메뉴 건너뛰기




Volumn 6, Issue 6, 2011, Pages

Plant Hsp90 proteins interact with B-cells and stimulate their proliferation

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 90; POLYMYXIN B; RECOMBINANT PROTEIN; TOLL LIKE RECEPTOR 4; VEGETABLE PROTEIN;

EID: 79959296591     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0021231     Document Type: Article
Times cited : (16)

References (53)
  • 1
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl LH, Prodromou C, (2006) Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu Rev Biochem 75: 271-294.
    • (2006) Annu Rev Biochem , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 2
    • 0034817255 scopus 로고    scopus 로고
    • The Hsp90 family of proteins in Arabidopsis thaliana
    • Krishna P, Gloor G, (2001) The Hsp90 family of proteins in Arabidopsis thaliana. Cell Stress Chaperones 6: 238-246.
    • (2001) Cell Stress Chaperones , vol.6 , pp. 238-246
    • Krishna, P.1    Gloor, G.2
  • 4
    • 42549158533 scopus 로고    scopus 로고
    • HIF-1alpha and STAT3 client proteins interacting with the cancer chaperone Hsp90: therapeutic considerations
    • Kim HL, Cassone M, Otvos L Jr, Vogiatzi P, (2008) HIF-1alpha and STAT3 client proteins interacting with the cancer chaperone Hsp90: therapeutic considerations. Cancer Biol Ther 7: 10-14.
    • (2008) Cancer Biol Ther , vol.7 , pp. 10-14
    • Kim, H.L.1    Cassone, M.2    Otvos Jr., L.3    Vogiatzi, P.4
  • 5
    • 0032703419 scopus 로고    scopus 로고
    • Contribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae
    • Scheibel T, Weikl T, Rimerman R, Smith D, Lindquist S, et al. (1999) Contribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae. Mol Microbiol 34: 701-713.
    • (1999) Mol Microbiol , vol.34 , pp. 701-713
    • Scheibel, T.1    Weikl, T.2    Rimerman, R.3    Smith, D.4    Lindquist, S.5
  • 6
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt WB, Toft DO, (2003) Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp Biol Med 228: 111-133.
    • (2003) Exp Biol Med , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 8
    • 0033520019 scopus 로고    scopus 로고
    • Activation of cytotoxic T cells in vitro by recombinant gp96 fusion proteins irrespective of the 'fused' antigenic peptide sequence
    • Moré S, Breloer M, Fleischer B, von Bonin A, (1999) Activation of cytotoxic T cells in vitro by recombinant gp96 fusion proteins irrespective of the 'fused' antigenic peptide sequence. Immunol Lett 69: 275-282.
    • (1999) Immunol Lett , vol.69 , pp. 275-282
    • Moré, S.1    Breloer, M.2    Fleischer, B.3    von Bonin, A.4
  • 9
    • 0033382112 scopus 로고    scopus 로고
    • Immunostimulatory properties of the Leishmania infantum heat shock proteins HSP70 and HSP83
    • Rico AI, Angel SO, Alonso C, Requena JM, (1999) Immunostimulatory properties of the Leishmania infantum heat shock proteins HSP70 and HSP83. Mol Immunol 36: 1131-1139.
    • (1999) Mol Immunol , vol.36 , pp. 1131-1139
    • Rico, A.I.1    Angel, S.O.2    Alonso, C.3    Requena, J.M.4
  • 10
    • 0035280984 scopus 로고    scopus 로고
    • Analysis of the adjuvant effect of recombinant Leishmania infantum Hsp83 protein as a tool for vaccination
    • Echeverria PC, Dran G, Pereda G, Rico AI, Requena JM, et al. (2001) Analysis of the adjuvant effect of recombinant Leishmania infantum Hsp83 protein as a tool for vaccination. Immunol Lett 76: 107-110.
    • (2001) Immunol Lett , vol.76 , pp. 107-110
    • Echeverria, P.C.1    Dran, G.2    Pereda, G.3    Rico, A.I.4    Requena, J.M.5
  • 11
    • 0036819236 scopus 로고    scopus 로고
    • The heat shock proteins, Hsp70 and Hsp83, of Leishmania infantum are mitogens for mouse B cells
    • Rico AI, Gironès N, Fresno M, Alonso C, Requena JM, (2002) The heat shock proteins, Hsp70 and Hsp83, of Leishmania infantum are mitogens for mouse B cells. Cell Stress Chaperones 7: 339-346.
    • (2002) Cell Stress Chaperones , vol.7 , pp. 339-346
    • Rico, A.I.1    Gironès, N.2    Fresno, M.3    Alonso, C.4    Requena, J.M.5
  • 12
    • 2342632478 scopus 로고    scopus 로고
    • Immunological aspects of heat-shock proteins-the optimum stress of life
    • Prohászka Z, Füst G, (2004) Immunological aspects of heat-shock proteins-the optimum stress of life. Mol Immunol 41: 29-44.
    • (2004) Mol Immunol , vol.41 , pp. 29-44
    • Prohászka, Z.1    Füst, G.2
  • 13
    • 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 PC, de Miguel N, Costas M, Angel SO, (2006) Potent antigen-specific immunity to Toxoplasma gondii in adjuvant-free vaccination system using Rop2-Leishmania infantum Hsp83 fusion protein. Vaccine 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
  • 14
    • 0034252699 scopus 로고    scopus 로고
    • gp96- the immune system's Swiss army knife
    • Rammensee HG, Schild H, (2000) gp96- the immune system's Swiss army knife. Nat Immunol 1: 100-101.
    • (2000) Nat Immunol , vol.1 , pp. 100-101
    • Rammensee, H.G.1    Schild, H.2
  • 15
    • 0036512171 scopus 로고    scopus 로고
    • Roles of heat-shock proteins in innate and adaptive immunity
    • Srivastava P, (2002) Roles of heat-shock proteins in innate and adaptive immunity. Nat Rev Immunol 2: 185-194.
    • (2002) Nat Rev Immunol , vol.2 , pp. 185-194
    • Srivastava, P.1
  • 16
    • 23844482773 scopus 로고    scopus 로고
    • Heat shock proteins as endogenous adjuvants in sterile and septic inflammation
    • Quintana FJ, Cohen IR, (2005) Heat shock proteins as endogenous adjuvants in sterile and septic inflammation. J Immunol 175: 2777-2782.
    • (2005) J Immunol , vol.175 , pp. 2777-2782
    • Quintana, F.J.1    Cohen, I.R.2
  • 17
    • 67149133632 scopus 로고    scopus 로고
    • Heat shock proteins and immune system
    • Tsan MF, Gao BD, (2009) Heat shock proteins and immune system. J Leukoc Biol 85: 905-910.
    • (2009) J Leukoc Biol , vol.85 , pp. 905-910
    • Tsan, M.F.1    Gao, B.D.2
  • 18
    • 0035205522 scopus 로고    scopus 로고
    • Hsp90-binding immunophilins in plants: the protein movers
    • Pratt WB, Krishna P, Olsen LJ, (2001) Hsp90-binding immunophilins in plants: the protein movers. Trends Plant Sci 6: 54-58.
    • (2001) Trends Plant Sci , vol.6 , pp. 54-58
    • Pratt, W.B.1    Krishna, P.2    Olsen, L.J.3
  • 19
    • 58149271606 scopus 로고    scopus 로고
    • Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms
    • Johnson JL, Brown C, (2009) Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms. Cell Stress Chaperones 14: 83-94.
    • (2009) Cell Stress Chaperones , vol.14 , pp. 83-94
    • Johnson, J.L.1    Brown, C.2
  • 20
    • 70349759364 scopus 로고    scopus 로고
    • Plants as bioreactors: Recent developments and emerging opportunities
    • Sharma AK, Sharma MK, (2009) Plants as bioreactors: Recent developments and emerging opportunities. Biotechnol Adv 27: 811-832.
    • (2009) Biotechnol Adv , vol.27 , pp. 811-832
    • Sharma, A.K.1    Sharma, M.K.2
  • 21
    • 14844293838 scopus 로고    scopus 로고
    • Magnifection- a new platform for expressing recombinant vaccines in plants
    • Gleba Y, Klimyuk V, Marillonnet S, (2005) Magnifection- a new platform for expressing recombinant vaccines in plants. Vaccine 23: 2042-2048.
    • (2005) Vaccine , vol.23 , pp. 2042-2048
    • Gleba, Y.1    Klimyuk, V.2    Marillonnet, S.3
  • 22
    • 65549134575 scopus 로고    scopus 로고
    • Plants as bioreactors for the production of vaccine antigens
    • Tiwari S, Verma PC, Singh PK, Tuli R, (2009) Plants as bioreactors for the production of vaccine antigens. Biotechnol Adv 27: 449-467.
    • (2009) Biotechnol Adv , vol.27 , pp. 449-467
    • Tiwari, S.1    Verma, P.C.2    Singh, P.K.3    Tuli, R.4
  • 23
    • 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
    • Laguia Becher M, Martin V, Kraemer M, Corigliano M, Yacono ML, et al. (2010) 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 10: 52.
    • (2010) BMC Biotechnol , vol.10 , pp. 52
    • Laguia Becher, M.1    Martin, V.2    Kraemer, M.3    Corigliano, M.4    Yacono, M.L.5
  • 24
    • 33845756751 scopus 로고    scopus 로고
    • Approaches to achieve high-level heterologous protein production in plants
    • Streatfield SJ, (2007) Approaches to achieve high-level heterologous protein production in plants. Plant Biotechnol J 5: 2-15.
    • (2007) Plant Biotechnol J , vol.5 , pp. 2-15
    • Streatfield, S.J.1
  • 25
    • 8844279192 scopus 로고    scopus 로고
    • The in vivo and in vitro characterization of DnaK from Agrobacterium tumefaciens
    • Boshoff A, Hennessy F, Blatch GL, (2004) The in vivo and in vitro characterization of DnaK from Agrobacterium tumefaciens. Prot Expr Purif 38: 161-169.
    • (2004) Prot Expr Purif , vol.38 , pp. 161-169
    • Boshoff, A.1    Hennessy, F.2    Blatch, G.L.3
  • 26
    • 71749096555 scopus 로고    scopus 로고
    • Structural and functional diversity in the family of small heat shock proteins from the parasite Toxoplasma gondii
    • de Miguel N, Braun N, Bepperling A, Kriehuber T, Kastenmüller A, et al. (2009) Structural and functional diversity in the family of small heat shock proteins from the parasite Toxoplasma gondii. Biochim Biophys Acta 1793: 1738-1748.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 1738-1748
    • de Miguel, N.1    Braun, N.2    Bepperling, A.3    Kriehuber, T.4    Kastenmüller, A.5
  • 27
    • 0037036369 scopus 로고    scopus 로고
    • The endoplasmic reticulum-resident heat shock protein Gp96 activates dendritic cells via the Toll-like receptor 2/4 pathway
    • Vabulas RM, Braedel S, Hilf N, Singh-Jasuja H, Herter S, et al. (2002) The endoplasmic reticulum-resident heat shock protein Gp96 activates dendritic cells via the Toll-like receptor 2/4 pathway. J Biol Chem 277: 20847-20853.
    • (2002) J Biol Chem , vol.277 , pp. 20847-20853
    • Vabulas, R.M.1    Braedel, S.2    Hilf, N.3    Singh-Jasuja, H.4    Herter, S.5
  • 28
    • 0036512501 scopus 로고    scopus 로고
    • An integrated view of the roles and mechanisms of heat shock protein gp96-peptide complex in eliciting immune response
    • Li Z, Dai J, Zheng H, Liu B, Caudill M, (2002) An integrated view of the roles and mechanisms of heat shock protein gp96-peptide complex in eliciting immune response. Front Biosci 7: 731-751.
    • (2002) Front Biosci , vol.7 , pp. 731-751
    • Li, Z.1    Dai, J.2    Zheng, H.3    Liu, B.4    Caudill, M.5
  • 30
    • 33644845097 scopus 로고    scopus 로고
    • Heat shock protein and innate immunity
    • Tsan MF, Gao B, (2004) Heat shock protein and innate immunity. Cell Mol Immunol 1: 274-279.
    • (2004) Cell Mol Immunol , vol.1 , pp. 274-279
    • Tsan, M.F.1    Gao, B.2
  • 31
    • 33845399734 scopus 로고    scopus 로고
    • Heat shock up-regulates lmp2 and lmp7 and enhances presentation of immunoproteasome-dependent epitopes
    • Callahan MK, Wohlfert EA, Ménoret A, Srivastava PK, (2006) Heat shock up-regulates lmp2 and lmp7 and enhances presentation of immunoproteasome-dependent epitopes. J Immunol 177: 8393-8399.
    • (2006) J Immunol , vol.177 , pp. 8393-8399
    • Callahan, M.K.1    Wohlfert, E.A.2    Ménoret, A.3    Srivastava, P.K.4
  • 32
  • 33
    • 84934440688 scopus 로고    scopus 로고
    • Chaperones as part of immune networks
    • Prohászka Z, (2007) Chaperones as part of immune networks. Adv Exp Med Biol 594: 159-166.
    • (2007) Adv Exp Med Biol , vol.594 , pp. 159-166
    • Prohászka, Z.1
  • 35
    • 79959301738 scopus 로고    scopus 로고
    • Plant heat shock protein 70 as carrier for immunization against a plant-expressed reporter antigen
    • Buriani G, Mancini C, Benvenuto E, Baschieri S, (2010) Plant heat shock protein 70 as carrier for immunization against a plant-expressed reporter antigen. Transgenic Res Jun 18.
    • (2010) Transgenic Res Jun , vol.18
    • Buriani, G.1    Mancini, C.2    Benvenuto, E.3    Baschieri, S.4
  • 36
    • 12244305592 scopus 로고    scopus 로고
    • Toxoplasma gondii-derived heat shock protein HSP70 functions as a B cell mitogen
    • Aosai F, Chen M, Kang HK, Mun HS, Norose K, et al. (2002) Toxoplasma gondii-derived heat shock protein HSP70 functions as a B cell mitogen. Cell Stress Chaperones 7: 357-364.
    • (2002) Cell Stress Chaperones , vol.7 , pp. 357-364
    • Aosai, F.1    Chen, M.2    Kang, H.K.3    Mun, H.S.4    Norose, K.5
  • 37
    • 6344276691 scopus 로고    scopus 로고
    • Bacterial heat shock proteins enhance class II MHC antigen processing and presentation of chaperoned peptides to CD4+ T cells
    • Tobian AA, Canaday DH, Harding CV, (2004) Bacterial heat shock proteins enhance class II MHC antigen processing and presentation of chaperoned peptides to CD4+ T cells. J Immunol 173: 5130-5137.
    • (2004) J Immunol , vol.173 , pp. 5130-5137
    • Tobian, A.A.1    Canaday, D.H.2    Harding, C.V.3
  • 38
    • 36348964221 scopus 로고    scopus 로고
    • Heat shock proteins: linking danger and pathogen recognition
    • Osterloh A, Breloer M, (2008) Heat shock proteins: linking danger and pathogen recognition. Med Microbiol Immunol 197: 1-8.
    • (2008) Med Microbiol Immunol , vol.197 , pp. 1-8
    • Osterloh, A.1    Breloer, M.2
  • 39
    • 0034972226 scopus 로고    scopus 로고
    • Toll-like receptors and innate immunity
    • Akira S, (2001) Toll-like receptors and innate immunity. Adv Immunol 78: 1-56.
    • (2001) Adv Immunol , vol.78 , pp. 1-56
    • Akira, S.1
  • 40
    • 12444341944 scopus 로고    scopus 로고
    • Toll-like receptors in innate immunity
    • Takeda K, Akira S, (2005) Toll-like receptors in innate immunity. Int Immunol 17: 1-14.
    • (2005) Int Immunol , vol.17 , pp. 1-14
    • Takeda, K.1    Akira, S.2
  • 41
    • 0033120990 scopus 로고    scopus 로고
    • Cutting edge: receptor-mediated endocytosis of heat shock proteins by professional antigen-presenting cells
    • Arnold-Schild D, Hanau D, Spehner D, Schmid C, Rammensee HG, et al. (1999) Cutting edge: receptor-mediated endocytosis of heat shock proteins by professional antigen-presenting cells. J Immunol 162: 3757-3760.
    • (1999) J Immunol , vol.162 , pp. 3757-3760
    • Arnold-Schild, D.1    Hanau, D.2    Spehner, D.3    Schmid, C.4    Rammensee, H.G.5
  • 42
    • 0033747044 scopus 로고    scopus 로고
    • Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a maturation signal to dendritic cells and activate the NFkB pathway
    • Basu SR, Binder J, Suto R, Anderson KM, Srivastava PK, (2000) Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a maturation signal to dendritic cells and activate the NFkB pathway. Int Immunol 12: 1539-1546.
    • (2000) Int Immunol , vol.12 , pp. 1539-1546
    • Basu, S.R.1    Binder, J.2    Suto, R.3    Anderson, K.M.4    Srivastava, P.K.5
  • 43
    • 0345074067 scopus 로고    scopus 로고
    • Human heat shock protein 60 induces maturation of dendritic cells versus a Th1-promoting phenotype
    • Flohé SB, Brüggemann J, Lendemans S, Nikulina M, Meierhoff G, et al. (2003) Human heat shock protein 60 induces maturation of dendritic cells versus a Th1-promoting phenotype. J Immunol 170: 2340-2348.
    • (2003) J Immunol , vol.170 , pp. 2340-2348
    • Flohé, S.B.1    Brüggemann, J.2    Lendemans, S.3    Nikulina, M.4    Meierhoff, G.5
  • 45
    • 77955236788 scopus 로고    scopus 로고
    • Plant-made immunogens and effective delivery strategies
    • Paul M, Ma JKC, (2010) Plant-made immunogens and effective delivery strategies. Expert Rev Vaccines 9: 821-833.
    • (2010) Expert Rev Vaccines , vol.9 , pp. 821-833
    • Paul, M.1    Ma, J.K.C.2
  • 46
    • 77953987341 scopus 로고    scopus 로고
    • Plant-made vaccines for humans and animals
    • Rybicki EP, (2010) Plant-made vaccines for humans and animals. Plant Biotechnol J 8: 620-637.
    • (2010) Plant Biotechnol J , vol.8 , pp. 620-637
    • Rybicki, E.P.1
  • 47
    • 0032170495 scopus 로고    scopus 로고
    • High-efficiency cloning of Arabidopsis full-length cDNA by biotinylated CAP trapper
    • Seki M, Carninci P, Nishiyama Y, Hayashizaki Y, Shinozaki K, (1998) High-efficiency cloning of Arabidopsis full-length cDNA by biotinylated CAP trapper. Plant Journal 15: 707-720.
    • (1998) Plant Journal , vol.15 , pp. 707-720
    • Seki, M.1    Carninci, P.2    Nishiyama, Y.3    Hayashizaki, Y.4    Shinozaki, K.5
  • 48
    • 20244377471 scopus 로고    scopus 로고
    • Functional Annotation of a Full-Length Arabidopsis cDNA Collection
    • Seki M, Narusaka M, Kamiya A, Ishida J, Satou M, et al. (2002) Functional Annotation of a Full-Length Arabidopsis cDNA Collection. Science 296: 141-145.
    • (2002) Science , vol.296 , pp. 141-145
    • Seki, M.1    Narusaka, M.2    Kamiya, A.3    Ishida, J.4    Satou, M.5
  • 51
    • 33845266757 scopus 로고    scopus 로고
    • Effects of N-acyl-2-Hydroxymethyl Aziridineson in vitro Proliferative Responses of Human Lymphocytes Stimulated by Mitogens
    • Baba AF, Medjahed W, Merzouk H, Kajima Mulengi J, Belleville J, et al. (2006) Effects of N-acyl-2-Hydroxymethyl Aziridineson in vitro Proliferative Responses of Human Lymphocytes Stimulated by Mitogens. Gen Physiol Biophys 25: 277-287.
    • (2006) Gen Physiol Biophys , vol.25 , pp. 277-287
    • Baba, A.F.1    Medjahed, W.2    Merzouk, H.3    Kajima Mulengi, J.4    Belleville, J.5
  • 52
    • 47149089294 scopus 로고    scopus 로고
    • Platelets inhibit in vitro response of lymphocytes to mitogens
    • Wang Y, Niu J, (2008) Platelets inhibit in vitro response of lymphocytes to mitogens. Immunology Letters 119: 57-61.
    • (2008) Immunology Letters , vol.119 , pp. 57-61
    • Wang, Y.1    Niu, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.