-340 (2009).
    • (2009) J. Biotechnol. , pp. 337-340
    • Gomez, E.1    Zoth, S.C.2    Asurmendi, S.3
  • 35
    • 60549084886 scopus 로고    scopus 로고
    • Strategies for improving vaccine antigens expression in transgenic plants: Fusion to carrier sequences
    • Escribano JM, Perez-Filgueira DM. Strategies for improving vaccine antigens expression in transgenic plants: fusion to carrier sequences. Methods Mol. Biol. 483, 275-287 (2009).
    • (2009) Methods Mol. Biol. , vol.483 , pp. 275-287
    • Escribano, J.M.1    Perez-Filgueira, D.M.2
  • 36
    • 33645115904 scopus 로고    scopus 로고
    • HIV-1 p24-immunoglobulin fusion molecule: A new strategy for plant-based protein production
    • Obregon P, Chargelegue D, Drake et al. HIV-1 p24-immunoglobulin fusion molecule: a new strategy for plant-based protein production. Plant Biotechnol. J. 4, 195-207 (2006).
    • (2006) Plant Biotechnol. J. , vol.4 , pp. 195-207
    • Obregon, P.1    Drake, C.D.2
  • 37
    • 34548381792 scopus 로고    scopus 로고
    • Infection, propagation, distribution and stability of plant virus in hairy root cultures
    • Shadwick FS, Doran PM. Infection, propagation, distribution and stability of plant virus in hairy root cultures. J. Biotechnol. 131, 318-329 (2007).
    • (2007) J. Biotechnol. , vol.131 , pp. 318-329
    • Shadwick, F.S.1    Doran, P.M.2
  • 38
    • 33846899777 scopus 로고    scopus 로고
    • Propagation of plant viruses in hairy root cultures: A potential method for in vitro production of epitope vaccines and foreign proteins
    • Shadwick FS, Doran PM. Propagation of plant viruses in hairy root cultures: a potential method for in vitro production of epitope vaccines and foreign proteins. Biotechnol. Bioeng. 96, 570-583 (2007).
    • (2007) Biotechnol. Bioeng. , vol.96 , pp. 570-583
    • Shadwick, F.S.1    Doran, P.M.2
  • 39
    • 46249126415 scopus 로고    scopus 로고
    • Production of recombinant proteins in clonal root cultures using episomal expression vectors
    • Skarjinskaia M, Karl J, Araujo A et al. Production of recombinant proteins in clonal root cultures using episomal expression vectors. Biotechnol. Bioeng. 100, 814-819 (2008).
    • (2008) Biotechnol. Bioeng. , vol.100 , pp. 814-819
    • Skarjinskaia, M.1    Karl, J.2    Araujo, A.3
  • 42
    • 0000049939 scopus 로고
    • The rod-shaped plant viruses
    • Van Regenmortel M, Fraenkel-Conrat H (Eds). Plenum Press, NY, USA
    • Palukaitis P, Zaitlin M. The rod-shaped plant viruses. In: The Plant Viruses (Volume 2). Van Regenmortel M, Fraenkel-Conrat H (Eds). Plenum Press, NY, USA, 105-131 (1986).
    • (1986) The Plant Viruses (Volume 2) , pp. 105-131
    • Palukaitis, P.1    Zaitlin, M.2
  • 43
    • 84934442853 scopus 로고    scopus 로고
    • Construction of infectious clones for RNA viruses: TMV
    • Chapman SN. Construction of infectious clones for RNA viruses: TMV. Methods Mol. Biol. 451, 477-490 (2008).
    • (2008) Methods Mol. Biol. , vol.451 , pp. 477-490
    • Chapman, S.N.1
  • 45
    • 50849086727 scopus 로고    scopus 로고
    • Insertion in the coding region of the movement protein improves stability of the plasmid encoding a tomato mosaic virus-based expression vector
    • Dohi K, Tamai A, Mori M. Insertion in the coding region of the movement protein improves stability of the plasmid encoding a tomato mosaic virus-based expression vector. Arch. Virol. 153, 1667-1675 (2008).
    • (2008) Arch. Virol. , vol.153 , pp. 1667-1675
    • Dohi, K.1    Tamai, A.2    Mori, M.3
  • 46
    • 33747346414 scopus 로고    scopus 로고
    • An internal ribosome entry site located upstream of the crTMV coat protein (CP) gene can be used for CP synthesis in vivo
    • Dorokhov YL, Ivanov PA, Komarova TV et al. An internal ribosome entry site located upstream of the crTMV coat protein (CP) gene can be used for CP synthesis in vivo. J. Gen. Virol. 87, 2693-2697 (2006).
    • (2006) J. Gen. Virol. , vol.87 , pp. 2693-2697
    • Dorokhov, Y.L.1    Ivanov, P.A.2    Komarova, T.V.3
  • 47
    • 15244344931 scopus 로고    scopus 로고
    • A new cell-to-cell transport model for Potexviruses
    • Verchot-Lubicz J. A new cell-to-cell transport model for Potexviruses. Mol. Plant Microbe Interact. 18, 283-290.
    • Mol. Plant Microbe Interact. , vol.18 , pp. 283-290
    • Verchot-Lubicz, J.1
  • 48
    • 34249818166 scopus 로고    scopus 로고
    • Molecular biology of potexviruses: Recent advances
    • Verchot-Lubicz J, Ye CM, Bamunusinghe D. Molecular biology of potexviruses: recent advances. J. Gen. Virol. 88, 1643-1655 (2007).
    • (2007) J. Gen. Virol. , vol.88 , pp. 1643-1655
    • Verchot-Lubicz, J.1    Ye, C.M.2    Bamunusinghe, D.3
  • 49
    • 0029311267 scopus 로고
    • Jellyfish green fluorescent protein as a reporter for virus infections
    • Baulcombe DC, Chapman S, Santa Cruz S. Jellyfish green fluorescent protein as a reporter for virus infections. Plant J. 7, 1045-1053 (1995).
    • (1995) Plant J. , vol.7 , pp. 1045-1053
    • Baulcombe, D.C.1    Chapman, S.2    Santa Cruz, S.3
  • 50
    • 28844438905 scopus 로고    scopus 로고
    • The use of viral vectors to produce hepatitis B virus core particles in plants
    • Mechtcheriakova IA, Eldarov MA, Nicholson L et al. The use of viral vectors to produce hepatitis B virus core particles in plants. J. Virol. Methods 131, 10-15.
    • J. Virol. Methods , vol.131 , pp. 10-15
    • Mechtcheriakova, I.A.1    Eldarov, M.A.2    Nicholson, L.3
  • 51
    • 34147126714 scopus 로고    scopus 로고
    • Stability of potato virus X expression vectors is related to insert size: Implications for replication models and risk assessment
    • Avesani L, Marconi G, Morandini F et al. Stability of potato virus X expression vectors is related to insert size: implications for replication models and risk assessment. Transgenic Res. 16, 587-597 (2007).
    • (2007) Transgenic Res. , vol.16 , pp. 587-597
    • Avesani, L.1    Marconi, G.2    Morandini, F.3
  • 52
    • 33749536223 scopus 로고    scopus 로고
    • Rapid high-yield expression of full-size IgG antibodies in plants coinfected with noncompeting viral vectors
    • Giritch A, Marillonnet S, Engler C et al. Rapid high-yield expression of full-size IgG antibodies in plants coinfected with noncompeting viral vectors. Proc. Natl Acad. Sci. USA 103, 14701-14706 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 14701-14706
    • Giritch, A.1    Marillonnet, S.2    Engler, C.3
  • 54
    • 12944263589 scopus 로고    scopus 로고
    • Expression of multiple foreign epitopes presented as synthetic antigens on the surface of potato virus X particles
    • Uhde K, Fischer R, Commandeur U. Expression of multiple foreign epitopes presented as synthetic antigens on the surface of potato virus X particles. Arch. Virol. 150, 327-340 (2005).
    • (2005) Arch. Virol. , vol.150 , pp. 327-340
    • Uhde, K.1    Fischer, R.2    Commandeur, U.3
  • 56
    • 0026448774 scopus 로고
    • Tagging of plant potyvirus replication and movement by insertion of -glucuronidase into the viralpolyprotein
    • Dolja VV, McBride HJ, Carrington JC. Tagging of plant potyvirus replication and movement by insertion of glucuronidase into the viralpolyprotein. Proc. Natl Acad. Sci. USA 89, 10208-10212 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10208-10212
    • Dolja, V.V.1    McBride, H.J.2    Carrington, J.C.3
  • 57
    • 0033982730 scopus 로고    scopus 로고
    • Mutations in the coat protein gene of plum pox virus suppress particle assembly, heterologous encapsidation and complementation in transgenic plants of Nicotiana benthamiana
    • Varrelmann M, Maiss E. Mutations in the coat protein gene of plum pox virus suppress particle assembly, heterologous encapsidation and complementation in transgenic plants of Nicotiana benthamiana. J. Gen. Virol. 81, 567-576 (2000).
    • (2000) J. Gen. Virol. , vol.81 , pp. 567-576
    • Varrelmann, M.1    Maiss, E.2
  • 58
    • 22044453958 scopus 로고    scopus 로고
    • Simultaneous production of two foreign proteins from a potyvirus-based vector
    • Beauchemin C, Bougie V, Laliberte JF. Simultaneous production of two foreign proteins from a potyvirus-based vector. Virus Res. 112, 1-8 (2005).
    • (2005) Virus Res. , vol.112 , pp. 1-8
    • Beauchemin, C.1    Bougie, V.2    Laliberte, J.F.3
  • 59
    • 45449101649 scopus 로고    scopus 로고
    • Three heterologous proteins simultaneously expressed from a chimeric potyvirus: Infectivity, stability and the correlation of genome and virion lengths
    • Kelloniemi J, Makinen K, Valkonen JP. Three heterologous proteins simultaneously expressed from a chimeric potyvirus: infectivity, stability and the correlation of genome and virion lengths. Virus Res. 135, 282-291 (2008).
    • (2008) Virus Res. , vol.135 , pp. 282-291
    • Kelloniemi, J.1    Makinen, K.2    Valkonen, J.P.3
  • 60
    • 0034523810 scopus 로고    scopus 로고
    • Development and evaluation of a complementation- dependent gene delivery system based on cucumber mosaic virus
    • Zhao Y, Hammond J, Tousignant ME, Hammond RW. Development and evaluation of a complementation- dependent gene delivery system based on cucumber mosaic virus. Arch. Virol. 145, 2285-2295 (2000).
    • (2000) Arch. Virol. , vol.145 , pp. 2285-2295
    • Zhao, Y.1    Hammond, J.2    Tousignant, M.E.3    Hammond, R.W.4
  • 61
    • 33747620065 scopus 로고    scopus 로고
    • A chemically inducible cucumber mosaic virus amplicon system for expression of heterologous proteins in plant tissues
    • Sudarshana MR, Plesha MA, Uratsu SL et al. A chemically inducible cucumber mosaic virus amplicon system for expression of heterologous proteins in plant tissues. Plant Biotechnol. J. 4, 551-559 (2006).
    • (2006) Plant Biotechnol. J. , vol.4 , pp. 551-559
    • Sudarshana, M.R.1    Plesha, M.A.2    Uratsu, S.L.3
  • 62
    • 1642503698 scopus 로고    scopus 로고
    • The C-terminal 33 amino acids of the cucumber mosaic virus 3a protein affect virus movement, RNA binding and inhibition of infection and translation
    • Kim SH, Kalinina NO, Andreev I et al. The C-terminal 33 amino acids of the cucumber mosaic virus 3a protein affect virus movement, RNA binding and inhibition of infection and translation. J. Gen. Virol. 85, 221-230 (2004).
    • (2004) J. Gen. Virol. , vol.85 , pp. 221-230
    • Kim, S.H.1    Kalinina, N.O.2    Andreev, I.3
  • 63
    • 54049087299 scopus 로고    scopus 로고
    • Development of a new cucumber mosaic virus-based plant expression vector with truncated 3a movement protein
    • Fujiki M, Kaczmarczyk JF, Yusibov V, Rabindran S. Development of a new cucumber mosaic virus-based plant expression vector with truncated 3a movement protein. Virology 381, 136-142 (2008).
    • (2008) Virology , vol.381 , pp. 136-142
    • Fujiki, M.1    Kaczmarczyk, J.F.2    Yusibov, V.3    Rabindran, S.4
  • 64
    • 58549084382 scopus 로고    scopus 로고
    • Transient protein expression in three Pisum sativum (green pea) varieties
    • Green BJ, Fujiki M, Mett V et al. Transient protein expression in three Pisum sativum (green pea) varieties. Biotechnol. J. 4, 230-237 (2009).
    • (2009) Biotechnol. J. , vol.4 , pp. 230-237
    • Green, B.J.1    Fujiki, M.2    Mett, V.3
  • 65
    • 60549090444 scopus 로고    scopus 로고
    • Cowpea mosaic virus-based systems for the expression of antigens and antibodies in plants
    • Sainsbury F, Liu L, Lomonossoff GP. Cowpea mosaic virus-based systems for the expression of antigens and antibodies in plants. Methods Mol. Biol. 483, 25-39 (2009).
    • (2009) Methods Mol. Biol. , vol.483 , pp. 25-39
    • Sainsbury, F.1    Liu, L.2    Lomonossoff, G.P.3
  • 66
    • 0034652706 scopus 로고    scopus 로고
    • Engineering cowpea mosaic virus RNA-2 into a vector to express heterologous proteins in plants
    • Gopinath K, Wellink J, Porta C, Taylor KM, Lomonossoff GP, van Kammen A. Engineering cowpea mosaic virus RNA-2 into a vector to express heterologous proteins in plants. Virology 267, 159-173 (2000).
    • (2000) Virology , vol.267 , pp. 159-173
    • Gopinath, K.1    Wellink, J.2    Porta, C.3    Taylor, K.M.4    Lomonossoff, G.P.5    Van Kammen, A.6
  • 67
    • 2542471449 scopus 로고    scopus 로고
    • Cowpea mosaic virus RNA-1 acts as an amplicon whose effects can be counteracted by a RNA-2- encoded suppressor of silencing
    • Liu L, Grainger J, Canizares MC, Angell SM, Lomonossoff GP. Cowpea mosaic virus RNA-1 acts as an amplicon whose effects can be counteracted by a RNA-2- encoded suppressor of silencing. Virology 323, 37-48 (2004).
    • (2004) Virology , vol.323 , pp. 37-48
    • Liu, L.1    Grainger, J.2    Canizares, M.C.3    Angell, S.M.4    Lomonossoff, G.P.5
  • 70
    • 34247250359 scopus 로고    scopus 로고
    • Improved expression of recombinant GFP using a replicating vector based on beet curly top virus in leaf-disks and infiltrated Nicotiana benthamiana leaves
    • Kim K, Sunter G, Bisaro DM, Chung IS. Improved expression of recombinant GFP using a replicating vector based on beet curly top virus in leaf-disks and infiltrated Nicotiana benthamiana leaves. Plant Mol. Biol. 64, 103-112 (2007).
    • (2007) Plant Mol. Biol. , vol.64 , pp. 103-112
    • Kim, K.1    Sunter, G.2    Bisaro, D.M.3    Chung, I.S.4
  • 71
    • 67650156117 scopus 로고    scopus 로고
    • A DNA replicon system for rapid high-level production of virus-like particles in plants
    • Huang Z, Chen Q, Hjelm B, Arntzen C, Mason H. A DNA replicon system for rapid high-level production of virus-like particles in plants. Biotechnol. Bioeng. 103, 706-714 (2009).
    • (2009) Biotechnol. Bioeng. , vol.103 , pp. 706-714
    • Huang, Z.1    Chen, Q.2    Hjelm, B.3    Arntzen, C.4    Mason, H.5
  • 73
    • 33745636103 scopus 로고    scopus 로고
    • A novel function for a ubiquitous plant enzyme pectin methylesterase: The enhancer of RNA silencing
    • Dorokhov YL, Frolova OY, Skurat EV et al. A novel function for a ubiquitous plant enzyme pectin methylesterase: the enhancer of RNA silencing. FEBS Lett. 580, 3872-3878 (2006).
    • (2006) FEBS Lett. , vol.580 , pp. 3872-3878
    • Dorokhov, Y.L.1    Frolova, O.Y.2    Skurat, E.V.3
  • 74
    • 34147095513 scopus 로고    scopus 로고
    • Viral vectors for the expression of proteins in plants
    • Gleba Y, Klimyuk V, Marillonnet S. Viral vectors for the expression of proteins in plants. Curr. Opin. Biotechnol. 18, 134-141 ( 2007).
    • (2007) Curr. Opin. Biotechnol. , vol.18 , pp. 134-141
    • Gleba, Y.1    Klimyuk, V.2    Marillonnet, S.3
  • 75
    • 65849183178 scopus 로고    scopus 로고
    • Golden gate shuffling: A one-pot DNA shuffling method based on type IIs restriction enzymes
    • Engler C, Gruetzner R, Kandzia R, Marillonnet S. Golden gate shuffling: a one-pot DNA shuffling method based on type IIs restriction enzymes. PLoS One 4, e5553 (2009).
    • (2009) PLoS One , vol.4
    • Engler, C.1    Gruetzner, R.2    Kandzia, R.3    Marillonnet, S.4
  • 76
    • 32244449213 scopus 로고    scopus 로고
    • Protection conferred by recombinant Yersinia pestis antigens produced by a rapid and highly scalable plant expression system
    • Santi L, Giritch A, Roy CJ et al. Protection conferred by recombinant Yersinia pestis antigens produced by a rapid and highly scalable plant expression system. Proc. Natl Acad. Sci. USA 103, 861-866 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 861-866
    • Santi, L.1    Giritch, A.2    Roy, C.J.3
  • 77
    • 0344339017 scopus 로고    scopus 로고
    • Protection of mice against challenge with Foot and mouth disease virus (FMDV) by immunization with foliar extracts from plants infected with recombinant Tobacco mosaic virus expressing the FMDV structural protein
    • Wigdorovitz A, Perez Fuilgueira DM, Robertson N et al. Protection of mice against challenge with Foot and mouth disease virus (FMDV) by immunization with foliar extracts from plants infected with recombinant Tobacco mosaic virus expressing the FMDV structural protein. Virology 264, 85-91 (1999).
    • (1999) Virology , vol.264 , pp. 85-91
    • Wigdorovitz, A.1    Perez Fuilgueira, D.M.2    Robertson, N.3
  • 78
    • 33846186010 scopus 로고    scopus 로고
    • Ubiquitin fusion enhances cholera toxin B subunit expression in transgenic plants and the plant-expressed protein binds GM1 receptors more efficiently
    • Mishra S, Yadav DK, Tuli R. Ubiquitin fusion enhances cholera toxin B subunit expression in transgenic plants and the plant-expressed protein binds GM1 receptors more efficiently. J. Biotechnol. 127, 95-108 (2006).
    • (2006) J. Biotechnol. , vol.127 , pp. 95-108
    • Mishra, S.1    Yadav, D.K.2    Tuli, R.3
  • 79
    • 33947315594 scopus 로고    scopus 로고
    • Elastin-like polypeptide fusions enhance the accumulation of recombinant proteins in tobacco leaves
    • Patel J, Zhu H, Menassa R, Gyenis L, Richman A, Brandle JE. Elastin-like polypeptide fusions enhance the accumulation of recombinant proteins in tobacco leaves. Transgenic Res. 16, 239-249.
    • Transgenic Res. , vol.16 , pp. 239-249
    • Patel, J.1    Zhu, H.2    Menassa, R.3    Gyenis, L.4    Richman, A.5    Brandle, J.E.6
  • 80
    • 33745199217 scopus 로고    scopus 로고
    • Immunological safety of vaccines: Facts hypothesis and allegations
    • Kaufmann SHE (Ed.). Wiley-VCH, Weinheim, Germany
    • Goldman M, Lambert P-H. Immunological safety of vaccines: facts hypothesis and allegations. In: Novel Vaccination Strategies. Kaufmann SHE (Ed.). Wiley-VCH, Weinheim, Germany, 595-611 (2004).
    • (2004) Novel Vaccination Strategies , pp. 595-611
    • Goldman, M.1    Lambert, P.-H.2
  • 81
    • 33344479476 scopus 로고    scopus 로고
    • Rapid, high-level production of hepatitis B core antigen in plant leaf and its immunogenicity in mice
    • Huang Z, Santi L, LePore K, Kilbourne J, Arntzen CJ, Mason HS. Rapid, high-level production of hepatitis B core antigen in plant leaf and its immunogenicity in mice. Vaccine 24, 2506-2513 (2006).
    • (2006) Vaccine , vol.24 , pp. 2506-2513
    • Huang, Z.1    Santi, L.2    Lepore, K.3    Kilbourne, J.4    Arntzen, C.J.5    Mason, H.S.6
  • 82
    • 40849140609 scopus 로고    scopus 로고
    • An efficient plant viral expression system generating orally immunogenic Norwalk virus-like particles
    • Santi L, Batchelora L, Huanga Z et al. An efficient plant viral expression system generating orally immunogenic Norwalk virus-like particles. Vaccine 26, 1846-1854.
    • Vaccine , vol.26 , pp. 1846-1854
    • Santi, L.1    Batchelora, L.2    Huanga, Z.3
  • 83
    • 55949124182 scopus 로고    scopus 로고
    • Influenza virus-like particles produced by transient expression in Nicotiana benthamiana induce a protective immune response against a lethal viral challenge in mice
    • D'Aoust MA, Lavoie PO, Couture MM et al. Influenza virus-like particles produced by transient expression in Nicotiana benthamiana induce a protective immune response against a lethal viral challenge in mice. Plant Biotechnol. J. 6, 930-940 (2008).
    • (2008) Plant Biotechnol. J. , vol.6 , pp. 930-940
    • D'Aoust, M.A.1    Lavoie, P.O.2    Couture, M.M.3
  • 84
    • 33745494115 scopus 로고    scopus 로고
    • Epitope presentation system based on cucumber mosaic virus coat protein expressed from a potato virus X-based vector
    • Natilla A, Hammond RW, Nemchinov LG. Epitope presentation system based on cucumber mosaic virus coat protein expressed from a potato virus X-based vector. Arch. Virol. 151, 1373-1386 (2006).
    • (2006) Arch. Virol. , vol.151 , pp. 1373-1386
    • Natilla, A.1    Hammond, R.W.2    Nemchinov, L.G.3
  • 85
    • 70349823197 scopus 로고    scopus 로고
    • Efficient generation of cowpea mosaic virus empty virus-like particles by the proteolytic processing of precursors in insect cells and plants
    • Saunders K, Sainsbury F, Lomonossoff GP. Efficient generation of cowpea mosaic virus empty virus-like particles by the proteolytic processing of precursors in insect cells and plants. Virology 393, 329-337 (2009).
    • (2009) Virology , vol.393 , pp. 329-337
    • Saunders, K.1    Sainsbury, F.2    Lomonossoff, G.P.3
  • 87
    • 70449389518 scopus 로고    scopus 로고
    • Models of antigen receptor activation in the design of vaccines
    • Molnar E, Dopfer EP, Deswal S, Schamel WW. Models of antigen receptor activation in the design of vaccines. Curr. Pharm. Des. 15, 3237-3248 (2009).
    • (2009) Curr. Pharm. Des. , vol.15 , pp. 3237-3248
    • Molnar, E.1    Dopfer, E.P.2    Deswal, S.3    Schamel, W.W.4
  • 88
    • 37349026910 scopus 로고    scopus 로고
    • Viral peptide immunogens: Current challenges and opportunities
    • Azizi A, Diaz-MitoForsyth M.A. Viral peptide immunogens: current challenges and opportunities. J. Pept. Sci. 13, 776-786 (2007).
    • (2007) J. Pept. Sci. , vol.13 , pp. 776-786
    • Azizi, A.1    Diaz-MitoForsyth, M.A.2
  • 90
    • 0033388724 scopus 로고    scopus 로고
    • Nine major HLA class i supertypes account for the vast preponderance of HLA-A and -B polymorphism
    • Sette A, Sidney J. Nine major HLA class I supertypes account for the vast preponderance of HLA-A and -B polymorphism. Immunogenetics 50, 201-212 (1999).
    • (1999) Immunogenetics , vol.50 , pp. 201-212
    • Sette, A.1    Sidney, J.2
  • 91
    • 0030793945 scopus 로고    scopus 로고
    • Presentation of heterologous peptides on plant viruses: Genetics, structure and function
    • Johnson J, Lin T, Lomonossoff G. Presentation of heterologous peptides on plant viruses: genetics, structure and function. Annu. Rev. Phytopathol. 35, 67-86 (1997).
    • (1997) Annu. Rev. Phytopathol. , vol.35 , pp. 67-86
    • Johnson, J.1    Lin, T.2    Lomonossoff, G.3
  • 92
    • 0033516507 scopus 로고    scopus 로고
    • Display of epitopes on the surface of Tobacco mosaic virus: Impact of charge and isoelectric point of the epitope on virus-host interaction
    • Bendahmane M, Koo M, Karrer E, Beachy RN. Display of epitopes on the surface of Tobacco mosaic virus: impact of charge and isoelectric point of the epitope on virus-host interaction. J. Mol. Biol. 290, 9-20 (1999).
    • (1999) J. Mol. Biol. , vol.290 , pp. 9-20
    • Bendahmane, M.1    Koo, M.2    Karrer, E.3    Beachy, R.N.4
  • 93
    • 33748333198 scopus 로고    scopus 로고
    • TMV-peptide fusion vaccines induce cell-mediated immune responses and tumor protection in two murine models
    • McCormick AA, Corbo TA, Wykoff- Clary S et al. TMV-peptide fusion vaccines induce cell-mediated immune responses and tumor protection in two murine models. Vaccine 24, 6414-6423 (2006).
    • (2006) Vaccine , vol.24 , pp. 6414-6423
    • McCormick, A.A.1    Corbo, T.A.2    Wykoff- Clary, S.3
  • 94
    • 33846596544 scopus 로고    scopus 로고
    • Morphology and stability changes of recombinant TMV particles caused by a cysteine residue in the foreign peptide fused to the coat protein
    • Li G, Jiang L, Li M et al. Morphology and stability changes of recombinant TMV particles caused by a cysteine residue in the foreign peptide fused to the coat protein. J. Virol. Methods 140, 212-217 (2007).
    • (2007) J. Virol. Methods , vol.140 , pp. 212-217
    • Li, G.1    Jiang, L.2    Li, M.3
  • 96
    • 33749065356 scopus 로고    scopus 로고
    • Peptide display on potato virus X: Molecular features of the coat protein- fused peptide affecting cell-to-cell and phloem movement of chimeric virus particles
    • Lico C, Capua no F, Renzone G et al. Peptide display on potato virus X: molecular features of the coat protein- fused peptide affecting cell-to-cell and phloem movement of chimeric virus particles. J. Gen. Virol. 87, 3103-3112 (2006).
    • (2006) J. Gen. Virol. , vol.87 , pp. 3103-3112
    • Lico, C.1    Capua No, F.2    Renzone, G.3
  • 97
    • 67650738556 scopus 로고    scopus 로고
    • Plant-produced potato virus X chimeric particles displaying an influenza virus- derived peptide activate specific CD8 + T cells in mice
    • Lico C , Mancini C , Ita lia ni P et al. Plant-produced potato virus X chimeric particles displaying an influenza virus- derived peptide activate specific CD8 + T cells in mice. Vaccine 27, 5069-5076 (2009).
    • (2009) Vaccine , vol.27 , pp. 5069-5076
    • Lico, C.1    Mancini, C.2    Ita Liani, P.3
  • 98
    • 77953999126 scopus 로고    scopus 로고
    • Production of antibodies in plants: Status after twenty years
    • De Muynck B, Navarre C, Boutry M. Production of antibodies in plants: status after twenty years. Plant Biotechnol. J. 8, 529-563 (2010).
    • (2010) Plant Biotechnol. J. , vol.8 , Issue.529-563
    • De Muynck, B.1    Navarre, C.2    Boutry, M.3
  • 99
    • 14744293469 scopus 로고    scopus 로고
    • Antibody processing and engineering in plants, and new strategies for vaccine production
    • Ma JK, Drake PM, Chargelegue D, Obregon P, Prada A. Antibody processing and engineering in plants, and new strategies for vaccine production. Vaccine 23, 1814-1818 (2005).
    • (2005) Vaccine , vol.23 , pp. 1814-1818
    • Ma, J.K.1    Drake, P.M.2    Chargelegue, D.3    Obregon, P.4    Prada, A.5
  • 100
    • 19444372752 scopus 로고    scopus 로고
    • Plant biopharming of monoclonal antibodies
    • Ko K, Koprowski H. Plant biopharming of monoclonal antibodies. Virus Res. 111, 93-100 (2005).
    • (2005) Virus Res. , vol.111 , pp. 93-100
    • Ko, K.1    Koprowski, H.2
  • 101
    • 33745015936 scopus 로고    scopus 로고
    • Plant-derived anti-Lewis y mAb exhibits biological activities for efficient immunotherapy against human cancer cells
    • Brodzik R, Glogowska M, Bandurska K et al. Plant-derived anti-Lewis Y mAb exhibits biological activities for efficient immunotherapy against human cancer cells. Proc. Natl Acad. Sci. USA 103, 8804-8809 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 8804-8809
    • Brodzik, R.1    Glogowska, M.2    Bandurska, K.3
  • 102
    • 20044364761 scopus 로고    scopus 로고
    • Human-derived, plant-produced monoclonal antibody for the treatment of anthrax
    • Hull AK, Criscuolo CJ, Mett V et al. Human-derived, plant-produced monoclonal antibody for the treatment of anthrax. Vaccine 23, 2082-2086 (2005).
    • (2005) Vaccine , vol.23 , pp. 2082-2086
    • Hull, A.K.1    Criscuolo, C.J.2    Mett, V.3
  • 103
    • 33645824134 scopus 로고    scopus 로고
    • Agroinjection of tomato fruits. A tool for rapid functional analysis of transgenes directly in fruit
    • Orzaez, D, Mirabel S, Wieland WH, Granell A. Agroinjection of tomato fruits. A tool for rapid functional analysis of transgenes directly in fruit. Plant Physiol. 140, 3-11 (2006).
    • (2006) Plant Physiol. , vol.140 , pp. 3-11
    • Orzaez, D.1    Mirabel, S.2    Wieland, W.H.3    Granell, A.4
  • 104
    • 0033613072 scopus 로고    scopus 로고
    • Transient expression of a tumor-specific single-chain fragment and a chimeric antibody in tobacco leaves
    • Vaquero C, Sack M, Chandler J et al. Transient expression of a tumor-specific single-chain fragment and a chimeric antibody in tobacco leaves. Proc. Natl Acad. Sci USA 96, 11128-11133 (1999).
    • (1999) Proc. Natl Acad. Sci USA , vol.96 , pp. 11128-11133
    • Vaquero, C.1    Sack, M.2    Chandler, J.3
  • 105
    • 65549122945 scopus 로고    scopus 로고
    • Transient co-expression for fast and high-yield production of antibodies with human-like N-glycans in plants
    • Vezina LP, Faye L, Lerouge P et al. Transient co-expression for fast and high-yield production of antibodies with human-like N-glycans in plants. Plant Biotechnol. J. 7, 442-455 (2009).
    • (2009) Plant Biotechnol. J. , vol.7 , pp. 442-455
    • Vezina, L.P.1    Faye, L.2    Lerouge, P.3
  • 106
    • 57649121662 scopus 로고    scopus 로고
    • Plant pharming of a full-sized, tumour- targeting antibody using different expression strategies
    • Villani MA, Morgun B, Brunetti P et al. Plant pharming of a full-sized, tumour- targeting antibody using different expression strategies. Plant Biotech. J. 7, 59-72 (2009).
    • (2009) Plant Biotech. J. , vol.7 , pp. 59-72
    • Valvano, M.A.1    Morgun, B.2    Brunetti, P.3
  • 107
    • 78149470963 scopus 로고    scopus 로고
    • Optimisation of the purification process of a tumour-targeting antibody produced in N. benthamiana using vacuum- agroinfiltration
    • DOI: 10.1007/s11248-010-9382-9389 Epub ahead of print
    • Lombardi R, Villani ME, Di Carli M, Brunetti P, Benvenuto E, Donini M. Optimisation of the purification process of a tumour-targeting antibody produced in N. benthamiana using vacuum- agroinfiltration. Transgenic Res. DOI: 10.1007/s11248-010-9382-9389 (2010) (Epub ahead of print)
    • (2010) Transgenic Res.
    • Lombardi, R.1    Villani, M.E.2    Di Carli, M.3    Brunetti, P.4    Benvenuto, E.5    Donini, M.6
  • 108
    • 77249090742 scopus 로고    scopus 로고
    • Monoclonal antibody produced in plants efficiently treats West Nile virus infection in mice
    • Lai H, Engle M, Fuchs A et al. Monoclonal antibody produced in plants efficiently treats West Nile virus infection in mice. Proc. Natl Acad. Sci. USA 107, 2419-2424 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 2419-2424
    • Lai, H.1    Engle, M.2    Fuchs, A.3
  • 109
    • 57749107463 scopus 로고    scopus 로고
    • Extremely high-level and rapid transient protein production in plants without the use of viral replication
    • Sainsbury F, Lomonossoff GP. Extremely high-level and rapid transient protein production in plants without the use of viral replication. Plant Physiol. 148, 1212-1218 (2008).
    • (2008) Plant Physiol. , vol.148 , pp. 1212-1218
    • Sainsbury, F.1    Lomonossoff, G.P.2
  • 110
    • 77949479819 scopus 로고    scopus 로고
    • High-level rapid production of full-size monoclonal antibodies in plants by a single-vector DNA replicon system
    • Huang Z, Phoolcharoen W, Lai H et al. High-level rapid production of full-size monoclonal antibodies in plants by a single-vector DNA replicon system. Biotechnol. Bioeng. 106, 9-17 (2010).
    • (2010) Biotechnol. Bioeng. , vol.106 , pp. 9-17
    • Huang, Z.1    Phoolcharoen, W.2    Lai, H.3
  • 111
    • 0037135676 scopus 로고    scopus 로고
    • Expression in plants and immunogenicity of plant virus-based experimental rabies vaccine
    • Yusibov V, Hooper DC, Spitsin SV et al. Expression in plants and immunogenicity of plant virus-based experimental rabies vaccine. Vaccine 20, 3155-3164 (2002).
    • (2002) Vaccine , vol.20 , pp. 3155-3164
    • Yusibov, V.1    Hooper, D.C.2    Spitsin, S.V.3
  • 112
    • 67849130904 scopus 로고    scopus 로고
    • Plant-based oral vaccines: Results of human trials
    • Tacket CC. Plant-based oral vaccines: results of human trials. Curr. Top. Microbiol. Immunol. 332, 103-117 (2009).
    • (2009) Curr. Top. Microbiol. Immunol. , vol.332 , pp. 103-117
    • Tacket, C.C.1
  • 113
    • 28444454488 scopus 로고    scopus 로고
    • A rice-based edible vaccine expressing multiple T cell epitopes induces oral tolerance for inhibition of Th2-mediated IgE responses
    • Takagi H, Hiroi T, Yang L et al. A rice-based edible vaccine expressing multiple T cell epitopes induces oral tolerance for inhibition of Th2-mediated IgE responses. Proc. Natl Acad. Sci. USA 102, 17525-17530 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 17525-17530
    • Takagi, H.1    Hiroi, T.2    Yang, L.3
  • 114
    • 0042635750 scopus 로고    scopus 로고
    • A plant-based allergy vaccine suppresses experimental asthma via an IFN-g and CD4+CD45RBlow T cell-dependent mechanism
    • Smart V, Foster PS, Rothenberg ME, Higgins TJ, Hogan SP. A plant-based allergy vaccine suppresses experimental asthma via an IFN-g and CD4+CD45RBlow T cell-dependent mechanism. J. Immunol. 171, 2116-2126 (2003).
    • (2003) J. Immunol. , vol.171 , pp. 2116-2126
    • Smart, V.1    Foster, P.S.2    Rothenberg, M.E.3    Higgins, T.J.4    Hogan, S.P.5
  • 115
    • 33645945885 scopus 로고    scopus 로고
    • Agrobacterium- mediated genetic transformation of plants: Biology and biotechnology
    • Tzfira T, Citovsky V. Agrobacterium- mediated genetic transformation of plants: biology and biotechnology. Curr. Opin. Biotechnol. 17, 1-8 (2006).
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 1-8
    • Tzfira, T.1    Citovsky, V.2
  • 116
    • 48649087304 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens caused bacteraemia does not lead to GFP gene expression in mouse organs
    • Petrunia IV, Frolova OY, Komarova TV et al. Agrobacterium tumefaciens caused bacteraemia does not lead to GFP gene expression in mouse organs. PLoS One 3, e2352 (2008).
    • (2008) PLoS One , vol.3
    • Petrunia, I.V.1    Frolova, O.Y.2    Komarova, T.V.3
  • 117
    • 77954013882 scopus 로고    scopus 로고
    • Plant-specific glycosylation patterns in the context of therapeutic protein production
    • Gomord V, Fitchette AC, Menu- Bouaouiche L et al. Plant-specific glycosylation patterns in the context of therapeutic protein production. Plant Biotechnol. J. 8, 564-587 (2010).
    • (2010) Plant Biotechnol. J. , vol.8 , pp. 564-587
    • Gomord, V.1    Fitchette, A.C.2    Menu- Bouaouiche, L.3
  • 118
    • 46949110898 scopus 로고    scopus 로고
    • Expression of HIV-1 antigens in plants as potential subunit vaccines
    • Meyers A, Chakauya E, Shephard E et al. Expression of HIV-1 antigens in plants as potential subunit vaccines. BMC Biotechnol. 8, 53 (2008).
    • (2008) BMC Biotechnol. , vol.8 , pp. 53
    • Meyers, A.1    Chakauya, E.2    Shephard, E.3
  • 119
    • 34248172560 scopus 로고    scopus 로고
    • Optimization of human papillomavirus type 16 (HPV-16) L1 expression in plants: Comparison of the suitability of different HPV-16 L1 gene variants and different cell-compartment localization
    • Maclean J, Koekemoer M, Olivier AJ et al. Optimization of human papillomavirus type 16 (HPV-16) L1 expression in plants: comparison of the suitability of different HPV-16 L1 gene variants and different cell-compartment localization. J. Gen. Virol. 88, 1460-1469 (2007).
    • (2007) J. Gen. Virol. , vol.88 , pp. 1460-1469
    • MacLean, J.1    Koekemoer, M.2    Olivier, A.J.3
  • 120
    • 14744296631 scopus 로고    scopus 로고
    • Plant based HIV-1 vaccine candidate: Tat protein produced in spinach
    • Karasev AV, Foulke S, Wellens C et al. Plant based HIV-1 vaccine candidate: Tat protein produced in spinach. Vaccine 23, 1875-1880 (2005).
    • (2005) Vaccine , vol.23 , pp. 1875-1880
    • Karasev, A.V.1    Foulke, S.2    Wellens, C.3
  • 121
    • 33745341751 scopus 로고    scopus 로고
    • Transient expression of human papillomavirus type 16 L1 protein in Nicotiana benthamiana using an infectious tobamovirus vector
    • Varsani A, Williamson AL, Stewart D, Rybicki EP. Transient expression of human papillomavirus type 16 L1 protein in Nicotiana benthamiana using an infectious tobamovirus vector. Virus Res. 120, 91-96 (2006).
    • (2006) Virus Res. , vol.120 , pp. 91-96
    • Varsani, A.1    Williamson, A.L.2    Stewart, D.3    Rybicki, E.P.4
  • 122
    • 34547819753 scopus 로고    scopus 로고
    • Production of dengue 2 envelope domain III in plant using TMV-based vector system
    • Saejung W, Fujiyama K, Takasaki T et al. Production of dengue 2 envelope domain III in plant using TMV-based vector system. Vaccine 25, 6646-6654. (2007).
    • (2007) Vaccine , vol.25 , pp. 6646-6654
    • Saejung, W.1    Fujiyama, K.2    Takasaki, T.3
  • 123
    • 66149190947 scopus 로고    scopus 로고
    • Plant-produced human growth hormone shows biological activity in a rat model
    • Rabindran S, Stevenson N, Roy G et al. Plant-produced human growth hormone shows biological activity in a rat model. Biotechnol. Prog. 25, 530-534 (2009).
    • (2009) Biotechnol. Prog. , vol.25 , pp. 530-534
    • Rabindran, S.1    Stevenson, N.2    Roy, G.3
  • 124
    • 34249860300 scopus 로고    scopus 로고
    • Smallpox subunit vaccine produced in planta confers protection in mice
    • Golovkin M, Spitsin S, Andrianov V et al. Smallpox subunit vaccine produced in planta confers protection in mice. Proc. Natl Acad. Sci. USA 104, 6864-6869 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 6864-6869
    • Golovkin, M.1    Spitsin, S.2    Andrianov, V.3
  • 125
    • 70449374925 scopus 로고    scopus 로고
    • Production and characterization of an orally immunogenic Plasmodium antigen in plants using a virus-based expression system
    • Webster DE, Wang L, Mulcair M et al. Production and characterization of an orally immunogenic Plasmodium antigen in plants using a virus-based expression system. Plant Biotechnol. J. 7, 1-10 (2009).
    • (2009) Plant Biotechnol. J. , vol.7 , pp. 1-10
    • Webster, D.E.1    Wang, L.2    Mulcair, M.3
  • 126
    • 33646199262 scopus 로고    scopus 로고
    • Expression of tuberculosis antigen ESAT-6 in Nicotiana tabacum using a potato virus X-based vector
    • Zelada AM, Calamante G, de la Paz Santangelo M et al. Expression of tuberculosis antigen ESAT-6 in Nicotiana tabacum using a potato virus X-based vector. Tuberculosis (Edinb.) 86, 263-267 (2006).
    • (2006) Tuberculosis (Edinb.) , vol.86 , pp. 263-267
    • Zelada, A.M.1    Calamante, G.2    De La Paz Santangelo, M.3
  • 128
    • 0035866318 scopus 로고    scopus 로고
    • Protection of rabbits against Rabbit hemorrhagic disease virus by immunization with the VP60 protein expressed in plants with a Potyvirus-based vector
    • Fernandez-Fernandez MR, Mourino M, Rivera J, Rodriguez F, Plana-Duran J, Garcia JA. Protection of rabbits against Rabbit hemorrhagic disease virus by immunization with the VP60 protein expressed in plants with a Potyvirus-based vector. Virology 280, 283-291, (2001).
    • (2001) Virology , vol.280 , pp. 283-291
    • Fernandez-Fernandez, M.R.1    Mourino, M.2    Rivera, J.3    Rodriguez, F.4    Plana-Duran, J.5    Garcia, J.A.6
  • 129
    • 0036645102 scopus 로고    scopus 로고
    • Plant-derived Human papillomavirus 16 E7 oncoprotein induces immune response and specific tumor protection
    • Franconi R, Di Bonito P, Dibello F et al. Plant-derived Human papillomavirus 16 E7 oncoprotein induces immune response and specific tumor protection. Cancer Res. 62, 3654-3658 (2002).
    • (2002) Cancer Res. , vol.62 , pp. 3654-3658
    • Franconi, R.1    Di Bonito, P.2    Dibello, F.3
  • 130
    • 10744229447 scopus 로고    scopus 로고
    • Bovine herpes virus gD protein produced in plants using a recombinant tobacco mosaic virus (TMV) vector possesses authentic antigenicity
    • Perez Filgueira DM, Zamorano PI, Dominguez MG et al. Bovine herpes virus gD protein produced in plants using a recombinant tobacco mosaic virus (TMV) vector possesses authentic antigenicity. Vaccine 21, 4201-4209 (2003).
    • (2003) Vaccine , vol.21 , pp. 4201-4209
    • Perez Filgueira, D.M.1    Zamorano, P.I.2    Dominguez, M.G.3
  • 132
    • 26244446912 scopus 로고    scopus 로고
    • Production of the main surface antigen of Toxoplasma gondii in tobacco leaves and analysis of its antigenicity and immunogenicity
    • Clemente M, Curilovic R, Sassone A, Zelada A, Angel SO, Mentaberry AN. Production of the main surface antigen of Toxoplasma gondii in tobacco leaves and analysis of its antigenicity and immunogenicity. Mol. Biotechnol. 30, 41-50 (2005).
    • (2005) Mol. Biotechnol. , vol.30 , pp. 41-50
    • Clemente, M.1    Curilovic, R.2    Sassone, A.3    Zelada, A.4    Angel, S.O.5    Mentaberry, A.N.6
  • 133
    • 33947574275 scopus 로고    scopus 로고
    • Immunogenicity of a subunit vaccine against Bacillus anthracis
    • Chichester JA, Musiychuk K, de la Rosa P et al. Immunogenicity of a subunit vaccine against Bacillus anthracis. Vaccine 25, 3111-3114 (2007).
    • (2007) Vaccine , vol.25 , pp. 3111-3114
    • Chichester, J.A.1    Musiychuk, K.2    De La Rosa, P.3
  • 134
    • 33947717551 scopus 로고    scopus 로고
    • Anti-cancer activity of plant-produced HPV16 E7 vaccine
    • Massa S, Franconi R, Brandi R et al. Anti-cancer activity of plant-produced HPV16 E7 vaccine. Vaccine 25, 3018-3021 (2007).
    • (2007) Vaccine , vol.25 , pp. 3018-3021
    • Massa, S.1    Franconi, R.2    Brandi, R.3
  • 135
    • 33947582603 scopus 로고    scopus 로고
    • A plant-produced plague vaccine candidate confers protection to monkeys
    • Mett V, Lyons J, Musiychuk K et al. A plant-produced plague vaccine candidate confers protection to monkeys. Vaccine 25, 3014-3017 (2007).
    • (2007) Vaccine , vol.25 , pp. 3014-3017
    • Mett, V.1    Lyons, J.2    Musiychuk, K.3
  • 136
    • 58549091833 scopus 로고    scopus 로고
    • Plant- derived hemagglutinin protects ferrets against challenge infection with the A/ Indonesia/ 05/05 strain of avian influenza
    • Shoji Y, Bi H, Musiychuk K et al. Plant- derived hemagglutinin protects ferrets against challenge infection with the A/ Indonesia/ 05/05 strain of avian influenza. Vaccine 27, 1087-1092 (2009).
    • (2009) Vaccine , vol.27 , pp. 1087-1092
    • Shoji, Y.1    Bi, H.2    Musiychuk, K.3
  • 137
    • 65549136839 scopus 로고    scopus 로고
    • Immunogenicity of hemagglutinin from A/Bar-headed Goose/Qinghai/1A/05 and A/Anhui/1/05 strains of H5N1 influenza viruses produced in Nicotiana benthamiana plants
    • Shoji Y, Farrance CE, Bi H et al. Immunogenicity of hemagglutinin from A/Bar-headed Goose/Qinghai/1A/05 and A/Anhui/1/05 strains of H5N1 influenza viruses produced in Nicotiana benthamiana plants. Vaccine 27, 3467-3470 (2009).
    • (2009) Vaccine , vol.27 , pp. 3467-3470
    • Shoji, Y.1    Farrance, C.E.2    Bi, H.3
  • 138
    • 59649121116 scopus 로고    scopus 로고
    • Immunological assessment of plant-derived avian flu H5/HA1 variants
    • Spitsin S, Andrianov V, Pogrebnyak N et al. Immunological assessment of plant-derived avian flu H5/HA1 variants. Vaccine 27, 1289-1292 (2009).
    • (2009) Vaccine , vol.27 , pp. 1289-1292
    • Spitsin, S.1    Andrianov, V.2    Pogrebnyak, N.3
  • 139
    • 0028122633 scopus 로고
    • Development of cowpea mosaic virus as a high-yielding system for the presentation of foreign peptides
    • Porta C, Spall VE, Loveleand J, Johnson JE, Barker PJ, Lomonossoff GP. Development of cowpea mosaic virus as a high-yielding system for the presentation of foreign peptides. Virology 202, 949-955 (1994).
    • (1994) Virology , vol.202 , pp. 949-955
    • Porta, C.1    Spall, V.E.2    Loveleand, J.3    Johnson, J.E.4    Barker, P.J.5    Lomonossoff, G.P.6
  • 140
    • 0030891738 scopus 로고    scopus 로고
    • Plant-derived vaccine protects target animals against a viral disease
    • Dalsgaard K, Uttenthal A, Jones GB et al. Plant-derived vaccine protects target animals against a viral disease. Nat. Biotechnol. 15, 248-252 (1997).
    • (1997) Nat. Biotechnol. , vol.15 , pp. 248-252
    • Dalsgaard, K.1    Uttenthal, A.2    Jones, G.B.3
  • 142
    • 0030951339 scopus 로고    scopus 로고
    • Antigens produced in plants by infection with chimeric plant viruses immunize against rabies virus and HIV-1
    • Yusibov V, Modelska A, Steplewski K et al. Antigens produced in plants by infection with chimeric plant viruses immunize against rabies virus and HIV-1. Proc. Natl Acad. Sci. USA 94, 5784-5788 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5784-5788
    • Yusibov, V.1    Modelska, A.2    Steplewski, K.3
  • 144
    • 0033537861 scopus 로고    scopus 로고
    • Immunogenicity of peptides derived from a fibronectin-binding protein of S. aureus expressed on two different plant viruses
    • Brennan FR, Jones TD, Longstaff M et al. Immunogenicity of peptides derived from a fibronectin-binding protein of S. aureus expressed on two different plant viruses. Vaccine 17, 1846-1857 (1999).
    • (1999) Vaccine , vol.17 , pp. 1846-1857
    • Brennan, F.R.1    Jones, T.D.2    Longstaff, M.3
  • 145
    • 0034009355 scopus 로고    scopus 로고
    • Immunization with a chimeric tobacco mosaic virus containing an epitope of outer membrane protein F of Pseudomonas aeruginosa provides protection against challenge with
    • Staczek J, Bendahmane M, Gilleland LB, Beachy RN, Gilleland HE Jr. Immunization with a chimeric tobacco mosaic virus containing an epitope of outer membrane protein F of Pseudomonas aeruginosa provides protection against challenge with P. aeruginosa. Vaccine 18, 2266-2274 (2000).
    • (2000) P. Aeruginosa. Vaccine , vol.18 , pp. 2266-2274
    • Staczek, J.1    Bendahmane, M.2    Gilleland, L.B.3    Beachy, R.N.4    Gilleland Jr., H.E.5
  • 146
    • 0035859281 scopus 로고    scopus 로고
    • Inactivated recombinant plant virus protects dogs from a lethal challenge with canine parvovirus
    • Langeveld JPM, Brennan FR, Martinez- Torrecuadrada JL et al. Inactivated recombinant plant virus protects dogs from a lethal challenge with canine parvovirus. Vaccine 19, 3661-3670 (2001).
    • (2001) Vaccine , vol.19 , pp. 3661-3670
    • Jpm, L.1    Brennan, F.R.2    Martinez-Torrecuadrada, J.L.3
  • 147
    • 0034881226 scopus 로고    scopus 로고
    • Chimeric plant virus particles as immunogens for inducing murine and human immune responses against human immunodeficiency virus type 1
    • Marusic C, Rizza P, Lattanzi L et al. Chimeric plant virus particles as immunogens for inducing murine and human immune responses against human immunodeficiency virus type 1. J. Virol. 75, 8434-8439 (2001).
    • (2001) J. Virol. , vol.75 , pp. 8434-8439
    • Marusic, C.1    Rizza, P.2    Lattanzi, L.3
  • 148
    • 0842330918 scopus 로고    scopus 로고
    • Cucumber mosaic virus as carrier of a hepatitis C virus-derived epitope
    • Natilla A, Piazzolla G, Nuzzaci M et al. Cucumber mosaic virus as carrier of a hepatitis C virus-derived epitope. Arch. Virol. 149, 137-154 (2004).
    • (2004) Arch. Virol. , vol.149 , pp. 137-154
    • Natilla, A.1    Piazzolla, G.2    Nuzzaci, M.3
  • 149
    • 14844320019 scopus 로고    scopus 로고
    • Peptide- based candidate vaccine against respiratory syncytial virus
    • Yusibov V, Mett V, Mett V et al. Peptide- based candidate vaccine against respiratory syncytial virus. Vaccine 23, 2261-2265 (2005).
    • (2005) Vaccine , vol.23 , pp. 2261-2265
    • Yusibov, V.1    Mett, V.2    Mett, V.3
  • 150
    • 33746950963 scopus 로고    scopus 로고
    • In planta production of two peptides of the Classical swine fever virus (CSFV) E2 glycoprotein fused to the coat protein of potato virus X
    • Marconi G, Albertini E, Barone P et al. In planta production of two peptides of the Classical swine fever virus (CSFV) E2 glycoprotein fused to the coat protein of potato virus X. BMC Biotechnol. 6, 29 (2006).
    • (2006) BMC Biotechnol. , vol.6 , pp. 29
    • Marconi, G.1    Albertini, E.2    Barone, P.3
  • 151
    • 33646256795 scopus 로고    scopus 로고
    • Modified tobacco mosaic virus particles as scaffolds for display of protein antigens for vaccine applications
    • Smith ML, Lindbo JA, Dillard-Telm S et al. Modified tobacco mosaic virus particles as scaffolds for display of protein antigens for vaccine applications. Virology 348, 475-488 (2006).
    • (2006) Virology , vol.348 , pp. 475-488
    • Smith, M.L.1    Lindbo, J.A.2    Dillard-Telm, S.3
  • 152
    • 70350755692 scopus 로고    scopus 로고
    • Cowpea mosaic virus chimeric particles bearing the ectodomain of matrix protein 2 (M2E) of the influenza A virus: Production and characterization
    • Meshcheryakova YA, Eldarov MA, Migunov AI et al. Cowpea mosaic virus chimeric particles bearing the ectodomain of matrix protein 2 (M2E) of the influenza A virus: production and characterization. Mol. Biol. 43, 685-694 (2009).
    • (2009) Mol. Biol. , vol.43 , pp. 685-694
    • Meshcheryakova, Y.A.1    Eldarov, M.A.2    Migunov, A.I.3
  • 153
    • 77950968711 scopus 로고    scopus 로고
    • In vitro stability of cucumber mosaic virus nanoparticles carrying a hepatitis C virus-derived epitope under simulated gastrointestinal conditions and in vivo efficacy of an edible vaccine
    • Nuzzaci M, Vitti A, Condelli V et al. In vitro stability of cucumber mosaic virus nanoparticles carrying a hepatitis C virus-derived epitope under simulated gastrointestinal conditions and in vivo efficacy of an edible vaccine. J. Virol. Meth. 165, 211-215 (2010).
    • (2010) J. Virol. Meth. , vol.165 , pp. 211-215
    • Nuzzaci, M.1    Vitti, A.2    Condelli, V.3
  • 154
    • 77952669353 scopus 로고    scopus 로고
    • Immunogenic properties of chimeric potato virus X particles displaying the hepatitis C virus hypervariable region i peptide R9
    • Uhde-Holzem K, Schlossera V, Viazov S, Fischer R, Commandeur U. Immunogenic properties of chimeric potato virus X particles displaying the hepatitis C virus hypervariable region I peptide R9. J. Virol. Meth. 166, 12-20 (2010).
    • (2010) J. Virol. Meth. , vol.166 , pp. 12-20
    • Uhde-Holzem, K.1    Schlossera, V.2    Viazov, S.3    Fischer, R.4    Commandeur, U.5
  • 157
    • 84925568306 scopus 로고    scopus 로고
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