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Volumn 10, Issue 5, 2015, Pages 748-759

The fusion of Toxoplasma gondii SAG1 vaccine candidate to Leishmania infantum heat shock protein 83-kDa improves expression levels in tobacco chloroplasts

Author keywords

Chloroplast transformation; Hsp83; Leishmania infantum; SAG1; Toxoplasma gondii

Indexed keywords

ANTIGENS; RECOMBINANT PROTEINS; TOBACCO; VACCINES;

EID: 84928825317     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201400742     Document Type: Article
Times cited : (32)

References (60)
  • 1
    • 84897031181 scopus 로고    scopus 로고
    • Recent advances on host plants and expression cassettes' structure and function in plant molecular pharming
    • Makhzoum, A., Benyammi, R., Moustafa, K., Trémouillaux-Guiller, J., Recent advances on host plants and expression cassettes' structure and function in plant molecular pharming. BioDrugs 2014, 28, 145-159.
    • (2014) BioDrugs , vol.28 , pp. 145-159
    • Makhzoum, A.1    Benyammi, R.2    Moustafa, K.3    Trémouillaux-Guiller, J.4
  • 2
    • 84877999567 scopus 로고    scopus 로고
    • Green factories for biopharmaceuticals.
    • Melnik, S., Stoger, E., Green factories for biopharmaceuticals. Curr. Med. Chem. 2013, 20, 1038-1046.
    • (2013) Curr. Med. Chem. , vol.20 , pp. 1038-1046
    • Melnik, S.1    Stoger, E.2
  • 3
    • 84881347629 scopus 로고    scopus 로고
    • Optimizing the yield of recombinant pharmaceutical proteins in plants.
    • Twyman, R. M., Schillberg, S., Fischer, R., Optimizing the yield of recombinant pharmaceutical proteins in plants. Curr. Pharm. Des. 2013, 19, 5486-5494.
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 5486-5494
    • Twyman, R.M.1    Schillberg, S.2    Fischer, R.3
  • 4
    • 84866046099 scopus 로고    scopus 로고
    • Using storage organelles for the accumulation and encapsulation of recombinant proteins.
    • Khan, I., Twyman, R. M., Arcalis, E., Stoger, E., Using storage organelles for the accumulation and encapsulation of recombinant proteins. Biotechnol. J. 2012, 7, 1099-1108.
    • (2012) Biotechnol. J. , vol.7 , pp. 1099-1108
    • Khan, I.1    Twyman, R.M.2    Arcalis, E.3    Stoger, E.4
  • 5
    • 84856968878 scopus 로고    scopus 로고
    • Production of foreign proteins using plastid transformation.
    • Scotti, N., Rigano, M. M., Cardi, T., Production of foreign proteins using plastid transformation. Biotechnol. Adv. 2012, 30, 387-397.
    • (2012) Biotechnol. Adv. , vol.30 , pp. 387-397
    • Scotti, N.1    Rigano, M.M.2    Cardi, T.3
  • 6
    • 84883266614 scopus 로고    scopus 로고
    • Genetic engineering of the chloroplast: novel tools and new applications.
    • Bock, R., Genetic engineering of the chloroplast: novel tools and new applications. Curr. Opin. Biotechnol. 2014, 26, 7-13.
    • (2014) Curr. Opin. Biotechnol. , vol.26 , pp. 7-13
    • Bock, R.1
  • 7
    • 13444271887 scopus 로고    scopus 로고
    • Accumulation of rotavirus VP6 protein in chloroplasts of transplastomic tobacco is limited by protein stability.
    • Birch-Machin, I., Newell, C. A., Hibberd, J. M., Gray, J. C., Accumulation of rotavirus VP6 protein in chloroplasts of transplastomic tobacco is limited by protein stability. Plant Biotechnol. J. 2004, 2, 261-270.
    • (2004) Plant Biotechnol. J. , vol.2 , pp. 261-270
    • Birch-Machin, I.1    Newell, C.A.2    Hibberd, J.M.3    Gray, J.C.4
  • 8
    • 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, M. E., Mentaberry, A., Bravo-Almonacid, F., Accumulation of hEGF and hEGF-fusion proteins in chloroplast-transformed tobacco plants is higher in the dark than in the light. J. Biotechnol. 2006, 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
  • 9
    • 40349091373 scopus 로고    scopus 로고
    • Translocation of aprotinin, a therapeutic protease inhibitor, into the thylakoid lumen of genetically engineered tobacco chloroplasts.
    • Tissot, G., Canard, H., Nadai, M., Martone, A. et al., Translocation of aprotinin, a therapeutic protease inhibitor, into the thylakoid lumen of genetically engineered tobacco chloroplasts. Plant Biotechnol. J. 2008, 6, 309-320.
    • (2008) Plant Biotechnol. J. , vol.6 , pp. 309-320
    • Tissot, G.1    Canard, H.2    Nadai, M.3    Martone, A.4
  • 10
    • 79957801371 scopus 로고    scopus 로고
    • A plant secretory signal peptide targets plastome-encoded recombinant proteins to the thylakoid membrane.
    • De Marchis, F., Pompa, A., Mannucci, R., Morosinotto, T. et al., A plant secretory signal peptide targets plastome-encoded recombinant proteins to the thylakoid membrane. Plant Mol. Biol. 2011, 76, 427-441.
    • (2011) Plant Mol. Biol. , vol.76 , pp. 427-441
    • De Marchis, F.1    Pompa, A.2    Mannucci, R.3    Morosinotto, T.4
  • 11
    • 84868521902 scopus 로고    scopus 로고
    • A chloroplast-derived Toxoplasma gondii GRA4 antigen used as an oral vaccine protects against toxoplasmosis in mice.
    • Del L Yácono, M., Farran, I., Becher, M. L., Sander, V. et al., A chloroplast-derived Toxoplasma gondii GRA4 antigen used as an oral vaccine protects against toxoplasmosis in mice. Plant Biotechnol. J. 2012, 10, 1136-1144.
    • (2012) Plant Biotechnol. J. , vol.10 , pp. 1136-1144
    • Del L Yácono, M.1    Farran, I.2    Becher, M.L.3    Sander, V.4
  • 12
    • 0034825369 scopus 로고    scopus 로고
    • Surface antigens of Toxoplasma gondii: variations on a theme.
    • Lekutis, C., Ferguson, D. J., Grigg, M. E., Camps, M. et al., Surface antigens of Toxoplasma gondii: variations on a theme. Int. J. Parasitol. 2001, 31, 1285-1292.
    • (2001) Int. J. Parasitol. , vol.31 , pp. 1285-1292
    • Lekutis, C.1    Ferguson, D.J.2    Grigg, M.E.3    Camps, M.4
  • 14
    • 33645862564 scopus 로고    scopus 로고
    • Congenital toxoplasmosis - prenatal aspects of Toxoplasma gondii infection.
    • Rorman, E., Zamir, C. S., Rilkis, I., Ben-David, H., Congenital toxoplasmosis - prenatal aspects of Toxoplasma gondii infection. Reprod. Toxicol. 2006, 21, 458-472.
    • (2006) Reprod. Toxicol. , vol.21 , pp. 458-472
    • Rorman, E.1    Zamir, C.S.2    Rilkis, I.3    Ben-David, H.4
  • 15
    • 0032146449 scopus 로고    scopus 로고
    • Immunization with E. coli produced recombinant T. gondii SAG1 with alum as adjuvant protect mice against lethal infection with Toxoplasma gondii.
    • Petersen, E., Nielsen, H. V., Christiansen, L., Spenter, J., Immunization with E. coli produced recombinant T. gondii SAG1 with alum as adjuvant protect mice against lethal infection with Toxoplasma gondii. Vaccine 1998, 16, 1283-1289.
    • (1998) Vaccine , vol.16 , pp. 1283-1289
    • Petersen, E.1    Nielsen, H.V.2    Christiansen, L.3    Spenter, J.4
  • 16
    • 0036803910 scopus 로고    scopus 로고
    • Protective effect of DNA-mediated immunization with a combination of SAG1 and IL-2 gene adjuvant against infection of Toxoplasma gondii in mice.
    • Chen, G., Chen, H., Guo, H., Zheng, H., Protective effect of DNA-mediated immunization with a combination of SAG1 and IL-2 gene adjuvant against infection of Toxoplasma gondii in mice. Chin. Med. J. (Engl) 2002, 115, 1448-1452.
    • (2002) Chin. Med. J. (Engl) , vol.115 , pp. 1448-1452
    • Chen, G.1    Chen, H.2    Guo, H.3    Zheng, H.4
  • 17
    • 0038513466 scopus 로고    scopus 로고
    • DNA vaccination with the immunodominant tachyzoite surface antigen (SAG-1) protects against adult acquired Toxoplasma gondii infection but does not prevent maternofoetal transmission.
    • Couper, K.N., Nielsen, H.V., Petersen, E., Roberts, F. et al., DNA vaccination with the immunodominant tachyzoite surface antigen (SAG-1) protects against adult acquired Toxoplasma gondii infection but does not prevent maternofoetal transmission. Vaccine 2003, 21, 2813-2820.
    • (2003) Vaccine , vol.21 , pp. 2813-2820
    • Couper, K.N.1    Nielsen, H.V.2    Petersen, E.3    Roberts, F.4
  • 18
    • 33846590526 scopus 로고    scopus 로고
    • Toxoplasma gondii: expression and characterization of a recombinant protein containing SAG1 and GRA2 in Pichia pastoris.
    • Zhou, H., Gu, Q., Zhao, Q., Zhang, J. et al., Toxoplasma gondii: expression and characterization of a recombinant protein containing SAG1 and GRA2 in Pichia pastoris. Parasitol. Res. 2007, 100, 829-835.
    • (2007) Parasitol. Res. , vol.100 , pp. 829-835
    • Zhou, H.1    Gu, Q.2    Zhao, Q.3    Zhang, J.4
  • 19
    • 48449106294 scopus 로고    scopus 로고
    • Protective effect of a DNA vaccine delivered in attenuated Salmonella typhimurium against Toxoplasma gondii infection in mice.
    • Qu, D., Wang, S., Cai, W., Du, A., Protective effect of a DNA vaccine delivered in attenuated Salmonella typhimurium against Toxoplasma gondii infection in mice. Vaccine 2008, 26, 4541-4548.
    • (2008) Vaccine , vol.26 , pp. 4541-4548
    • Qu, D.1    Wang, S.2    Cai, W.3    Du, A.4
  • 20
    • 80052318043 scopus 로고    scopus 로고
    • Comparative evaluation of immunization with recombinant protein and plasmid DNA vaccines of fusion antigen ROP2 and SAG1 from Toxoplasma gondii in mice: cellular and humoral immune responses.
    • Li, W. S., Chen, Q. X., Ye, J. X., Xie, Z. X. et al., Comparative evaluation of immunization with recombinant protein and plasmid DNA vaccines of fusion antigen ROP2 and SAG1 from Toxoplasma gondii in mice: cellular and humoral immune responses. Parasitol. Res. 2011, 109, 637-644.
    • (2011) Parasitol. Res. , vol.109 , pp. 637-644
    • Li, W.S.1    Chen, Q.X.2    Ye, J.X.3    Xie, Z.X.4
  • 21
    • 78650583066 scopus 로고    scopus 로고
    • Evaluation of three recombinant multi-antigenic vaccines composed of surface and secretory antigens of Toxoplasma gondii in murine models of experimental toxoplasmosis.
    • Dziadek, B., Gatkowska, J., Brzostek, A., Dziadek, J. et al., Evaluation of three recombinant multi-antigenic vaccines composed of surface and secretory antigens of Toxoplasma gondii in murine models of experimental toxoplasmosis. Vaccine 2011, 29, 821-830.
    • (2011) Vaccine , vol.29 , pp. 821-830
    • Dziadek, B.1    Gatkowska, J.2    Brzostek, A.3    Dziadek, J.4
  • 22
    • 0023737790 scopus 로고
    • Molecular analysis of the gene encoding the major surface antigen of Toxoplasma gondii.
    • Burg, J.L., Perelman, D., Kasper, L.H., Ware, P.L. et al., Molecular analysis of the gene encoding the major surface antigen of Toxoplasma gondii. J. Immunol. 1988, 141, 3584-3591.
    • (1988) J. Immunol. , vol.141 , pp. 3584-3591
    • Burg, J.L.1    Perelman, D.2    Kasper, L.H.3    Ware, P.L.4
  • 23
    • 0025832186 scopus 로고
    • Toxoplasmacidal activity of macrophages activated by recombinant major surface antigen (P30) of Toxoplasma gondii.
    • Makioka, A., Kobayashi, A., Toxoplasmacidal activity of macrophages activated by recombinant major surface antigen (P30) of Toxoplasma gondii. Infect. Immun. 1991, 59, 2851-2852.
    • (1991) Infect. Immun. , vol.59 , pp. 2851-2852
    • Makioka, A.1    Kobayashi, A.2
  • 24
    • 0029895353 scopus 로고    scopus 로고
    • Recombinant Toxoplasma gondii surface antigen 1 (P30) expressed in Escherichia coli is recognized by human Toxoplasma-specific immunoglobulin M (IgM) and IgG antibodies.
    • Harning, D., Spenter, J., Metsis, A., Vuust, J. et al., Recombinant Toxoplasma gondii surface antigen 1 (P30) expressed in Escherichia coli is recognized by human Toxoplasma-specific immunoglobulin M (IgM) and IgG antibodies. Clin. Diagn. Lab. Immunol. 1996, 3, 355-357.
    • (1996) Clin. Diagn. Lab. Immunol. , vol.3 , pp. 355-357
    • Harning, D.1    Spenter, J.2    Metsis, A.3    Vuust, J.4
  • 25
    • 0347356270 scopus 로고    scopus 로고
    • Evaluation of Toxoplasma gondii recombinant proteins for the diagnosis of recently acquired toxoplasmosis by an immunoglobulin G analysis.
    • Nigro, M., Gutierrez, A., Hoffer, A. M., Clemente, M. et al., Evaluation of Toxoplasma gondii recombinant proteins for the diagnosis of recently acquired toxoplasmosis by an immunoglobulin G analysis. Diagn. Microbiol. Infect. Dis. 2003, 47, 609-613.
    • (2003) Diagn. Microbiol. Infect. Dis. , vol.47 , pp. 609-613
    • Nigro, M.1    Gutierrez, A.2    Hoffer, A.M.3    Clemente, M.4
  • 26
    • 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. et al., Production of the main surface antigen of Toxoplasma gondii in tobacco leaves and analysis of its antigenicity and immunogenicity. Mol. Biotechnol. 2005, 30, 41-50.
    • (2005) Mol. Biotechnol. , vol.30 , pp. 41-50
    • Clemente, M.1    Curilovic, R.2    Sassone, A.3    Zelada, A.4
  • 27
    • 77954560597 scopus 로고    scopus 로고
    • Effect of codon optimization and subcellular targeting on Toxoplasma gondii antigen SAG1 expression in tobacco leaves to use in subcutaneous and oral immunization in mice.
    • Laguía-Becher, M., Martín, V., Kraemer, M., Corigliano, M. et al., Effect of codon optimization and subcellular targeting on Toxoplasma gondii antigen SAG1 expression in tobacco leaves to use in subcutaneous and oral immunization in mice. BMC Biotechnol. 2010, 10, 52.
    • (2010) BMC Biotechnol. , vol.10 , pp. 52
    • Laguía-Becher, M.1    Martín, V.2    Kraemer, M.3    Corigliano, M.4
  • 28
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery.
    • Pearl, L. H., Prodromou, C., Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 2006, 75, 271-294.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 29
    • 0033230242 scopus 로고    scopus 로고
    • Protein Folding in the Plant Cell.
    • Miernyk, J. A., Protein Folding in the Plant Cell. Plant Physiol. 1999, 121, 695-703.
    • (1999) Plant Physiol. , vol.121 , pp. 695-703
    • Miernyk, J.A.1
  • 30
    • 0036810352 scopus 로고    scopus 로고
    • Heat-shock protein 90 a chaperone for folding and regulation.
    • Picard, D., Heat-shock protein 90 a chaperone for folding and regulation. Cell Mol. Life Sci. 2002, 59, 1640-1648.
    • (2002) Cell Mol. Life Sci. , vol.59 , pp. 1640-1648
    • Picard, D.1
  • 31
    • 0028675649 scopus 로고
    • Analysis of tissue-specific expression of Arabidopsis thaliana HSP90-family gene HSP81.
    • Yabe, N., Takahashi, T., Komeda, Y., Analysis of tissue-specific expression of Arabidopsis thaliana HSP90-family gene HSP81. Plant Cell Physiol. 1994, 35, 1207-1219.
    • (1994) Plant Cell Physiol. , vol.35 , pp. 1207-1219
    • Yabe, N.1    Takahashi, T.2    Komeda, Y.3
  • 32
    • 33646469572 scopus 로고    scopus 로고
    • Potent antigen-specific immunity to Toxoplasma gondii in adjuvant-free vaccination system using Rop2-Leishmania infantum Hsp83 fusion protein.
    • Echeverria, P. C., de Miguel, N., Costas, M., Angel, S. O., Potent antigen-specific immunity to Toxoplasma gondii in adjuvant-free vaccination system using Rop2-Leishmania infantum Hsp83 fusion protein. Vaccine 2006, 24, 4102-4110.
    • (2006) Vaccine , vol.24 , pp. 4102-4110
    • Echeverria, P.C.1    de Miguel, N.2    Costas, M.3    Angel, S.O.4
  • 33
    • 77955282541 scopus 로고    scopus 로고
    • Evaluation of the antigenic value of recombinant Toxoplasma gondii HSP20 to detect specific immunoglobulin G antibodies in Toxoplasma infected humans.
    • Cóceres, V. M., Becher, M. L., De Napoli, M. G., Corvi, M. M. et al., Evaluation of the antigenic value of recombinant Toxoplasma gondii HSP20 to detect specific immunoglobulin G antibodies in Toxoplasma infected humans. Exp. Parasitol. 2010, 126, 263-266.
    • (2010) Exp. Parasitol. , vol.126 , pp. 263-266
    • Cóceres, V.M.1    Becher, M.L.2    De Napoli, M.G.3    Corvi, M.M.4
  • 34
    • 77950533184 scopus 로고    scopus 로고
    • The vaccine adjuvant extra domain A from fibronectin retains its proinflammatory properties when expressed in tobacco chloroplasts.
    • Farran, I., McCarthy-Suárez, I., Río-Manterola, F., Mansilla, C. et al., The vaccine adjuvant extra domain A from fibronectin retains its proinflammatory properties when expressed in tobacco chloroplasts. Planta 2010, 231, 977-990.
    • (2010) Planta , vol.231 , pp. 977-990
    • Farran, I.1    McCarthy-Suárez, I.2    Río-Manterola, F.3    Mansilla, C.4
  • 35
    • 77954537905 scopus 로고    scopus 로고
    • Stable production of peptide antigens in transgenic tobacco chloroplasts by fusion to the p53 tetramerisation domain.
    • Ortigosa, S. M., Fernández-San Millán, A., Veramendi, J., Stable production of peptide antigens in transgenic tobacco chloroplasts by fusion to the p53 tetramerisation domain. Transgenic Res. 2010, 19, 703-709.
    • (2010) Transgenic Res. , vol.19 , pp. 703-709
    • Ortigosa, S.M.1    Fernández-San Millán, A.2    Veramendi, J.3
  • 36
    • 0033382112 scopus 로고    scopus 로고
    • Immunostimulatory properties of the Leishmania infantum heat shock proteins HSP70 and HSP83.
    • Rico, A., Angel, S. O., Alonso, C., Requena, J. M., Immunostimulatory properties of the Leishmania infantum heat shock proteins HSP70 and HSP83. Mol. Immunol. 1999, 36, 1131-1139.
    • (1999) Mol. Immunol. , vol.36 , pp. 1131-1139
    • Rico, A.1    Angel, S.O.2    Alonso, C.3    Requena, J.M.4
  • 37
    • 0030642368 scopus 로고    scopus 로고
    • Transformation and foreign gene expression in plants by microprojectile bombardment.
    • Daniell, H., Transformation and foreign gene expression in plants by microprojectile bombardment. Methods Mol. Biol. 1997, 62, 463-489.
    • (1997) Methods Mol. Biol. , vol.62 , pp. 463-489
    • Daniell, H.1
  • 38
    • 33845645433 scopus 로고    scopus 로고
    • Expression of recombinant proteins lacking methionine as N-terminal amino acid in plastids: human serum albumin as a case study.
    • Fernández-San Millán, A., Farran, I., Molina, A., Mingo-Castel, A. M. et al., Expression of recombinant proteins lacking methionine as N-terminal amino acid in plastids: human serum albumin as a case study. J. Biotechnol. 2007, 127, 593-604.
    • (2007) J. Biotechnol. , vol.127 , pp. 593-604
    • Fernández-San Millán, A.1    Farran, I.2    Molina, A.3    Mingo-Castel, A.M.4
  • 39
    • 0030250830 scopus 로고    scopus 로고
    • During canine leishmaniasis a protein belonging to the 83-kDa heat-shock protein family elicits a strong humoral response.
    • Angel, S. O., Requena, J. M., Soto, M., Criado, D. et al., During canine leishmaniasis a protein belonging to the 83-kDa heat-shock protein family elicits a strong humoral response. Acta Trop. 1996, 62, 45-56.
    • (1996) Acta Trop. , vol.62 , pp. 45-56
    • Angel, S.O.1    Requena, J.M.2    Soto, M.3    Criado, D.4
  • 40
    • 0035112076 scopus 로고    scopus 로고
    • Plastid-expressed 5-enolpyruvylshikimate-3-phosphate synthase genes provide high level glyphosate tolerance in tobacco.
    • Ye, G. N., Hajdukiewicz, P. T., Broyles, D., Rodriguez, D. et al., Plastid-expressed 5-enolpyruvylshikimate-3-phosphate synthase genes provide high level glyphosate tolerance in tobacco. Plant J. 2001, 25, 261-270.
    • (2001) Plant J. , vol.25 , pp. 261-270
    • Ye, G.N.1    Hajdukiewicz, P.T.2    Broyles, D.3    Rodriguez, D.4
  • 41
    • 4944264765 scopus 로고    scopus 로고
    • High-yield expression of a viral peptide animal vaccine in transgenic tobacco chloroplasts.
    • Molina, A., Hervás-Stubbs, S., Daniell, H., Mingo-Castel, A. M. et al., High-yield expression of a viral peptide animal vaccine in transgenic tobacco chloroplasts. Plant Biotechnol. J. 2004, 2, 141-153.
    • (2004) Plant Biotechnol. J. , vol.2 , pp. 141-153
    • Molina, A.1    Hervás-Stubbs, S.2    Daniell, H.3    Mingo-Castel, A.M.4
  • 42
    • 84899489949 scopus 로고    scopus 로고
    • Research progress on surface antigen 1 (SAG1) of Toxoplasma gondii.
    • Wang, Y., Yin, H., Research progress on surface antigen 1 (SAG1) of Toxoplasma gondii. Parasit. Vectors 2014, 7, 180.
    • (2014) Parasit. Vectors , vol.7 , pp. 180
    • Wang, Y.1    Yin, H.2
  • 43
    • 0344505225 scopus 로고    scopus 로고
    • The conformation of purified Toxoplasma gondii SAG1 antigen, secreted from engineered Pichia pastoris, is adequate for serorecognition and cell proliferation.
    • Biemans, R., Grégoire, D., Haumont, M., Bosseloir, A. et al., The conformation of purified Toxoplasma gondii SAG1 antigen, secreted from engineered Pichia pastoris, is adequate for serorecognition and cell proliferation. J. Biotechnol. 1998, 66, 137-146.
    • (1998) J. Biotechnol. , vol.66 , pp. 137-146
    • Biemans, R.1    Grégoire, D.2    Haumont, M.3    Bosseloir, A.4
  • 44
    • 0035118541 scopus 로고    scopus 로고
    • Characterization of Toxoplasma gondii surface antigen 1 (SAG1) secreted from Pichia pastoris: evidence of hyper O-glycosylation.
    • Letourneur, O., Gervasi, G., Gaïa, S., Pagès, J. et al., Characterization of Toxoplasma gondii surface antigen 1 (SAG1) secreted from Pichia pastoris: evidence of hyper O-glycosylation. Biotechnol. Appl. Biochem. 2001, 33, 35-45.
    • (2001) Biotechnol. Appl. Biochem. , vol.33 , pp. 35-45
    • Letourneur, O.1    Gervasi, G.2    Gaïa, S.3    Pagès, J.4
  • 45
    • 0027976238 scopus 로고
    • Conformationally appropriate expression of the Toxoplasma antigen SAG1 (p30) in CHO cells.
    • Kim, K., Bülow, R., Kampmeier, J., Boothroyd, J. C., Conformationally appropriate expression of the Toxoplasma antigen SAG1 (p30) in CHO cells. Infect. Immun. 1994, 62, 203-209.
    • (1994) Infect. Immun. , vol.62 , pp. 203-209
    • Kim, K.1    Bülow, R.2    Kampmeier, J.3    Boothroyd, J.C.4
  • 46
    • 84892489162 scopus 로고    scopus 로고
    • Transgene-induced pleiotropic effects in transplastomic plants.
    • Scotti, N., Cardi, T., Transgene-induced pleiotropic effects in transplastomic plants. Biotechnol. Lett. 2014, 36, 229-239.
    • (2014) Biotechnol. Lett. , vol.36 , pp. 229-239
    • Scotti, N.1    Cardi, T.2
  • 47
    • 0346034697 scopus 로고    scopus 로고
    • The chlorate-resistant and photomorphogenesis-defective mutant cr88 encodes a chloroplast-targeted HSP90.
    • Cao, D., Froehlich, J. E., Zhang, H., Cheng, C. L., The chlorate-resistant and photomorphogenesis-defective mutant cr88 encodes a chloroplast-targeted HSP90. Plant J. 2003, 33, 107-118.
    • (2003) Plant J. , vol.33 , pp. 107-118
    • Cao, D.1    Froehlich, J.E.2    Zhang, H.3    Cheng, C.L.4
  • 48
    • 84892482896 scopus 로고    scopus 로고
    • Chloroplast-targeted Hsp90 plays essential roles in plastid development and embryogenesis in Arabidopsis possibly linking with VIPP1.
    • Feng, J., Fan, P., Jiang, P., Lv, S. et al., Chloroplast-targeted Hsp90 plays essential roles in plastid development and embryogenesis in Arabidopsis possibly linking with VIPP1. Physiol. Plant 2014, 150, 292-307.
    • (2014) Physiol. Plant , vol.150 , pp. 292-307
    • Feng, J.1    Fan, P.2    Jiang, P.3    Lv, S.4
  • 49
    • 34547503534 scopus 로고    scopus 로고
    • Zeolin is a recombinant storage protein with different solubility and stability properties according to its localization in the endoplasmic reticulum or in the chloroplast.
    • Bellucci, M., De Marchis, F., Nicoletti, I., Arcioni, S., Zeolin is a recombinant storage protein with different solubility and stability properties according to its localization in the endoplasmic reticulum or in the chloroplast. J. Biotechnol. 2007, 131, 97-105.
    • (2007) J. Biotechnol. , vol.131 , pp. 97-105
    • Bellucci, M.1    De Marchis, F.2    Nicoletti, I.3    Arcioni, S.4
  • 50
    • 0034016818 scopus 로고    scopus 로고
    • High-yield production of a human therapeutic protein in tobacco chloroplasts.
    • Staub, J. M., Garcia, B., Graves, J., Hajdukiewicz, P. T. et al., High-yield production of a human therapeutic protein in tobacco chloroplasts. Nat. Biotechnol. 2000, 18, 333-338.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 333-338
    • Staub, J.M.1    Garcia, B.2    Graves, J.3    Hajdukiewicz, P.T.4
  • 51
    • 80053072127 scopus 로고    scopus 로고
    • Metabolic adaptation in transplastomic plants massively accumulating recombinant proteins.
    • Bally, J., Job, C., Belghazi, M., Job, D., Metabolic adaptation in transplastomic plants massively accumulating recombinant proteins. PLoS One 2011, 6, e25289.
    • (2011) PLoS One , vol.6 , pp. e25289
    • Bally, J.1    Job, C.2    Belghazi, M.3    Job, D.4
  • 52
    • 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., Exhaustion of the chloroplast protein synthesis capacity by massive expression of a highly stable protein antibiotic. Plant J. 2009, 57, 436-445.
    • (2009) Plant J. , vol.57 , pp. 436-445
    • Oey, M.1    Lohse, M.2    Kreikemeyer, B.3    Bock, R.4
  • 53
    • 84857048585 scopus 로고    scopus 로고
    • Evolution and function of diverse Hsp90 homologs and cochaperone proteins.
    • Johnson, J. L., Evolution and function of diverse Hsp90 homologs and cochaperone proteins. Biochim. Biophys Acta 2012, 1823, 607-613.
    • (2012) Biochim. Biophys Acta , vol.1823 , pp. 607-613
    • Johnson, J.L.1
  • 54
    • 84890522100 scopus 로고    scopus 로고
    • Richter, K. Functions of the Hsp90 chaperone system: lifting client proteins to new heights.
    • Eckl, J. M., Richter, K. Functions of the Hsp90 chaperone system: lifting client proteins to new heights. Int. J. Biochem. Mol. Biol. 2013, 4, 157-165.
    • (2013) Int. J. Biochem. Mol. Biol. , vol.4 , pp. 157-165
    • Eckl, J.M.1
  • 56
    • 79955672685 scopus 로고    scopus 로고
    • Tobacco plastidial thioredoxins as modulators of recombinant protein production in transgenic chloroplasts.
    • Sanz-Barrio, R., Fernandez-San Millan, A., Corral-Martinez, P., Segui-Simarro, J. M. et al., Tobacco plastidial thioredoxins as modulators of recombinant protein production in transgenic chloroplasts. Plant Biotechnol. J. 2011, 9, 639-650.
    • (2011) Plant Biotechnol. J. , vol.9 , pp. 639-650
    • Sanz-Barrio, R.1    Fernandez-San Millan, A.2    Corral-Martinez, P.3    Segui-Simarro, J.M.4
  • 58
    • 44349102957 scopus 로고    scopus 로고
    • High-level expression of SAG1 and GRA7 gene of Toxoplasma gondii (Izatnagar isolate) and their application in serodiagnosis of goat toxoplasmosis.
    • Velmurugan, G. V., Tewari, A. K., Rao, J. R., Baidya, S. et al., High-level expression of SAG1 and GRA7 gene of Toxoplasma gondii (Izatnagar isolate) and their application in serodiagnosis of goat toxoplasmosis. Vet. Parasitol. 2008, 154, 185-192.
    • (2008) Vet. Parasitol. , vol.154 , pp. 185-192
    • Velmurugan, G.V.1    Tewari, A.K.2    Rao, J.R.3    Baidya, S.4
  • 59
    • 68949194535 scopus 로고    scopus 로고
    • Toxoplasma gondii: P30 peptides recognition pattern in human toxoplasmosis.
    • Cardona, N., de-la-Torre, A., Siachoque, H., Patarroyo, M. A. et al., Toxoplasma gondii: P30 peptides recognition pattern in human toxoplasmosis. Exp. Parasitol. 2009, 123, 199-202.
    • (2009) Exp. Parasitol. , vol.123 , pp. 199-202
    • Cardona, N.1    de-la-Torre, A.2    Siachoque, H.3    Patarroyo, M.A.4
  • 60
    • 33746905060 scopus 로고    scopus 로고
    • Toxoplasma gondii: immunogenicity and protection by P30 peptides in a murine model.
    • Siachoque, H., Guzman, F., Burgos, J., Patarroyo, M. E. et al., Toxoplasma gondii: immunogenicity and protection by P30 peptides in a murine model. Exp. Parasitol. 2006, 114, 62-65.
    • (2006) Exp. Parasitol. , vol.114 , pp. 62-65
    • Siachoque, H.1    Guzman, F.2    Burgos, J.3    Patarroyo, M.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.