메뉴 건너뛰기




Volumn 28, Issue 6, 2008, Pages 381-391

Expression of bioactive single-chain murine IL-12 in transgenic plants

Author keywords

[No Author keywords available]

Indexed keywords

GAMMA INTERFERON; GLYCAN DERIVATIVE; GLYCOPROTEIN; HETERODIMER; INTERLEUKIN 12; INTERLEUKIN 12P35; INTERLEUKIN 12P40; SIGNAL PEPTIDE;

EID: 46449102360     PISSN: 10799907     EISSN: None     Source Type: Journal    
DOI: 10.1089/jir.2007.0129     Document Type: Article
Times cited : (19)

References (52)
  • 1
    • 0037695239 scopus 로고    scopus 로고
    • Intranasal vaccination using interleukin-12 and cholera toxin subunit B as adjuvants to enhance mucosal and systemic immunity to human immunodeficiency virus type 1 glycoproteins
    • Albu DI, Jones-Trower A, Woron AM, Stellrecht K, Broder CC, Metzger DW. 2003. Intranasal vaccination using interleukin-12 and cholera toxin subunit B as adjuvants to enhance mucosal and systemic immunity to human immunodeficiency virus type 1 glycoproteins. J Virol 77:5589-5597.
    • (2003) J Virol , vol.77 , pp. 5589-5597
    • Albu, D.I.1    Jones-Trower, A.2    Woron, A.M.3    Stellrecht, K.4    Broder, C.C.5    Metzger, D.W.6
  • 2
    • 0030751570 scopus 로고    scopus 로고
    • Construction and biological characterization of an interleukin-12 fusion protein (Flexi-12): Delivery to acute myeloid leukemic blasts using adeno-associated virus
    • Anderson R, Macdonald I, Corbett T, Hacking G, Lowdel, MW, Prentice HG. 1997. Construction and biological characterization of an interleukin-12 fusion protein (Flexi-12): delivery to acute myeloid leukemic blasts using adeno-associated virus. Hum Gene Ther 8:1125-1135.
    • (1997) Hum Gene Ther , vol.8 , pp. 1125-1135
    • Anderson, R.1    Macdonald, I.2    Corbett, T.3    Hacking, G.4    Lowdel, M.W.5    Prentice, H.G.6
  • 3
    • 0035798020 scopus 로고    scopus 로고
    • Plant members of the alpha1→3/4-fucosyltransferase gene family encode an alpha1→4fucosyltransferase, potentially involved in Lewis(a) biosynthesis, and two core alpha1→3fucosyltransferases
    • Bakker H, Schijlen E, de Vries T, Schiphorst WE, Jordi W, Lommen A, Bosch D, van Die I. 2001. Plant members of the alpha1→3/4-fucosyltransferase gene family encode an alpha1→4fucosyltransferase, potentially involved in Lewis(a) biosynthesis, and two core alpha1→3fucosyltransferases. FEBS Lett 507:307-312.
    • (2001) FEBS Lett , vol.507 , pp. 307-312
    • Bakker, H.1    Schijlen, E.2    de Vries, T.3    Schiphorst, W.E.4    Jordi, W.5    Lommen, A.6    Bosch, D.7    van Die, I.8
  • 4
    • 0025098346 scopus 로고
    • Binary vectors which allow the exchange of plant selectable markers and reporter genes
    • Becker D. 1990. Binary vectors which allow the exchange of plant selectable markers and reporter genes. Nucleic Acids Res 18:203.
    • (1990) Nucleic Acids Res , vol.18 , pp. 203
    • Becker, D.1
  • 5
    • 3042659382 scopus 로고    scopus 로고
    • Bermúdez-Humarán LG, Langella P, Cortes-Perez NG, Gruss A, Tamez-Guerra RS, Oliveira SC, Saucedo-Cardenas O, Montes de Oca-Luna R, Le Loir Y. 2003. Intranasal immunization with recombinant Lactococcus lactis secreting murine interleukin-12 enhances antigen-specific Th1 cytokine production. Infect Immun 71:1887-1896.
    • Bermúdez-Humarán LG, Langella P, Cortes-Perez NG, Gruss A, Tamez-Guerra RS, Oliveira SC, Saucedo-Cardenas O, Montes de Oca-Luna R, Le Loir Y. 2003. Intranasal immunization with recombinant Lactococcus lactis secreting murine interleukin-12 enhances antigen-specific Th1 cytokine production. Infect Immun 71:1887-1896.
  • 7
    • 0034194222 scopus 로고    scopus 로고
    • Biosynthesis and posttranslational regulation of human IL-12
    • Carra G, Gerosa F, Trinchieri G. 2000. Biosynthesis and posttranslational regulation of human IL-12. J Immunol 164:4752-4761.
    • (2000) J Immunol , vol.164 , pp. 4752-4761
    • Carra, G.1    Gerosa, F.2    Trinchieri, G.3
  • 8
    • 0025261806 scopus 로고
    • Cap-independent enhancement of translation by a plant potyvirus 5′ nontranslated region
    • Carrington JC, Freed DD. 1990. Cap-independent enhancement of translation by a plant potyvirus 5′ nontranslated region. J Virol 64:1590-1597.
    • (1990) J Virol , vol.64 , pp. 1590-1597
    • Carrington, J.C.1    Freed, D.D.2
  • 9
    • 0028119214 scopus 로고    scopus 로고
    • Enhanced recovery of transformants of Agrobacterium tumefaciens after freeze-thaw transformation and drug selection
    • Chen H, Nelson RS, Sherwood JL. 2004. Enhanced recovery of transformants of Agrobacterium tumefaciens after freeze-thaw transformation and drug selection. Biotechniques 16:664-670.
    • (2004) Biotechniques , vol.16 , pp. 664-670
    • Chen, H.1    Nelson, R.S.2    Sherwood, J.L.3
  • 10
    • 0025718126 scopus 로고
    • Lectins, lectin genes, and their role in plant defense
    • Chrispeels MJ, Raikhel NV. 1991. Lectins, lectin genes, and their role in plant defense. Plant Cell 3:1-9.
    • (1991) Plant Cell , vol.3 , pp. 1-9
    • Chrispeels, M.J.1    Raikhel, N.V.2
  • 11
    • 0036005890 scopus 로고    scopus 로고
    • Interleukin-12 in anti-tumor immunity and immunotherapy
    • Colombo MP, Trinchieri G. 2002. Interleukin-12 in anti-tumor immunity and immunotherapy. Cytokine Growth Factor Rev 13:155-168.
    • (2002) Cytokine Growth Factor Rev , vol.13 , pp. 155-168
    • Colombo, M.P.1    Trinchieri, G.2
  • 12
    • 0032952346 scopus 로고    scopus 로고
    • Transgenic plants for therapeutic proteins: Linking upstream and downstream strategies
    • Cramer CL, Boothe JG, Oishi KK. 1999. Transgenic plants for therapeutic proteins: linking upstream and downstream strategies. Curr Top Microbiol Immunol 240:95-118.
    • (1999) Curr Top Microbiol Immunol , vol.240 , pp. 95-118
    • Cramer, C.L.1    Boothe, J.G.2    Oishi, K.K.3
  • 15
    • 23344441590 scopus 로고    scopus 로고
    • Virus-like particle vaccine conferred complete protection against a lethal influenza virus challenge
    • Galarza JM, Latham T, Cupo A. 2005. Virus-like particle vaccine conferred complete protection against a lethal influenza virus challenge. Viral Immunol 18:365-372.
    • (2005) Viral Immunol , vol.18 , pp. 365-372
    • Galarza, J.M.1    Latham, T.2    Cupo, A.3
  • 16
    • 0029433808 scopus 로고
    • Interleukin-12: A pivotal regulator of cell-mediated immunity
    • Gately MK, Brunda M J. 1995. Interleukin-12: a pivotal regulator of cell-mediated immunity. Cancer Treat Res 80:341-366.
    • (1995) Cancer Treat Res , vol.80 , pp. 341-366
    • Gately, M.K.1    Brunda, M.J.2
  • 17
    • 0041473693 scopus 로고    scopus 로고
    • Rhizosecretion of recombinant proteins from plant hairy roots
    • Gaume A, Komarnytsky S, Borisjuk N, Raskin I. 2003. Rhizosecretion of recombinant proteins from plant hairy roots. Plant Cell Rep 21:1188-1193.
    • (2003) Plant Cell Rep , vol.21 , pp. 1188-1193
    • Gaume, A.1    Komarnytsky, S.2    Borisjuk, N.3    Raskin, I.4
  • 18
    • 1542291118 scopus 로고    scopus 로고
    • Posttranslational modification of therapeutic proteins in plants
    • Gomord, V, Faye, L. 2004. Posttranslational modification of therapeutic proteins in plants. Curr Opin Plant Biol 7:171-181.
    • (2004) Curr Opin Plant Biol , vol.7 , pp. 171-181
    • Gomord, V.1    Faye, L.2
  • 19
    • 0035399604 scopus 로고    scopus 로고
    • + T cell development for contact hypersensitivity responses and circumvents anti-CD154 antibody-mediated inhibition
    • + T cell development for contact hypersensitivity responses and circumvents anti-CD154 antibody-mediated inhibition. J Immunol 167:156-162.
    • (2001) J Immunol , vol.167 , pp. 156-162
    • Gorbachev, A.V.1    DiIulio, N.A.2    Fairchild, R.L.3
  • 26
    • 0344603636 scopus 로고    scopus 로고
    • Construction of a single-chain interleukin-12-expressing retroviral vector and its application in cytokine gene therapy against experimental coccidioidomycosis
    • Jiang C, Magee DM, Cox RA. 1999. Construction of a single-chain interleukin-12-expressing retroviral vector and its application in cytokine gene therapy against experimental coccidioidomycosis. Infect Immun 67:2996-3001.
    • (1999) Infect Immun , vol.67 , pp. 2996-3001
    • Jiang, C.1    Magee, D.M.2    Cox, R.A.3
  • 27
    • 0024467154 scopus 로고
    • Identification and purification of natural killer cell stimulatory factor (NKSF), a cytokine with multiple biologic effects on human lymphocytes
    • Kobayashi M, Fitz L, Ryan M, Hewick RM, Clark SC, Chan S, Loudon R, Sherman F, Perussia B, Trinchieri G. 1989. Identification and purification of natural killer cell stimulatory factor (NKSF), a cytokine with multiple biologic effects on human lymphocytes. J Exp Med 170:827-845.
    • (1989) J Exp Med , vol.170 , pp. 827-845
    • Kobayashi, M.1    Fitz, L.2    Ryan, M.3    Hewick, R.M.4    Clark, S.C.5    Chan, S.6    Loudon, R.7    Sherman, F.8    Perussia, B.9    Trinchieri, G.10
  • 28
    • 0037473195 scopus 로고    scopus 로고
    • Expression and secretion of the heterodimeric protein interleukin-12 in plant cell suspension culture
    • Kwon TH, Seo JE, Kim J, Lee JH, Jang YS, Yang MS. 2003. Expression and secretion of the heterodimeric protein interleukin-12 in plant cell suspension culture. Biotechnol Bioeng 81:870-875.
    • (2003) Biotechnol Bioeng , vol.81 , pp. 870-875
    • Kwon, T.H.1    Seo, J.E.2    Kim, J.3    Lee, J.H.4    Jang, Y.S.5    Yang, M.S.6
  • 29
    • 0024746306 scopus 로고
    • Site-specific mutations alter in vitro factor binding and change promoter expression pattern in transgenic plants
    • Lam E, Benfey PN, Gilmartin PM, Fang RX, Chua NH. 1989. Site-specific mutations alter in vitro factor binding and change promoter expression pattern in transgenic plants. Proc Natl Acad Sci USA 86:7890-7894.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 7890-7894
    • Lam, E.1    Benfey, P.N.2    Gilmartin, P.M.3    Fang, R.X.4    Chua, N.H.5
  • 30
    • 0033755678 scopus 로고    scopus 로고
    • Immunization of cats against feline immunodeficiency virus (FIV) infection by using minimalistic immunogenic defined gene expression vector vaccines expressing FIV gp140 alone or with feline interleukin-12 (IL-12), IL-16, or a CpG motif
    • Leutenegger CM, Boretti FS, Mislin CN, Flynn JN, Schroff M, Habel A, Junghans C, Koenig-Merediz SA, Sigrist B, Aubert A, Pedersen NC, Wittig B, Lutz H. 2000. Immunization of cats against feline immunodeficiency virus (FIV) infection by using minimalistic immunogenic defined gene expression vector vaccines expressing FIV gp140 alone or with feline interleukin-12 (IL-12), IL-16, or a CpG motif. J Virol 74:10447-10457.
    • (2000) J Virol , vol.74 , pp. 10447-10457
    • Leutenegger, C.M.1    Boretti, F.S.2    Mislin, C.N.3    Flynn, J.N.4    Schroff, M.5    Habel, A.6    Junghans, C.7    Koenig-Merediz, S.A.8    Sigrist, B.9    Aubert, A.10    Pedersen, N.C.11    Wittig, B.12    Lutz, H.13
  • 31
    • 0031012127 scopus 로고    scopus 로고
    • Bioactive murine and human interleukin-12 fusion proteins which retain antitumor activity in vivo
    • Lieschke GJ, Rao PK, Gately MK, Mulligan RC. 1997. Bioactive murine and human interleukin-12 fusion proteins which retain antitumor activity in vivo. Nat Biotechnol 15:35-40.
    • (1997) Nat Biotechnol , vol.15 , pp. 35-40
    • Lieschke, G.J.1    Rao, P.K.2    Gately, M.K.3    Mulligan, R.C.4
  • 32
    • 0141706699 scopus 로고    scopus 로고
    • The production of recombinant pharmaceutical proteins in plants
    • Ma, JK-C, Drake PMW, 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.-C.1    Drake, P.M.W.2    Christou, P.3
  • 33
    • 0032960196 scopus 로고    scopus 로고
    • Use of intranasal IL-12 to target predominantly Th1 responses to nasal and Th2 responses to oral vaccines given with cholera toxin
    • Marinaro M, Boyaka PN, Jackson RJ, Finkelman FD, Kiyono H, Jirillo E, McGhee JR. 1999. Use of intranasal IL-12 to target predominantly Th1 responses to nasal and Th2 responses to oral vaccines given with cholera toxin. J Immunol 162:114-121.
    • (1999) J Immunol , vol.162 , pp. 114-121
    • Marinaro, M.1    Boyaka, P.N.2    Jackson, R.J.3    Finkelman, F.D.4    Kiyono, H.5    Jirillo, E.6    McGhee, J.R.7
  • 35
    • 4644363275 scopus 로고    scopus 로고
    • Production of recombinant proteins by hairy roots cultured in plastic sleeve bioreactors
    • Medina-Bolivar F, Cramer C. 2004. Production of recombinant proteins by hairy roots cultured in plastic sleeve bioreactors. Methods Mol Biol 267:351-363.
    • (2004) Methods Mol Biol , vol.267 , pp. 351-363
    • Medina-Bolivar, F.1    Cramer, C.2
  • 38
    • 0028944328 scopus 로고
    • Influence of interleukin 12 on p53 peptide vaccination against established Meth A sarcoma
    • Noguchi Y, Richards EC, Chen YT, Old LJ. 1995. Influence of interleukin 12 on p53 peptide vaccination against established Meth A sarcoma. Proc Natl Acad Sci USA 92:2219-2223.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2219-2223
    • Noguchi, Y.1    Richards, E.C.2    Chen, Y.T.3    Old, L.J.4
  • 39
    • 0346785399 scopus 로고    scopus 로고
    • Anti-solasodine glycoside single-chain Fv antibody stimulates biosynthesis of solasodine glycoside in plants
    • Putalun W, Taura F, Qing W, Matsushita H, Tanaka H, Shoyama Y. 2003. Anti-solasodine glycoside single-chain Fv antibody stimulates biosynthesis of solasodine glycoside in plants. Plant Cell Rep 2:344-349.
    • (2003) Plant Cell Rep , vol.2 , pp. 344-349
    • Putalun, W.1    Taura, F.2    Qing, W.3    Matsushita, H.4    Tanaka, H.5    Shoyama, Y.6
  • 40
    • 46449132888 scopus 로고    scopus 로고
    • ROOTec Bioactives GmbH, founded May 2005; Basel, Switzerland, by Drs. Hélène Corbière-Divialle, Alain Denis Meyer, and Peter Ripplinger. Available at www.RooTec.com
    • ROOTec Bioactives GmbH, founded May 2005; Basel, Switzerland, by Drs. Hélène Corbière-Divialle, Alain Denis Meyer, and Peter Ripplinger. Available at www.RooTec.com
  • 45
    • 36849049955 scopus 로고    scopus 로고
    • Bioreactor technology: A novel industrial tool for high-tech production of bioactive molecules and biopharmaceuticals from plant roots
    • Sivakumar G. 2006. Bioreactor technology: a novel industrial tool for high-tech production of bioactive molecules and biopharmaceuticals from plant roots. Biotechnol J 1:1419-1427.
    • (2006) Biotechnol , vol.J 1 , pp. 1419-1427
    • Sivakumar, G.1
  • 46
    • 33947321425 scopus 로고    scopus 로고
    • Pharma-Planta: Road testing the developing regulatory guidelines for plant-made pharmaceuticals
    • Sparrow PAC, Irwin JA, Dale PJ, Twyman RM, Ma JK-C. 2007. Pharma-Planta: road testing the developing regulatory guidelines for plant-made pharmaceuticals. Transgenic Res 16:147-161.
    • (2007) Transgenic Res , vol.16 , pp. 147-161
    • Sparrow, P.A.C.1    Irwin, J.A.2    Dale, P.J.3    Twyman, R.M.4    Ma, J.K.-C.5
  • 48
    • 0036217835 scopus 로고    scopus 로고
    • Production and in vivo testing of a recombinant bovine IL-12 as an adjuvant for Salmonella typhimurium vaccination in calves
    • Takehara K, Kikuma R, Ishikawa S, Kamikawa M, Nagata T, Yokomizo Y, Nakamura M. 2002. Production and in vivo testing of a recombinant bovine IL-12 as an adjuvant for Salmonella typhimurium vaccination in calves. Vet Immunol Immunopathol 86:23-30.
    • (2002) Vet Immunol Immunopathol , vol.86 , pp. 23-30
    • Takehara, K.1    Kikuma, R.2    Ishikawa, S.3    Kamikawa, M.4    Nagata, T.5    Yokomizo, Y.6    Nakamura, M.7
  • 49
    • 0025923253 scopus 로고
    • Peptide-N4-(N-acetyl-beta- glucosaminyl) asparagine amidase F cannot release glycans with fucose attached alpha 1→3 to the asparagine-linked N-acetylglucosamine residue
    • Tretter V, Altmann F, Marz L. 1991. Peptide-N4-(N-acetyl-beta- glucosaminyl) asparagine amidase F cannot release glycans with fucose attached alpha 1→3 to the asparagine-linked N-acetylglucosamine residue. Eur J Biochem 199:647-652.
    • (1991) Eur J Biochem , vol.199 , pp. 647-652
    • Tretter, V.1    Altmann, F.2    Marz, L.3
  • 50
    • 0028043326 scopus 로고
    • Interleukin-12: A cytokine produced by antigen-presenting cells with immunoregulatory functions in the generation of T-helper cells type 1 and cytotoxic lymphocytes
    • Trinchieri G. 1994. Interleukin-12: a cytokine produced by antigen-presenting cells with immunoregulatory functions in the generation of T-helper cells type 1 and cytotoxic lymphocytes. Blood 84:4008-4027.
    • (1994) Blood , vol.84 , pp. 4008-4027
    • Trinchieri, G.1
  • 51
    • 0025875022 scopus 로고
    • Cloning of cDNA for natural killer cell stimulatory factor, a heterodimeric cytokine with multiple biologic effects on T and natural killer cells
    • Wolf SF, Temple PA, Kobayashi M, Young D, Dicig M, Lowe L, Dzialo R, Fitz L, Ferenz C, Hewick RM. 1991. Cloning of cDNA for natural killer cell stimulatory factor, a heterodimeric cytokine with multiple biologic effects on T and natural killer cells. J Immunol 146:3074-3081.
    • (1991) J Immunol , vol.146 , pp. 3074-3081
    • Wolf, S.F.1    Temple, P.A.2    Kobayashi, M.3    Young, D.4    Dicig, M.5    Lowe, L.6    Dzialo, R.7    Fitz, L.8    Ferenz, C.9    Hewick, R.M.10
  • 52
    • 0033257934 scopus 로고    scopus 로고
    • Potentiation of antitumor effects of IL-12 in combination with paclitaxel in murine melanoma model in vivo
    • Zagozdzon R, Golab J, Mucha K, Foroncewicz B, Jakobisiak M. 1999. Potentiation of antitumor effects of IL-12 in combination with paclitaxel in murine melanoma model in vivo. Int J Mol Med 4:645-648.
    • (1999) Int J Mol Med , vol.4 , pp. 645-648
    • Zagozdzon, R.1    Golab, J.2    Mucha, K.3    Foroncewicz, B.4    Jakobisiak, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.