메뉴 건너뛰기




Volumn 7, Issue 8, 2012, Pages

Production of a subunit vaccine candidate against porcine post-weaning diarrhea in high-biomass transplastomic tobacco

Author keywords

[No Author keywords available]

Indexed keywords

F4 RECEPTOR; PEPTIDE VACCINE; RECEPTOR; RECOMBINANT FAEG PROTEIN VACCINE; UNCLASSIFIED DRUG;

EID: 84864565209     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0042405     Document Type: Article
Times cited : (37)

References (92)
  • 1
    • 26044455874 scopus 로고    scopus 로고
    • Escherichia coli in postweaning diarrhea in pigs: an update on bacterial types, pathogenesis, and prevention strategies
    • Fairbrother JM, Nadeau E, Gyles CL, ((2005)) Escherichia coli in postweaning diarrhea in pigs: an update on bacterial types, pathogenesis, and prevention strategies. Anim Health Res Rev 6: 17-39.
    • (2005) Anim Health Res Rev , vol.6 , pp. 17-39
    • Fairbrother, J.M.1    Nadeau, E.2    Gyles, C.L.3
  • 2
    • 0001614178 scopus 로고
    • Postweaning Escherichia coli diarrhoea in pigs
    • In: Gyles CL, editor, Wallingford: CAB International
    • Hampson DJ (1994) Postweaning Escherichia coli diarrhoea in pigs. In: Gyles CL, editor. Escherichia coli in domestic animals and humans. Wallingford: CAB International. 171-191.
    • (1994) Escherichia coli in domestic animals and humans , pp. 171-191
    • Hampson, D.J.1
  • 3
    • 0000329563 scopus 로고    scopus 로고
    • Escherichia coli infections
    • In: Straw BE, D'Allaire S, Mengeling WL, Taylor DJ, editors, 8th Edition. Iowa: Iowa State University Press
    • Bertschinger HU, Fairbrother JM (1999) Escherichia coli infections. In: Straw BE, D'Allaire S, Mengeling WL, Taylor DJ, editors. Diseases of Swine, 8th Edition. Iowa: Iowa State University Press. 431-454.
    • (1999) Diseases of Swine , pp. 431-454
    • Bertschinger, H.U.1    Fairbrother, J.M.2
  • 4
    • 0021015034 scopus 로고
    • The effectiveness of inactivated vaccines applied parenterally to sows to control Escherichia coli diarrhea in piglets in an industrial fattening farm
    • Ciosek D, Truszczynski M, Jagodzinski M, ((1983)) The effectiveness of inactivated vaccines applied parenterally to sows to control Escherichia coli diarrhea in piglets in an industrial fattening farm. Comp Immunol Microbiol Infect Dis 6: 313-319.
    • (1983) Comp Immunol Microbiol Infect Dis , vol.6 , pp. 313-319
    • Ciosek, D.1    Truszczynski, M.2    Jagodzinski, M.3
  • 5
    • 0032934725 scopus 로고    scopus 로고
    • Receptor-dependent immune responses in pigs after oral immunization with F4 fimbriae
    • Van den Broeck W, Cox E, Goddeeris BM, ((1999)) Receptor-dependent immune responses in pigs after oral immunization with F4 fimbriae. Infect Immun 67: 520-526.
    • (1999) Infect Immun , vol.67 , pp. 520-526
    • van den Broeck, W.1    Cox, E.2    Goddeeris, B.M.3
  • 6
    • 0030273775 scopus 로고    scopus 로고
    • Molecular and structural aspects of fimbriae biosynthesis and assembly in Escherichia coli
    • Mol O, Oudega B, ((1996)) Molecular and structural aspects of fimbriae biosynthesis and assembly in Escherichia coli. FEMS Microbiol Rev 19: 25-52.
    • (1996) FEMS Microbiol Rev , vol.19 , pp. 25-52
    • Mol, O.1    Oudega, B.2
  • 7
    • 0033973105 scopus 로고    scopus 로고
    • The F4 fimbrial antigen of Escherichia coli and its receptors
    • Van den Broeck W, Cox E, Oudega B, Goddeeris BM, ((2000)) The F4 fimbrial antigen of Escherichia coli and its receptors. Vet Microbiol 71: 223-244.
    • (2000) Vet Microbiol , vol.71 , pp. 223-244
    • van den Broeck, W.1    Cox, E.2    Oudega, B.3    Goddeeris, B.M.4
  • 8
    • 70449646172 scopus 로고    scopus 로고
    • Structural and thermodynamic characterization of pre- and postpolymerization states in the F4 fimbrial subunit FaeG
    • Van Molle I, Moonens K, Garcia-Pino A, Buts L, De Kerpel M, et al. ((2009)) Structural and thermodynamic characterization of pre- and postpolymerization states in the F4 fimbrial subunit FaeG. J Mol Biol 394: 957-967.
    • (2009) J Mol Biol , vol.394 , pp. 957-967
    • van Molle, I.1    Moonens, K.2    Garcia-Pino, A.3    Buts, L.4    de Kerpel, M.5
  • 9
    • 4344654762 scopus 로고    scopus 로고
    • Conserved regions in the sequence of the F4 (K88) fimbrial adhesin FaeG suggest a donor strand mechanism in F4 assembly
    • Verdonck F, Cox E, Schepers E, Imberechts H, Joensuu J, et al. ((2004)) Conserved regions in the sequence of the F4 (K88) fimbrial adhesin FaeG suggest a donor strand mechanism in F4 assembly. Vet Microbiol 102: 215-225.
    • (2004) Vet Microbiol , vol.102 , pp. 215-225
    • Verdonck, F.1    Cox, E.2    Schepers, E.3    Imberechts, H.4    Joensuu, J.5
  • 10
    • 0020524989 scopus 로고
    • The nucleotide sequence of the K88ad protein subunit of porcine enterotoxigenic Escherichia coli
    • Gaastra W, Klemm P, Graaf FKd, ((1983)) The nucleotide sequence of the K88ad protein subunit of porcine enterotoxigenic Escherichia coli. FEMS Microbiol Lett 18: 177-183.
    • (1983) FEMS Microbiol Lett , vol.18 , pp. 177-183
    • Gaastra, W.1    Klemm, P.2    Graaf, F.K.3
  • 11
    • 0018386708 scopus 로고
    • Behavior of Escherichia coli K antigens K88ab, K88ac, and K88ad in immunoelectrophoresis, double diffusion, and hemagglutination
    • Guinee PA, Jansen WH, ((1979)) Behavior of Escherichia coli K antigens K88ab, K88ac, and K88ad in immunoelectrophoresis, double diffusion, and hemagglutination. Infect Immun 23: 700-705.
    • (1979) Infect Immun , vol.23 , pp. 700-705
    • Guinee, P.A.1    Jansen, W.H.2
  • 12
    • 0021742053 scopus 로고
    • The nucleotide sequence of the protein subunit of the K88ac fimbriae of porcine enterotoxigenic Escherichia coli
    • Josephsen J, Hansen F, Graaf FKd, Gaastra W, ((1984)) The nucleotide sequence of the protein subunit of the K88ac fimbriae of porcine enterotoxigenic Escherichia coli. FEMS Microbiol Lett 25: 301-306.
    • (1984) FEMS Microbiol Lett , vol.25 , pp. 301-306
    • Josephsen, J.1    Hansen, F.2    Graaf, F.K.3    Gaastra, W.4
  • 13
    • 0019585612 scopus 로고
    • The complete amino-acid sequence of the K88 antigen, a fimbrial protein from Escherichia coli
    • Klemm P, ((1981)) The complete amino-acid sequence of the K88 antigen, a fimbrial protein from Escherichia coli. Eur J Biochem 117: 617-627.
    • (1981) Eur J Biochem , vol.117 , pp. 617-627
    • Klemm, P.1
  • 14
    • 78651158362 scopus 로고
    • K Antigens K88ab(L) and K88ac(L) in E. Coli. A New O Antigen: 0147 and a New K Antigen: K89(B)
    • Orskov I, Orskov F, Sojka WJ, Wittig W, ((1964)) K Antigens K88ab(L) and K88ac(L) in E. Coli. A New O Antigen: 0147 and a New K Antigen: K89(B). Acta Pathol Microbiol Scand 62: 439-447.
    • (1964) Acta Pathol Microbiol Scand , vol.62 , pp. 439-447
    • Orskov, I.1    Orskov, F.2    Sojka, W.J.3    Wittig, W.4
  • 15
    • 33748423069 scopus 로고    scopus 로고
    • Adhesion of Escherichia coli K88ab fimbriae to porcine enterocytes: effect on enzymatic activities of the brush border, and cyclic AMP and GMP levels
    • Caloca MJ, Suarez S, ((2006)) Adhesion of Escherichia coli K88ab fimbriae to porcine enterocytes: effect on enzymatic activities of the brush border, and cyclic AMP and GMP levels. Comp Immunol Microbiol Infect Dis 29: 225-231.
    • (2006) Comp Immunol Microbiol Infect Dis , vol.29 , pp. 225-231
    • Caloca, M.J.1    Suarez, S.2
  • 16
    • 34249710368 scopus 로고    scopus 로고
    • Two specific sites for binding of K88ab Escherichia coli fimbriae to porcine intestinal brush border membranes
    • Caloca MJ, Suarez S, ((2007)) Two specific sites for binding of K88ab Escherichia coli fimbriae to porcine intestinal brush border membranes. Comp Immunol Microbiol Infect Dis 30: 187-195.
    • (2007) Comp Immunol Microbiol Infect Dis , vol.30 , pp. 187-195
    • Caloca, M.J.1    Suarez, S.2
  • 17
    • 0015458839 scopus 로고
    • Role of the K88 antigen in the pathogenesis of neonatal diarrhea caused by Escherichia coli in piglets
    • Jones GW, Rutter JM, ((1972)) Role of the K88 antigen in the pathogenesis of neonatal diarrhea caused by Escherichia coli in piglets. Infect Immun 6: 918-927.
    • (1972) Infect Immun , vol.6 , pp. 918-927
    • Jones, G.W.1    Rutter, J.M.2
  • 18
    • 34250338181 scopus 로고    scopus 로고
    • Screening of pigs resistant to F4 enterotoxigenic Escherichia coli (ETEC) infection
    • Rasschaert K, Verdonck F, Goddeeris BM, Duchateau L, Cox E, ((2007)) Screening of pigs resistant to F4 enterotoxigenic Escherichia coli (ETEC) infection. Vet Microbiol 123: 249-253.
    • (2007) Vet Microbiol , vol.123 , pp. 249-253
    • Rasschaert, K.1    Verdonck, F.2    Goddeeris, B.M.3    Duchateau, L.4    Cox, E.5
  • 19
    • 0026598765 scopus 로고
    • Characterization of the antigenic and adhesive properties of FaeG, the major subunit of K88 fimbriae
    • Bakker D, Willemsen PT, Simons LH, van Zijderveld FG, de Graaf FK, ((1992)) Characterization of the antigenic and adhesive properties of FaeG, the major subunit of K88 fimbriae. Mol Microbiol 6: 247-255.
    • (1992) Mol Microbiol , vol.6 , pp. 247-255
    • Bakker, D.1    Willemsen, P.T.2    Simons, L.H.3    van Zijderveld, F.G.4    de Graaf, F.K.5
  • 20
    • 33745143962 scopus 로고    scopus 로고
    • Glycosylated F4 (K88) fimbrial adhesin FaeG expressed in barley endosperm induces ETEC-neutralizing antibodies in mice
    • Joensuu JJ, Kotiaho M, Teeri TH, Valmu L, Nuutila AM, et al. ((2006)) Glycosylated F4 (K88) fimbrial adhesin FaeG expressed in barley endosperm induces ETEC-neutralizing antibodies in mice. Transgenic Res 15: 359-373.
    • (2006) Transgenic Res , vol.15 , pp. 359-373
    • Joensuu, J.J.1    Kotiaho, M.2    Teeri, T.H.3    Valmu, L.4    Nuutila, A.M.5
  • 21
    • 33344456812 scopus 로고    scopus 로고
    • F4 (K88) fimbrial adhesin FaeG expressed in alfalfa reduces F4+ enterotoxigenic Escherichia coli excretion in weaned piglets
    • Joensuu JJ, Verdonck F, Ehrstrom A, Peltola M, Siljander-Rasi H, et al. ((2006)) F4 (K88) fimbrial adhesin FaeG expressed in alfalfa reduces F4+ enterotoxigenic Escherichia coli excretion in weaned piglets. Vaccine 24: 2387-2394.
    • (2006) Vaccine , vol.24 , pp. 2387-2394
    • Joensuu, J.J.1    Verdonck, F.2    Ehrstrom, A.3    Peltola, M.4    Siljander-Rasi, H.5
  • 22
    • 33947244049 scopus 로고    scopus 로고
    • Comparison of immune responses in parenteral FaeG DNA primed pigs boosted orally with F4 protein or reimmunized with the DNA vaccine
    • Melkebeek V, Verdonck F, Goddeeris BM, Cox E, ((2007)) Comparison of immune responses in parenteral FaeG DNA primed pigs boosted orally with F4 protein or reimmunized with the DNA vaccine. Vet Immunol Immunopathol 116: 199-214.
    • (2007) Vet Immunol Immunopathol , vol.116 , pp. 199-214
    • Melkebeek, V.1    Verdonck, F.2    Goddeeris, B.M.3    Cox, E.4
  • 23
    • 33947165423 scopus 로고    scopus 로고
    • Protective immune response of bacterially-derived recombinant FaeG in piglets
    • Yahong H, Liang W, Pan A, Zhou Z, Wang Q, et al. ((2006)) Protective immune response of bacterially-derived recombinant FaeG in piglets. J Microbiol 44: 548-555.
    • (2006) J Microbiol , vol.44 , pp. 548-555
    • Yahong, H.1    Liang, W.2    Pan, A.3    Zhou, Z.4    Wang, Q.5
  • 24
    • 4644357706 scopus 로고    scopus 로고
    • Oral immunization of piglets with recombinant F4 fimbrial adhesin FaeG monomers induces a mucosal and systemic F4-specific immune response
    • Verdonck F, Cox E, Van der Stede Y, Goddeeris BM, ((2004)) Oral immunization of piglets with recombinant F4 fimbrial adhesin FaeG monomers induces a mucosal and systemic F4-specific immune response. Vaccine 22: 4291-4299.
    • (2004) Vaccine , vol.22 , pp. 4291-4299
    • Verdonck, F.1    Cox, E.2    van der Stede, Y.3    Goddeeris, B.M.4
  • 25
    • 0042324122 scopus 로고    scopus 로고
    • Production of FaeG, the major subunit of K88 fimbriae, in transgenic tobacco plants and its immunogenicity in mice
    • Huang Y, Liang W, Pan A, Zhou Z, Huang C, et al. ((2003)) Production of FaeG, the major subunit of K88 fimbriae, in transgenic tobacco plants and its immunogenicity in mice. Infect Immun 71: 5436-5439.
    • (2003) Infect Immun , vol.71 , pp. 5436-5439
    • Huang, Y.1    Liang, W.2    Pan, A.3    Zhou, Z.4    Huang, C.5
  • 26
    • 3943058951 scopus 로고    scopus 로고
    • Fimbrial subunit protein FaeG expressed in transgenic tobacco inhibits the binding of F4ac enterotoxigenic Escherichia coli to porcine enterocytes
    • Joensuu JJ, Kotiaho M, Riipi T, Snoeck V, Palva ET, et al. ((2004)) Fimbrial subunit protein FaeG expressed in transgenic tobacco inhibits the binding of F4ac enterotoxigenic Escherichia coli to porcine enterocytes. Transgenic Res 13: 295-298.
    • (2004) Transgenic Res , vol.13 , pp. 295-298
    • Joensuu, J.J.1    Kotiaho, M.2    Riipi, T.3    Snoeck, V.4    Palva, E.T.5
  • 27
    • 77955179888 scopus 로고    scopus 로고
    • Immunogenicity of recombinant F4 (K88) fimbrial adhesin FaeG expressed in tobacco chloroplast
    • Shen H, Qian B, Chen W, Liu Z, Yang L, et al. ((2010)) Immunogenicity of recombinant F4 (K88) fimbrial adhesin FaeG expressed in tobacco chloroplast. Acta Biochim Biophys Sin (Shanghai) 42: 558-567.
    • (2010) Acta Biochim Biophys Sin (Shanghai) , vol.42 , pp. 558-567
    • Shen, H.1    Qian, B.2    Chen, W.3    Liu, Z.4    Yang, L.5
  • 28
    • 34047118001 scopus 로고    scopus 로고
    • Chloroplasts assemble the major subunit FaeG of Escherichia coli F4 (K88) fimbriae to strand-swapped dimers
    • Van Molle I, Joensuu JJ, Buts L, Panjikar S, Kotiaho M, et al. ((2007)) Chloroplasts assemble the major subunit FaeG of Escherichia coli F4 (K88) fimbriae to strand-swapped dimers. J Mol Biol 368: 791-799.
    • (2007) J Mol Biol , vol.368 , pp. 791-799
    • van Molle, I.1    Joensuu, J.J.2    Buts, L.3    Panjikar, S.4    Kotiaho, M.5
  • 29
    • 0037472387 scopus 로고    scopus 로고
    • Vaccine antigen production in transgenic plants: strategies, gene constructs and perspectives
    • Sala F, Manuela Rigano M, Barbante A, Basso B, Walmsley AM, et al. ((2003)) Vaccine antigen production in transgenic plants: strategies, gene constructs and perspectives. Vaccine 21: 803-808.
    • (2003) Vaccine , vol.21 , pp. 803-808
    • Sala, F.1    Manuela Rigano, M.2    Barbante, A.3    Basso, B.4    Walmsley, A.M.5
  • 30
    • 0141706699 scopus 로고    scopus 로고
    • The production of recombinant pharmaceutical proteins in plants
    • Ma JK, Drake PM, Christou P, ((2003)) The production of recombinant pharmaceutical proteins in plants. Nat Rev Genet 4: 794-805.
    • (2003) Nat Rev Genet , vol.4 , pp. 794-805
    • Ma, J.K.1    Drake, P.M.2    Christou, P.3
  • 31
    • 23744514106 scopus 로고    scopus 로고
    • Molecular farming for new drugs and vaccines. Current perspectives on the production of pharmaceuticals in transgenic plants
    • Ma JK, Barros E, Bock R, Christou P, Dale PJ, et al. ((2005)) Molecular farming for new drugs and vaccines. Current perspectives on the production of pharmaceuticals in transgenic plants. EMBO Rep 6: 593-599.
    • (2005) EMBO Rep , vol.6 , pp. 593-599
    • Ma, J.K.1    Barros, E.2    Bock, R.3    Christou, P.4    Dale, P.J.5
  • 32
    • 33646193336 scopus 로고    scopus 로고
    • Plant-made vaccines: biotechnology and immunology in animal health
    • Rice J, Ainley WM, Shewen P, ((2005)) Plant-made vaccines: biotechnology and immunology in animal health. Anim Health Res Rev 6: 199-209.
    • (2005) Anim Health Res Rev , vol.6 , pp. 199-209
    • Rice, J.1    Ainley, W.M.2    Shewen, P.3
  • 35
    • 0035162968 scopus 로고    scopus 로고
    • Overexpression of the Bt cry2Aa2 operon in chloroplasts leads to formation of insecticidal crystals
    • De Cosa B, Moar W, Lee SB, Miller M, Daniell H, ((2001)) Overexpression of the Bt cry2Aa2 operon in chloroplasts leads to formation of insecticidal crystals. Nat Biotechnol 19: 71-74.
    • (2001) Nat Biotechnol , vol.19 , pp. 71-74
    • de Cosa, B.1    Moar, W.2    Lee, S.B.3    Miller, M.4    Daniell, H.5
  • 36
    • 0037440739 scopus 로고    scopus 로고
    • Expression of tetanus toxin Fragment C in tobacco chloroplasts
    • Tregoning JS, Nixon P, Kuroda H, Svab Z, Clare S, et al. ((2003)) Expression of tetanus toxin Fragment C in tobacco chloroplasts. Nucleic Acids Res 31: 1174-1179.
    • (2003) Nucleic Acids Res , vol.31 , pp. 1174-1179
    • Tregoning, J.S.1    Nixon, P.2    Kuroda, H.3    Svab, Z.4    Clare, S.5
  • 38
    • 55949120435 scopus 로고    scopus 로고
    • High-level expression of human immunodeficiency virus antigens from the tobacco and tomato plastid genomes
    • Zhou F, Badillo-Corona JA, Karcher D, Gonzalez-Rabade N, Piepenburg K, et al. ((2008)) High-level expression of human immunodeficiency virus antigens from the tobacco and tomato plastid genomes. Plant Biotechnol J 6: 897-913.
    • (2008) Plant Biotechnol J , vol.6 , pp. 897-913
    • Zhou, F.1    Badillo-Corona, J.A.2    Karcher, D.3    Gonzalez-Rabade, N.4    Piepenburg, K.5
  • 39
    • 58849157867 scopus 로고    scopus 로고
    • Exhaustion of the chloroplast protein synthesis capacity by massive expression of a highly stable protein antibiotic
    • Oey M, Lohse M, Kreikemeyer B, Bock R, ((2009)) Exhaustion of the chloroplast protein synthesis capacity by massive expression of a highly stable protein antibiotic. Plant Journal 57: 436-445.
    • (2009) Plant Journal , vol.57 , pp. 436-445
    • Oey, M.1    Lohse, M.2    Kreikemeyer, B.3    Bock, R.4
  • 40
    • 0037212098 scopus 로고    scopus 로고
    • Progress towards commercialization of plastid transformation technology
    • Maliga P, ((2003)) Progress towards commercialization of plastid transformation technology. Trends Biotechnol 21: 20-28.
    • (2003) Trends Biotechnol , vol.21 , pp. 20-28
    • Maliga, P.1
  • 41
    • 34147158443 scopus 로고    scopus 로고
    • Plastid biotechnology: prospects for herbicide and insect resistance, metabolic engineering and molecular farming
    • Bock R, ((2007)) Plastid biotechnology: prospects for herbicide and insect resistance, metabolic engineering and molecular farming. Curr Opin Biotechnol 18: 100-106.
    • (2007) Curr Opin Biotechnol , vol.18 , pp. 100-106
    • Bock, R.1
  • 42
    • 79955661319 scopus 로고    scopus 로고
    • Chloroplast-derived vaccines against human diseases: achievements, challenges and scopes
    • Lossl AG, Waheed MT, ((2011)) Chloroplast-derived vaccines against human diseases: achievements, challenges and scopes. Plant Biotechnol J 9: 527-539.
    • (2011) Plant Biotechnol J , vol.9 , pp. 527-539
    • Lossl, A.G.1    Waheed, M.T.2
  • 43
    • 79957924097 scopus 로고    scopus 로고
    • Plastid biotechnology for crop production: present status and future perspectives
    • Clarke JL, Daniell H, ((2011)) Plastid biotechnology for crop production: present status and future perspectives. Plant Mol Biol 76: 211-220.
    • (2011) Plant Mol Biol , vol.76 , pp. 211-220
    • Clarke, J.L.1    Daniell, H.2
  • 44
    • 34249860016 scopus 로고    scopus 로고
    • Determining the transgene containment level provided by chloroplast transformation
    • Ruf S, Karcher D, Bock R, ((2007)) Determining the transgene containment level provided by chloroplast transformation. Proc Natl Acad Sci USA 104: 6998-7002.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 6998-7002
    • Ruf, S.1    Karcher, D.2    Bock, R.3
  • 45
    • 34249860848 scopus 로고    scopus 로고
    • Exceptional transmission of plastids and mitochondria from the transplastomic pollen parent and its impact on transgene containment
    • Svab Z, Maliga P, ((2007)) Exceptional transmission of plastids and mitochondria from the transplastomic pollen parent and its impact on transgene containment. Proc Natl Acad Sci USA 104: 7003-7008.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 7003-7008
    • Svab, Z.1    Maliga, P.2
  • 46
    • 5644303930 scopus 로고    scopus 로고
    • Recombinant anti-hCG antibodies retained in the endoplasmic reticulum of transformed plants lack core-xylose and core-alpha(1,3)-fucose residues
    • Sriraman R, Bardor M, Sack M, Vaquero C, Faye L, et al. ((2004)) Recombinant anti-hCG antibodies retained in the endoplasmic reticulum of transformed plants lack core-xylose and core-alpha(1,3)-fucose residues. Plant Biotechnol J 2: 279-287.
    • (2004) Plant Biotechnol J , vol.2 , pp. 279-287
    • Sriraman, R.1    Bardor, M.2    Sack, M.3    Vaquero, C.4    Faye, L.5
  • 47
    • 34147153529 scopus 로고    scopus 로고
    • Production of biopharmaceuticals and vaccines in plants via the chloroplast genome
    • Daniell H, ((2006)) Production of biopharmaceuticals and vaccines in plants via the chloroplast genome. Biotechnol J 1: 1071-1079.
    • (2006) Biotechnol J , vol.1 , pp. 1071-1079
    • Daniell, H.1
  • 48
    • 14744286603 scopus 로고    scopus 로고
    • Chloroplast-derived vaccine antigens and other therapeutic proteins
    • Daniell H, Chebolu S, Kumar S, Singleton M, Falconer R, ((2005)) Chloroplast-derived vaccine antigens and other therapeutic proteins. Vaccine 23: 1779-1783.
    • (2005) Vaccine , vol.23 , pp. 1779-1783
    • Daniell, H.1    Chebolu, S.2    Kumar, S.3    Singleton, M.4    Falconer, R.5
  • 49
    • 77951975776 scopus 로고    scopus 로고
    • Solar-powered factories for new vaccines and antibiotics
    • Bock R, Warzecha H, ((2010)) Solar-powered factories for new vaccines and antibiotics. Trends Biotechnol 28: 246-252.
    • (2010) Trends Biotechnol , vol.28 , pp. 246-252
    • Bock, R.1    Warzecha, H.2
  • 50
    • 0000146626 scopus 로고    scopus 로고
    • An Agrobacterium-mediated transient gene expression system for intact leaves
    • Kapila J, De Rycke R, Van Montagu M, Angenon G, ((1997)) An Agrobacterium-mediated transient gene expression system for intact leaves. Plant Science 122: 101-108.
    • (1997) Plant Science , vol.122 , pp. 101-108
    • Kapila, J.1    de Rycke, R.2    van Montagu, M.3    Angenon, G.4
  • 51
    • 0037342553 scopus 로고    scopus 로고
    • An enhanced transient expression system in plants based on suppression of gene silencing by the p19 protein of tomato bushy stunt virus
    • Voinnet O, Rivas S, Mestre P, Baulcombe D, ((2003)) An enhanced transient expression system in plants based on suppression of gene silencing by the p19 protein of tomato bushy stunt virus. Plant Journal 33: 949-956.
    • (2003) Plant Journal , vol.33 , pp. 949-956
    • Voinnet, O.1    Rivas, S.2    Mestre, P.3    Baulcombe, D.4
  • 52
    • 75949109975 scopus 로고    scopus 로고
    • Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamiana
    • Joensuu JJ, Conley AJ, Lienemann M, Brandle JE, Linder MB, et al. ((2010)) Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamiana. Plant Physiol 152: 622-633.
    • (2010) Plant Physiol , vol.152 , pp. 622-633
    • Joensuu, J.J.1    Conley, A.J.2    Lienemann, M.3    Brandle, J.E.4    Linder, M.B.5
  • 53
    • 33747134398 scopus 로고    scopus 로고
    • Expression of viral capsid protein antigen against Epstein-Barr virus in plastids of Nicotiana tabacum cv. SR1
    • Lee MY, Zhou Y, Lung RW, Chye ML, Yip WK, et al. ((2006)) Expression of viral capsid protein antigen against Epstein-Barr virus in plastids of Nicotiana tabacum cv. SR1. Biotechnol Bioeng 94: 1129-1137.
    • (2006) Biotechnol Bioeng , vol.94 , pp. 1129-1137
    • Lee, M.Y.1    Zhou, Y.2    Lung, R.W.3    Chye, M.L.4    Yip, W.K.5
  • 54
    • 77950526756 scopus 로고    scopus 로고
    • The role of heterologous chloroplast sequence elements in transgene integration and expression
    • Ruhlman T, Verma D, Samson N, Daniell H, ((2010)) The role of heterologous chloroplast sequence elements in transgene integration and expression. Plant Physiol 152: 2088-2104.
    • (2010) Plant Physiol , vol.152 , pp. 2088-2104
    • Ruhlman, T.1    Verma, D.2    Samson, N.3    Daniell, H.4
  • 55
    • 62149100748 scopus 로고    scopus 로고
    • High-level expression of active human alpha1-antitrypsin in transgenic tobacco chloroplasts
    • Nadai M, Bally J, Vitel M, Job C, Tissot G, et al. ((2009)) High-level expression of active human alpha1-antitrypsin in transgenic tobacco chloroplasts. Transgenic Res 18: 173-183.
    • (2009) Transgenic Res , vol.18 , pp. 173-183
    • Nadai, M.1    Bally, J.2    Vitel, M.3    Job, C.4    Tissot, G.5
  • 56
    • 36349016215 scopus 로고    scopus 로고
    • Identification of a plastid intercistronic expression element (IEE) facilitating the expression of stable translatable monocistronic mRNAs from operons
    • Zhou F, Karcher D, Bock R, ((2007)) Identification of a plastid intercistronic expression element (IEE) facilitating the expression of stable translatable monocistronic mRNAs from operons. Plant Journal 52: 961-972.
    • (2007) Plant Journal , vol.52 , pp. 961-972
    • Zhou, F.1    Karcher, D.2    Bock, R.3
  • 57
    • 0028939306 scopus 로고
    • Chloroplast rRNA transcription from structurally different tandem promoters: an additional novel-type promoter
    • Vera A, Sugiura M, ((1995)) Chloroplast rRNA transcription from structurally different tandem promoters: an additional novel-type promoter. Curr Genet 27: 280-284.
    • (1995) Curr Genet , vol.27 , pp. 280-284
    • Vera, A.1    Sugiura, M.2
  • 58
    • 79954586079 scopus 로고    scopus 로고
    • Recombinant protein production in a variety of Nicotiana hosts: a comparative analysis
    • Conley AJ, Zhu H, Le LC, Jevnikar AM, Lee BH, et al. ((2011)) Recombinant protein production in a variety of Nicotiana hosts: a comparative analysis. Plant Biotechnol J 9: 434-444.
    • (2011) Plant Biotechnol J , vol.9 , pp. 434-444
    • Conley, A.J.1    Zhu, H.2    Le, L.C.3    Jevnikar, A.M.4    Lee, B.H.5
  • 59
    • 0035707558 scopus 로고    scopus 로고
    • A self-contained system for the field production of plant recombinant interleukin-10
    • Menassa R, Nguyen V, Jevnikar A, Brandle J, ((2001)) A self-contained system for the field production of plant recombinant interleukin-10. Mol Breed 8: 177-185.
    • (2001) Mol Breed , vol.8 , pp. 177-185
    • Menassa, R.1    Nguyen, V.2    Jevnikar, A.3    Brandle, J.4
  • 60
    • 34249803206 scopus 로고    scopus 로고
    • Field production and functional evaluation of chloroplast-derived interferon-alpha2b
    • Arlen PA, Falconer R, Cherukumilli S, Cole A, Cole AM, et al. ((2007)) Field production and functional evaluation of chloroplast-derived interferon-alpha2b. Plant Biotechnol J 5: 511-525.
    • (2007) Plant Biotechnol J , vol.5 , pp. 511-525
    • Arlen, P.A.1    Falconer, R.2    Cherukumilli, S.3    Cole, A.4    Cole, A.M.5
  • 61
    • 55949087097 scopus 로고    scopus 로고
    • Plastid transformation of high-biomass tobacco variety Maryland Mammoth for production of human immunodeficiency virus type 1 (HIV-1) p24 antigen
    • McCabe MS, Klaas M, Gonzalez-Rabade N, Poage M, Badillo-Corona JA, et al. ((2008)) Plastid transformation of high-biomass tobacco variety Maryland Mammoth for production of human immunodeficiency virus type 1 (HIV-1) p24 antigen. Plant Biotechnol J 6: 914-929.
    • (2008) Plant Biotechnol J , vol.6 , pp. 914-929
    • McCabe, M.S.1    Klaas, M.2    Gonzalez-Rabade, N.3    Poage, M.4    Badillo-Corona, J.A.5
  • 62
    • 34548396828 scopus 로고    scopus 로고
    • Expression of thermostable microbial cellulases in the chloroplasts of nicotine-free tobacco
    • Yu LX, Gray BN, Rutzke CJ, Walker LP, Wilson DB, et al. ((2007)) Expression of thermostable microbial cellulases in the chloroplasts of nicotine-free tobacco. J Biotechnol 131: 362-369.
    • (2007) J Biotechnol , vol.131 , pp. 362-369
    • Yu, L.X.1    Gray, B.N.2    Rutzke, C.J.3    Walker, L.P.4    Wilson, D.B.5
  • 63
    • 79953792539 scopus 로고    scopus 로고
    • Recombinant protein expression in Nicotiana
    • Matoba N, Davis KR, Palmer KE, ((2011)) Recombinant protein expression in Nicotiana. Methods Mol Biol 701: 199-219.
    • (2011) Methods Mol Biol , vol.701 , pp. 199-219
    • Matoba, N.1    Davis, K.R.2    Palmer, K.E.3
  • 64
    • 0035979785 scopus 로고    scopus 로고
    • Expression of the native cholera toxin B subunit gene and assembly as functional oligomers in transgenic tobacco chloroplasts
    • Daniell H, Lee SB, Panchal T, Wiebe PO, ((2001)) Expression of the native cholera toxin B subunit gene and assembly as functional oligomers in transgenic tobacco chloroplasts. J Mol Biol 311: 1001-1009.
    • (2001) J Mol Biol , vol.311 , pp. 1001-1009
    • Daniell, H.1    Lee, S.B.2    Panchal, T.3    Wiebe, P.O.4
  • 65
    • 0035193462 scopus 로고    scopus 로고
    • Expression of an antimicrobial peptide via the chloroplast genome to control phytopathogenic bacteria and fungi
    • DeGray G, Rajasekaran K, Smith F, Sanford J, Daniell H, ((2001)) Expression of an antimicrobial peptide via the chloroplast genome to control phytopathogenic bacteria and fungi. Plant Physiol 127: 852-862.
    • (2001) Plant Physiol , vol.127 , pp. 852-862
    • DeGray, G.1    Rajasekaran, K.2    Smith, F.3    Sanford, J.4    Daniell, H.5
  • 66
    • 0033514914 scopus 로고    scopus 로고
    • Overexpression of the Bacillus thuringiensis (Bt) Cry2Aa2 protein in chloroplasts confers resistance to plants against susceptible and Bt-resistant insects
    • Kota M, Daniell H, Varma S, Garczynski SF, Gould F, et al. ((1999)) Overexpression of the Bacillus thuringiensis (Bt) Cry2Aa2 protein in chloroplasts confers resistance to plants against susceptible and Bt-resistant insects. Proc Natl Acad Sci USA 96: 1840-1845.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1840-1845
    • Kota, M.1    Daniell, H.2    Varma, S.3    Garczynski, S.F.4    Gould, F.5
  • 67
    • 79952296790 scopus 로고    scopus 로고
    • Selection of Shine-Dalgarno sequences in plastids
    • Drechsel O, Bock R, ((2011)) Selection of Shine-Dalgarno sequences in plastids. Nucleic Acids Res 39: 1427-1438.
    • (2011) Nucleic Acids Res , vol.39 , pp. 1427-1438
    • Drechsel, O.1    Bock, R.2
  • 68
    • 85169106486 scopus 로고    scopus 로고
    • A chloroplast transgenic approach to hyper-express and purify Human Serum Albumin, a protein highly susceptible to proteolytic degradation
    • Fernandez-San Millan A, Mingo-Castel A, Miller M, Daniell H, ((2003)) A chloroplast transgenic approach to hyper-express and purify Human Serum Albumin, a protein highly susceptible to proteolytic degradation. Plant Biotechnol J 1: 71-79.
    • (2003) Plant Biotechnol J , vol.1 , pp. 71-79
    • Fernandez-San Millan, A.1    Mingo-Castel, A.2    Miller, M.3    Daniell, H.4
  • 69
    • 0032837715 scopus 로고    scopus 로고
    • In vivo analysis of plastid psbA, rbcL and rpl32 UTR elements by chloroplast transformation: tobacco plastid gene expression is controlled by modulation of transcript levels and translation efficiency
    • Eibl C, Zou Z, Beck a, Kim M, Mullet J, et al. ((1999)) In vivo analysis of plastid psbA, rbcL and rpl32 UTR elements by chloroplast transformation: tobacco plastid gene expression is controlled by modulation of transcript levels and translation efficiency. Plant Journal 19: 333-345.
    • (1999) Plant Journal , vol.19 , pp. 333-345
    • Eibl, C.1    Zou, Z.2    Beck, A.3    Kim, M.4    Mullet, J.5
  • 70
    • 0027395945 scopus 로고
    • Accumulation of D1 polypeptide in tobacco plastids is regulated via the untranslated region of the psbA mRNA
    • Staub JM, Maliga P, ((1993)) Accumulation of D1 polypeptide in tobacco plastids is regulated via the untranslated region of the psbA mRNA. EMBO J 12: 601-606.
    • (1993) EMBO J , vol.12 , pp. 601-606
    • Staub, J.M.1    Maliga, P.2
  • 71
    • 0028518530 scopus 로고
    • Translation of psbA mRNA is regulated by light via the 5′-untranslated region in tobacco plastids
    • Staub JM, Maliga P, ((1994)) Translation of psbA mRNA is regulated by light via the 5′-untranslated region in tobacco plastids. Plant Journal 6: 547-553.
    • (1994) Plant Journal , vol.6 , pp. 547-553
    • Staub, J.M.1    Maliga, P.2
  • 72
    • 43449123620 scopus 로고    scopus 로고
    • High-density seedling expression system for the production of bioactive human cardiotrophin-1, a potential therapeutic cytokine, in transgenic tobacco chloroplasts
    • Farran I, Rio-Manterola F, Iniguez M, Garate S, Prieto J, et al. ((2008)) High-density seedling expression system for the production of bioactive human cardiotrophin-1, a potential therapeutic cytokine, in transgenic tobacco chloroplasts. Plant Biotechnol J 6: 516-527.
    • (2008) Plant Biotechnol J , vol.6 , pp. 516-527
    • Farran, I.1    Rio-Manterola, F.2    Iniguez, M.3    Garate, S.4    Prieto, J.5
  • 73
    • 0033959891 scopus 로고    scopus 로고
    • Translation of chloroplast psbA mRNA is modulated in the light by counteracting oxidizing and reducing activities
    • Trebitsh T, Levitan A, Sofer A, Danon A, ((2000)) Translation of chloroplast psbA mRNA is modulated in the light by counteracting oxidizing and reducing activities. Mol Cell Biol 20: 1116-1123.
    • (2000) Mol Cell Biol , vol.20 , pp. 1116-1123
    • Trebitsh, T.1    Levitan, A.2    Sofer, A.3    Danon, A.4
  • 74
    • 33746876406 scopus 로고    scopus 로고
    • Accumulation of hEGF and hEGF-fusion proteins in chloroplast-transformed tobacco plants is higher in the dark than in the light
    • Wirth S, Segretin ME, Mentaberry A, Bravo-Almonacid F, ((2006)) Accumulation of hEGF and hEGF-fusion proteins in chloroplast-transformed tobacco plants is higher in the dark than in the light. J Biotechnol 125: 159-172.
    • (2006) J Biotechnol , vol.125 , pp. 159-172
    • Wirth, S.1    Segretin, M.E.2    Mentaberry, A.3    Bravo-Almonacid, F.4
  • 75
    • 0001237853 scopus 로고    scopus 로고
    • Mucosal immune responses: An overview
    • In: Orga PL, Mestecky J, Lamm ME, Strober W, Bienenstock J, et al., editors. editors, 2nd Edition. San Diego: Academic Press
    • McGhee JR, Lamm ML, Strober W (1999) Mucosal immune responses: An overview. In: Orga PL, Mestecky J, Lamm ME, Strober W, Bienenstock J, et al., editors. editors. Mucosal Immunology, 2nd Edition. San Diego: Academic Press. 485-506.
    • (1999) Mucosal Immunology , pp. 485-506
    • McGhee, J.R.1    Lamm, M.L.2    Strober, W.3
  • 76
    • 0346735302 scopus 로고    scopus 로고
    • Gastrointestinal transit time of nondisintegrating radio-opaque pellets in suckling and recently weaned piglets
    • Snoeck V, Huyghebaert N, Cox E, Vermeire A, Saunders J, et al. ((2004)) Gastrointestinal transit time of nondisintegrating radio-opaque pellets in suckling and recently weaned piglets. J Control Release 94: 143-153.
    • (2004) J Control Release , vol.94 , pp. 143-153
    • Snoeck, V.1    Huyghebaert, N.2    Cox, E.3    Vermeire, A.4    Saunders, J.5
  • 77
    • 78650678024 scopus 로고    scopus 로고
    • Assessment of gastrointestinal pH, fluid and lymphoid tissue in the guinea pig, rabbit and pig, and implications for their use in drug development
    • Merchant HA, McConnell EL, Liu F, Ramaswamy C, Kulkarni RP, et al. ((2011)) Assessment of gastrointestinal pH, fluid and lymphoid tissue in the guinea pig, rabbit and pig, and implications for their use in drug development. European Journal of Pharmaceutical Sciences 42: 3-10.
    • (2011) European Journal of Pharmaceutical Sciences , vol.42 , pp. 3-10
    • Merchant, H.A.1    McConnell, E.L.2    Liu, F.3    Ramaswamy, C.4    Kulkarni, R.P.5
  • 78
    • 0027509419 scopus 로고
    • Upper gastrointestinal pH in seventy-nine healthy, elderly, North American men and women
    • Russell TL, Berardi RR, Barnett JL, Dermentzoglou LC, Jarvenpaa KM, et al. ((1993)) Upper gastrointestinal pH in seventy-nine healthy, elderly, North American men and women. Pharm Res 10: 187-196.
    • (1993) Pharm Res , vol.10 , pp. 187-196
    • Russell, T.L.1    Berardi, R.R.2    Barnett, J.L.3    Dermentzoglou, L.C.4    Jarvenpaa, K.M.5
  • 80
    • 52949095018 scopus 로고    scopus 로고
    • The polymeric stability of the Escherichia coli F4 (K88) fimbriae enhances its mucosal immunogenicity following oral immunization
    • Verdonck F, Joensuu JJ, Stuyven E, De Meyer J, Muilu M, et al. ((2008)) The polymeric stability of the Escherichia coli F4 (K88) fimbriae enhances its mucosal immunogenicity following oral immunization. Vaccine 26: 5728-5735.
    • (2008) Vaccine , vol.26 , pp. 5728-5735
    • Verdonck, F.1    Joensuu, J.J.2    Stuyven, E.3    de Meyer, J.4    Muilu, M.5
  • 81
    • 0032888146 scopus 로고    scopus 로고
    • Receptor-specific binding of purified F4 to isolated villi
    • Van den Broeck W, Cox E, Goddeeris BM, ((1999)) Receptor-specific binding of purified F4 to isolated villi. Vet Microbiol 68: 255-263.
    • (1999) Vet Microbiol , vol.68 , pp. 255-263
    • van den Broeck, W.1    Cox, E.2    Goddeeris, B.M.3
  • 82
    • 0036211238 scopus 로고    scopus 로고
    • F4 receptor-independent priming of the systemic immune system of pigs by low oral doses of F4 fimbriae
    • Van den Broeck W, Bouchaut H, Cox E, Goddeeris BM, ((2002)) F4 receptor-independent priming of the systemic immune system of pigs by low oral doses of F4 fimbriae. Vet Immunol Immunopathol 85: 171-178.
    • (2002) Vet Immunol Immunopathol , vol.85 , pp. 171-178
    • van den Broeck, W.1    Bouchaut, H.2    Cox, E.3    Goddeeris, B.M.4
  • 83
    • 33845793938 scopus 로고    scopus 로고
    • Therapeutic effectiveness of orally administered transgenic low-alkaloid tobacco expressing human interleukin-10 in a mouse model of colitis
    • Menassa R, Du C, Yin ZQ, Ma S, Poussier P, et al. ((2007)) Therapeutic effectiveness of orally administered transgenic low-alkaloid tobacco expressing human interleukin-10 in a mouse model of colitis. Plant Biotechnol J 5: 50-59.
    • (2007) Plant Biotechnol J , vol.5 , pp. 50-59
    • Menassa, R.1    Du, C.2    Yin, Z.Q.3    Ma, S.4    Poussier, P.5
  • 84
    • 0034979060 scopus 로고    scopus 로고
    • A modified Rpl3 gene from rice confers tolerance of the Fusarium graminearum mycotoxin deoxynivalenol to transgenic tobacco
    • Harris LJ, Gleddie SC, ((2001)) A modified Rpl3 gene from rice confers tolerance of the Fusarium graminearum mycotoxin deoxynivalenol to transgenic tobacco. Physiol Mol Plant Pathol 58: 173-181.
    • (2001) Physiol Mol Plant Pathol , vol.58 , pp. 173-181
    • Harris, L.J.1    Gleddie, S.C.2
  • 85
    • 0025188017 scopus 로고
    • Stable transformation of plastids in higher plants
    • Svab Z, Hajdukiewicz P, Maliga P, ((1990)) Stable transformation of plastids in higher plants. Proc Natl Acad Sci USA 87: 8526-8530.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 8526-8530
    • Svab, Z.1    Hajdukiewicz, P.2    Maliga, P.3
  • 86
    • 42049111811 scopus 로고    scopus 로고
    • A protocol for expression of foreign genes in chloroplasts
    • Verma D, Samson NP, Koya V, Daniell H, ((2008)) A protocol for expression of foreign genes in chloroplasts. Nat Protocols 3: 739-758.
    • (2008) Nat Protocols , vol.3 , pp. 739-758
    • Verma, D.1    Samson, N.P.2    Koya, V.3    Daniell, H.4
  • 87
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, ((1976)) A rapid and sensitive method for the quantitation 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.M.1
  • 88
    • 84864542565 scopus 로고
    • The United States Pharmacopeia, Simulated, TS. USP XXII, N-F XVII. Rockville, MD: United States Pharmacopeial Convention, Inc
    • The United States Pharmacopeia (1990) Gastric Fluid, Simulated, TS. USP XXII, N-F XVII. Rockville, MD: United States Pharmacopeial Convention, Inc.
    • (1990) Gastric Fluid
  • 89
    • 84864533476 scopus 로고    scopus 로고
    • The United States Pharmacopeia, Simulated, TS. USP 34, NF 29, V. 1. Rockville, MD: United States Pharmacopeial Convention, Inc
    • The United States Pharmacopeia (2011) Gastric Fluid, Simulated, TS. USP 34, NF 29, V. 1. Rockville, MD: United States Pharmacopeial Convention, Inc. 968.
    • (2011) Gastric Fluid , pp. 968
  • 90
    • 84864533480 scopus 로고    scopus 로고
    • The United States Pharmacopeia, USP 34, NF 29, V. 3. Rockville, MD: United States Pharmacopeial Convention, Inc
    • The United States Pharmacopeia (2011) Pancreatin. USP 34, NF 29, V. 3. Rockville, MD: United States Pharmacopeial Convention, Inc. 3803-3805.
    • (2011) Pancreatin , pp. 3803-3805
  • 91
    • 84864533479 scopus 로고    scopus 로고
    • The United States Pharmacopeia, Simulated, TS. USP 34, NF 29, V. 1. Rockville, MD: United States Pharmacopeial Convention, Inc
    • The United States Pharmacopeia (2011) Intestinal Fluid, Simulated, TS. USP 34, NF 29, V. 1. Rockville, MD: United States Pharmacopeial Convention, Inc. 969.
    • (2011) Intestinal Fluid , pp. 969
  • 92
    • 0027476007 scopus 로고
    • Comparison of the in vitro adhesion of K88, K99, F41 and P987 positive Escherichia coli to intestinal villi of 4- to 5-week-old pigs
    • Cox E, Houvenaghel A, ((1993)) Comparison of the in vitro adhesion of K88, K99, F41 and P987 positive Escherichia coli to intestinal villi of 4- to 5-week-old pigs. Vet Microbiol 34: 7-18.
    • (1993) Vet Microbiol , vol.34 , pp. 7-18
    • Cox, E.1    Houvenaghel, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.