메뉴 건너뛰기




Volumn 199, Issue , 2004, Pages 54-67

DNA vaccines expressing antigens with a stress protein-capturing domain display enhanced immunogenicity

Author keywords

[No Author keywords available]

Indexed keywords

CD8 ANTIGEN; CHIMERIC PROTEIN; DNA VACCINE; EPITOPE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 73; MUTANT PROTEIN; TUMOR ANTIGEN;

EID: 2942571812     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.0105-2896.2004.00136.x     Document Type: Review
Times cited : (15)

References (118)
  • 1
    • 0032007493 scopus 로고    scopus 로고
    • Polyvalent vaccination against hepatitis B surface and core antigen using dicistronic expression plasmids
    • Wild J, et al. Polyvalent vaccination against hepatitis B surface and core antigen using dicistronic expression plasmids. Vaccine 1998;16:353-360.
    • (1998) Vaccine , vol.16 , pp. 353-360
    • Wild, J.1
  • 2
    • 0035880772 scopus 로고    scopus 로고
    • Composition and arrangement of genes define the strength of IRES-driven translation in bicistronic mRNAs
    • Hennecke M, et al. Composition and arrangement of genes define the strength of IRES-driven translation in bicistronic mRNAs. Nucleic Acids Res 2001;29:3327-3334.
    • (2001) Nucleic Acids Res , vol.29 , pp. 3327-3334
    • Hennecke, M.1
  • 4
    • 0031134912 scopus 로고    scopus 로고
    • An ovalbumin-IL-12 fusion protein is more effective than ovalbumin plus free recombinant IL-12 in inducing a T helper cell type 1-dominated immune response and inhibiting antigen-specific IgE production
    • Kim TS, DeKruyff RH, Rupper R, Maecker HT, Levy S, Umetsu DT. An ovalbumin-IL-12 fusion protein is more effective than ovalbumin plus free recombinant IL-12 in inducing a T helper cell type 1-dominated immune response and inhibiting antigen-specific IgE production. J Immunol 1997;158:4137-4144.
    • (1997) J Immunol , vol.158 , pp. 4137-4144
    • Kim, T.S.1    DeKruyff, R.H.2    Rupper, R.3    Maecker, H.T.4    Levy, S.5    Umetsu, D.T.6
  • 5
    • 0034652784 scopus 로고    scopus 로고
    • Enhancement of DNA vaccine potency by linkage of antigen gene to an HSP70 gene
    • Chen CH, et al. Enhancement of DNA vaccine potency by linkage of antigen gene to an HSP70 gene. Cancer Res 2000;60:1035-1042.
    • (2000) Cancer Res , vol.60 , pp. 1035-1042
    • Chen, C.H.1
  • 6
    • 0035925610 scopus 로고    scopus 로고
    • Genetic adjuvants for DNA vaccines
    • Scheerlinck JY. Genetic adjuvants for DNA vaccines. Vaccine 2001;19:2647-2656.
    • (2001) Vaccine , vol.19 , pp. 2647-2656
    • Scheerlinck, J.Y.1
  • 7
    • 0031573541 scopus 로고    scopus 로고
    • Immunostimulatory effects of a plasmid expressing CD40 ligand (CD154) on gene immunization
    • Mendoza RB, Cantwell MJ, Kipps TJ. Immunostimulatory effects of a plasmid expressing CD40 ligand (CD154) on gene immunization. J Immunol 1997;159:5777-5781.
    • (1997) J Immunol , vol.159 , pp. 5777-5781
    • Mendoza, R.B.1    Cantwell, M.J.2    Kipps, T.J.3
  • 8
    • 0032213323 scopus 로고    scopus 로고
    • CD40 ligand/trimer DNA enhances both humoral and cellular immune responses and induces protective immunity to infectious and tumor challenge
    • Gurunathan S, et al. CD40 ligand/trimer DNA enhances both humoral and cellular immune responses and induces protective immunity to infectious and tumor challenge. J Immunol 1998;161:4563-4571.
    • (1998) J Immunol , vol.161 , pp. 4563-4571
    • Gurunathan, S.1
  • 9
    • 0034612321 scopus 로고    scopus 로고
    • A fusion DNA vaccine that targets antigen-presenting cells increases protection from viral challenge
    • Deliyannis G, Boyle JS, Brady JL, Brown LE, Lew AM. A fusion DNA vaccine that targets antigen-presenting cells increases protection from viral challenge. Proc Natl Acad Sci USA 2000;97:6676-6680.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6676-6680
    • Deliyannis, G.1    Boyle, J.S.2    Brady, J.L.3    Brown, L.E.4    Lew, A.M.5
  • 10
    • 0035478352 scopus 로고    scopus 로고
    • + T cell responses by effects on dendritic cells
    • + T cell responses by effects on dendritic cells. J Immunol 2001;167:3592-3599.
    • (2001) J Immunol , vol.167 , pp. 3592-3599
    • Eo, S.K.1    Kumaraguru, U.2    Rouse, B.T.3
  • 11
    • 0036284363 scopus 로고    scopus 로고
    • Regulation of DNA-raised immune responses by cotransfected interferon regulatory factors
    • Sasaki S, Amara RR, Yeow WS, Pitha PM, Robinson HL. Regulation of DNA-raised immune responses by cotransfected interferon regulatory factors. J Virol 2002;76:6652-6659.
    • (2002) J Virol , vol.76 , pp. 6652-6659
    • Sasaki, S.1    Amara, R.R.2    Yeow, W.S.3    Pitha, P.M.4    Robinson, H.L.5
  • 12
    • 0028358733 scopus 로고
    • Peptide transporter-independent, stress protein-mediated endosomal processing of endogenous protein antigens for major histocompatibility complex class I presentation
    • Schirmbeck R, Reimann J. Peptide transporter-independent, stress protein-mediated endosomal processing of endogenous protein antigens for major histocompatibility complex class I presentation. Eur J Immunol 1994;24:1478-1486.
    • (1994) Eur J Immunol , vol.24 , pp. 1478-1486
    • Schirmbeck, R.1    Reimann, J.2
  • 13
    • 1842299355 scopus 로고    scopus 로고
    • Stress protein (hsp73)-mediated, TAP-independent processing of endogenous, truncated SV40 large T antigen for Db-restricted peptide presentation
    • Schirmbeck R, Bōhm W, Reimann J. Stress protein (hsp73)-mediated, TAP-independent processing of endogenous, truncated SV40 large T antigen for Db-restricted peptide presentation. Eur J Immunol 1997;27:2016-2023.
    • (1997) Eur J Immunol , vol.27 , pp. 2016-2023
    • Schirmbeck, R.1    Bohm, W.2    Reimann, J.3
  • 14
    • 0022633461 scopus 로고
    • Antigenic binding site of monoclonal antibodies specific for simian virus 40 large T antigen
    • Gurney EG, Tamowsky S, Deppert W. Antigenic binding site of monoclonal antibodies specific for simian virus 40 large T antigen. J Virol 1986;57:1168-1172.
    • (1986) J Virol , vol.57 , pp. 1168-1172
    • Gurney, E.G.1    Tamowsky, S.2    Deppert, W.3
  • 16
    • 0023155617 scopus 로고
    • Medium tumor antigen of polyoma virus transformation-defective mutant NG59 is associated with 73-kilodalton heat shock protein
    • Walter G, Carbone A, Welch WJ. Medium tumor antigen of polyoma virus transformation-defective mutant NG59 is associated with 73-kilodalton heat shock protein. J Virol 1987;61:405-410.
    • (1987) J Virol , vol.61 , pp. 405-410
    • Walter, G.1    Carbone, A.2    Welch, W.J.3
  • 17
    • 0024354855 scopus 로고
    • Association of heat shock proteins with the SV40 large T antigen
    • Sawai ET, Butel JS. Association of heat shock proteins with the SV40 large T antigen. J Virol 1989;63:3961-3973.
    • (1989) J Virol , vol.63 , pp. 3961-3973
    • Sawai, E.T.1    Butel, J.S.2
  • 18
    • 0036631767 scopus 로고    scopus 로고
    • Priming polyvalent immunity by DNA vaccines expressing chimeric antigens with a stress protein-capturing, viral J-domain
    • Schirmbeck R, Kwissa M, Fissolo N, Elkholy S, Riedl P, Reimann J. Priming polyvalent immunity by DNA vaccines expressing chimeric antigens with a stress protein-capturing, viral J-domain. FASEB J 2002;16:1108-1110.
    • (2002) FASEB J , vol.16 , pp. 1108-1110
    • Schirmbeck, R.1    Kwissa, M.2    Fissolo, N.3    Elkholy, S.4    Riedl, P.5    Reimann, J.6
  • 19
    • 0002664005 scopus 로고
    • Interaction of vertebrate hsc70 and hsp70 with unfolded proteins and peptides
    • Morimoto RI, Tissieres A, Georgopoulos C, eds. Cold Spring Harbor: CSHL Press
    • Hightower LE, Sadis SE, Takenaka IM. Interaction of vertebrate hsc70 and hsp70 with unfolded proteins and peptides. In: Morimoto RI, Tissieres A, Georgopoulos C, eds. The Biology of Heat Shock Proteins and Molecular Chaperones. Cold Spring Harbor: CSHL Press, 1994: 179-207.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 179-207
    • Hightower, L.E.1    Sadis, S.E.2    Takenaka, I.M.3
  • 20
    • 0033592379 scopus 로고    scopus 로고
    • Interaction between Hsc70 and DnaJ homologues: Relationship between Hsc70 polymerization and ATPase activity
    • King C, Eisenberg E, Greene LE. Interaction between Hsc70 and DnaJ homologues: relationship between Hsc70 polymerization and ATPase activity. Biochemistry 1999;38:12452-12459.
    • (1999) Biochemistry , vol.38 , pp. 12452-12459
    • King, C.1    Eisenberg, E.2    Greene, L.E.3
  • 21
    • 0032961047 scopus 로고    scopus 로고
    • Truncated or chimeric endogenous protein antigens gain immunogenicity for B cells by stress protein-facilitated expression
    • Schirmbeck R, Gerstner O, Reimann J. Truncated or chimeric endogenous protein antigens gain immunogenicity for B cells by stress protein-facilitated expression. Eur J Immunol 1999;29:1740-1749.
    • (1999) Eur J Immunol , vol.29 , pp. 1740-1749
    • Schirmbeck, R.1    Gerstner, O.2    Reimann, J.3
  • 22
    • 0035852269 scopus 로고    scopus 로고
    • PsaA (pneumococcal surface adhesin A) and PspA (pneumococcal surface protein A) DNA vaccines induce humoral and cellular immune responses against Streptococcus pneumoniae
    • Miyaji EN, et al. PsaA (pneumococcal surface adhesin A) and PspA (pneumococcal surface protein A) DNA vaccines induce humoral and cellular immune responses against Streptococcus pneumoniae. Vaccine 2001;20:805-812.
    • (2001) Vaccine , vol.20 , pp. 805-812
    • Miyaji, E.N.1
  • 23
    • 0036681810 scopus 로고    scopus 로고
    • Priming biologically active antibody responses against an isolated, conformational viral epitope by DNA vaccination
    • Riedl P, El Kholy S, Reimann J, Schirmbeck R. Priming biologically active antibody responses against an isolated, conformational viral epitope by DNA vaccination. J Immunol 2002;169:1251-1260.
    • (2002) J Immunol , vol.169 , pp. 1251-1260
    • Riedl, P.1    El Kholy, S.2    Reimann, J.3    Schirmbeck, R.4
  • 25
    • 0042346200 scopus 로고    scopus 로고
    • + T cell responses by DNA vaccines expressing stress protein-binding polytope peptides
    • + T cell responses by DNA vaccines expressing stress protein-binding polytope peptides. J Immunol 2003;171:1140-1246.
    • (2003) J Immunol , vol.171 , pp. 1140-1246
    • Schirmbeck, R.1    Fissolo, N.2    Chaplin, P.3    Reimann, J.4
  • 26
    • 0024332976 scopus 로고
    • Limited receptor repertoire in a mycobacteria-reactive subset of γδ T lymphocytes
    • Happ MP, Kubo RT, Palmer E, Born W, O'Brien RL. Limited receptor repertoire in a mycobacteria-reactive subset of γδ T lymphocytes. Nature 1989;342:696-698.
    • (1989) Nature , vol.342 , pp. 696-698
    • Happ, M.P.1    Kubo, R.T.2    Palmer, E.3    Born, W.4    O'Brien, R.L.5
  • 27
    • 0024309528 scopus 로고
    • Lymphocytes bearing antigen-specific γδ T-cell receptors accumulate in human infectious disease lesions
    • Modlin RL, et al. Lymphocytes bearing antigen-specific γδ T-cell receptors accumulate in human infectious disease lesions. Nature 1989;339:544-548.
    • (1989) Nature , vol.339 , pp. 544-548
    • Modlin, R.L.1
  • 28
    • 0025746629 scopus 로고
    • A systematic molecular analysis of the T cell-stimulating antigens from Mycobacterium leprae with T cell clones of leprosy patients: Identification of a novel M. leprae HSP 70 fragment by M. leprae-specific T cells
    • Janson AAM, et al. A systematic molecular analysis of the T cell-stimulating antigens from Mycobacterium leprae with T cell clones of leprosy patients: Identification of a novel M. leprae HSP 70 fragment by M. leprae-specific T cells. J Immunol 1991;147:3530-3537.
    • (1991) J Immunol , vol.147 , pp. 3530-3537
    • Janson, A.A.M.1
  • 29
    • 0026527762 scopus 로고
    • A major T cell antigen of Mycobacterium leprae is a 10-kD heat-shock cognate protein
    • Mehra V, et al. A major T cell antigen of Mycobacterium leprae is a 10-kD heat-shock cognate protein. J Exp Med 1992;175:275-284.
    • (1992) J Exp Med , vol.175 , pp. 275-284
    • Mehra, V.1
  • 31
    • 0034671574 scopus 로고    scopus 로고
    • Highly autoproliferative T cells specific for 60-kDa heat shock protein produce IL-4/IL-10 and IFNγ and are protective in adjuvant arthritis
    • Paul AG, van Kooten PJ, van Eden W, van der Zee R. Highly autoproliferative T cells specific for 60-kDa heat shock protein produce IL-4/IL-10 and IFNγ and are protective in adjuvant arthritis. J Immunol 2000;165:7270-7277.
    • (2000) J Immunol , vol.165 , pp. 7270-7277
    • Paul, A.G.1    Van Kooten, P.J.2    Van Eden, W.3    Van Der Zee, R.4
  • 32
    • 0024468050 scopus 로고
    • Chlamydial disease pathogenesis. The 57-kD chlamydial hypersensitivity antigen is a stress response protein
    • Morrison RP, Belland RJ, Lyng K, Caldwell HD. Chlamydial disease pathogenesis. The 57-kD chlamydial hypersensitivity antigen is a stress response protein. J Exp Med 1989;170:1271-1283.
    • (1989) J Exp Med , vol.170 , pp. 1271-1283
    • Morrison, R.P.1    Belland, R.J.2    Lyng, K.3    Caldwell, H.D.4
  • 33
    • 0034142024 scopus 로고    scopus 로고
    • + T cell response to a single 12-mer epitope of the immunodominant heat-shock protein 60 of Yersinia enterocolitica in Yersinia-triggered reactive arthritis: Overlap with the B27-restricted CD8 epitope, functional properties, and epitope presentation by multiple DR alleles
    • + T cell response to a single 12-mer epitope of the immunodominant heat-shock protein 60 of Yersinia enterocolitica in Yersinia-triggered reactive arthritis: overlap with the B27-restricted CD8 epitope, functional properties, and epitope presentation by multiple DR alleles. J Immunol 2000;164:1529-1537.
    • (2000) J Immunol , vol.164 , pp. 1529-1537
    • Mertz, A.K.1
  • 34
    • 0034997928 scopus 로고    scopus 로고
    • Immunogenicity and protective efficacy of a Plasmodium yoelii Hsp60 DNA vaccine in BALB/c mice
    • Sanchez GI, et al. Immunogenicity and protective efficacy of a Plasmodium yoelii Hsp60 DNA vaccine in BALB/c mice. Infect Immun 2001;69:3897-3905.
    • (2001) Infect Immun , vol.69 , pp. 3897-3905
    • Sanchez, G.I.1
  • 35
    • 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. 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.I.1    Angel, S.O.2    Alonso, C.3    Requena, J.M.4
  • 36
    • 0029016247 scopus 로고
    • Self and foreign 60-kilodalton heat shock protein T cell epitope peptides serve as immunogenic carriers for a T cell-independent sugar antigen
    • Konen-Waisman S, Fridkin M, Cohen IR. Self and foreign 60-kilodalton heat shock protein T cell epitope peptides serve as immunogenic carriers for a T cell-independent sugar antigen. J Immunol 1995;154:5977-5985.
    • (1995) J Immunol , vol.154 , pp. 5977-5985
    • Konen-Waisman, S.1    Fridkin, M.2    Cohen, I.R.3
  • 37
    • 0033198580 scopus 로고    scopus 로고
    • Autoimmune intestinal pathology induced by hsp60-specific CD8 T cells
    • Steinhoff U, et al. Autoimmune intestinal pathology induced by hsp60-specific CD8 T cells. Immunity 1999;11:349-358.
    • (1999) Immunity , vol.11 , pp. 349-358
    • Steinhoff, U.1
  • 38
    • 0037988743 scopus 로고    scopus 로고
    • A peptide from heat shock protein 60 is the dominant peptide bound to Qa-1 in the absence of the MHC class Ia leader sequence peptide Qdm
    • Davies A, et al. A peptide from heat shock protein 60 is the dominant peptide bound to Qa-1 in the absence of the MHC class Ia leader sequence peptide Qdm. J Immunol 2003;170:5027-5033.
    • (2003) J Immunol , vol.170 , pp. 5027-5033
    • Davies, A.1
  • 39
    • 0030028801 scopus 로고    scopus 로고
    • Adjuvant-free hsp70 fusion protein system elicits humoral and cellular immune responses to HIV-1 p24
    • Suzue K, Young R. Adjuvant-free hsp70 fusion protein system elicits humoral and cellular immune responses to HIV-1 p24. J Immunol 1996;156:873-879.
    • (1996) J Immunol , vol.156 , pp. 873-879
    • Suzue, K.1    Young, R.2
  • 40
    • 0030667939 scopus 로고    scopus 로고
    • Heat shock fusion proteins as vehicles for antigen delivery into the major histocompatibility complex class I presentation pathway
    • Suzue K, Zhou X, Eisen HN, Young R. Heat shock fusion proteins as vehicles for antigen delivery into the major histocompatibility complex class I presentation pathway. Proc Natl Acad Sci USA 1997;94:13146-13151.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13146-13151
    • Suzue, K.1    Zhou, X.2    Eisen, H.N.3    Young, R.4
  • 42
    • 0034782206 scopus 로고    scopus 로고
    • Generation of cytotoxic T lymphocytes by MHC class I ligands fused to heat shock cognate protein 70
    • Udono H, Yamano T, Kawabata Y, Ueda M, Yui K. Generation of cytotoxic T lymphocytes by MHC class I ligands fused to heat shock cognate protein 70. Int Immunol 2001;13:1233-1242.
    • (2001) Int Immunol , vol.13 , pp. 1233-1242
    • Udono, H.1    Yamano, T.2    Kawabata, Y.3    Ueda, M.4    Yui, K.5
  • 43
    • 0033695064 scopus 로고    scopus 로고
    • A proposed mechanism for the induction of cytotoxic T lymphocyte production by heat shock fusion proteins
    • Cho BK, et al. A proposed mechanism for the induction of cytotoxic T lymphocyte production by heat shock fusion proteins. Immunity 2000;12:263-272.
    • (2000) Immunity , vol.12 , pp. 263-272
    • Cho, B.K.1
  • 44
    • 0033994625 scopus 로고    scopus 로고
    • Recombinant adeno-associated virus expressing human papillomavirus type 16 E7 peptide DNA fused with heat shock protein DNA as a potential vaccine for cervical cancer
    • Liu DW, et al. Recombinant adeno-associated virus expressing human papillomavirus type 16 E7 peptide DNA fused with heat shock protein DNA as a potential vaccine for cervical cancer. J Virol 2000;74:2888-2894.
    • (2000) J Virol , vol.74 , pp. 2888-2894
    • Liu, D.W.1
  • 45
    • 0035873726 scopus 로고    scopus 로고
    • Enhancement of sindbis virus self-replicating RNA vaccine potency by linkage of Mycobacterium tuberculosis heat shock protein 70 gene to an antigen gene
    • Cheng WF, et al. Enhancement of sindbis virus self-replicating RNA vaccine potency by linkage of Mycobacterium tuberculosis heat shock protein 70 gene to an antigen gene. J Immunol 2001;166:6218-6226.
    • (2001) J Immunol , vol.166 , pp. 6218-6226
    • Cheng, W.F.1
  • 46
    • 0034724336 scopus 로고    scopus 로고
    • Induction of cellular immunity by immunization with novel hybrid peptides complexed to heat shock protein 70
    • Moroi Y, et al. Induction of cellular immunity by immunization with novel hybrid peptides complexed to heat shock protein 70. Proc Natl Acad Sci USA 2000;97:3485-3490.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3485-3490
    • Moroi, Y.1
  • 47
    • 0037343184 scopus 로고    scopus 로고
    • Perforin is required for innate and adaptive immunity induced by heat shock protein gp96
    • Strbo N, Oizumi S, Sotosek-Tokmadzic V, Podack ER. Perforin is required for innate and adaptive immunity induced by heat shock protein gp96. Immunity 2003;18:381-390.
    • (2003) Immunity , vol.18 , pp. 381-390
    • Strbo, N.1    Oizumi, S.2    Sotosek-Tokmadzic, V.3    Podack, E.R.4
  • 48
  • 49
    • 0034608387 scopus 로고    scopus 로고
    • Cross-presentation of glycoprotein 96-associated antigens on major histocompatibility complex class I molecules requires receptor-mediated endocytosis
    • Singh JH, et al. Cross-presentation of glycoprotein 96-associated antigens on major histocompatibility complex class I molecules requires receptor-mediated endocytosis. J Exp Med 2000;191:1965-1974.
    • (2000) J Exp Med , vol.191 , pp. 1965-1974
    • Singh, J.H.1
  • 50
    • 0034500353 scopus 로고    scopus 로고
    • Characterization of a receptor for heat shock protein 70 on macrophages and monocytes
    • Sondermann H, Becker T, Mayhew M, Wieland F, Hartl FU. Characterization of a receptor for heat shock protein 70 on macrophages and monocytes. Biol Chem 2000;381:1165-1174.
    • (2000) Biol Chem , vol.381 , pp. 1165-1174
    • Sondermann, H.1    Becker, T.2    Mayhew, M.3    Wieland, F.4    Hartl, F.U.5
  • 51
    • 0036175927 scopus 로고    scopus 로고
    • Heat shock proteins 70 and 60 share common receptors which are expressed on human monocyte-derived but not epidermal dendritic cells
    • Lipsker D, et al. Heat shock proteins 70 and 60 share common receptors which are expressed on human monocyte-derived but not epidermal dendritic cells. Eur J Immunol 2002;32:322-332.
    • (2002) Eur J Immunol , vol.32 , pp. 322-332
    • Lipsker, D.1
  • 52
    • 0029127770 scopus 로고
    • Cross-priming of minor histocompatibility antigen-specific cytotoxic T cells upon immunization with the heat shock protein gp96
    • Arnold-Schild D, Faath S, Rammensee HG, Schild H. Cross-priming of minor histocompatibility antigen-specific cytotoxic T cells upon immunization with the heat shock protein gp96. J Exp Med 1995;182:885-889.
    • (1995) J Exp Med , vol.182 , pp. 885-889
    • Arnold-Schild, D.1    Faath, S.2    Rammensee, H.G.3    Schild, H.4
  • 53
    • 0033103513 scopus 로고    scopus 로고
    • Calreticulin, a peptide-binding chaperone of the endoplasmic reticulum, elicits tumor- and peptide-specific immunity
    • Basu S, Srivastava P. Calreticulin, a peptide-binding chaperone of the endoplasmic reticulum, elicits tumor- and peptide-specific immunity. J Exp Med 1999;189:797-802.
    • (1999) J Exp Med , vol.189 , pp. 797-802
    • Basu, S.1    Srivastava, P.2
  • 54
    • 0034113617 scopus 로고    scopus 로고
    • HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine
    • Asea A, et al. HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine. Nat Med 2000;6:435-442.
    • (2000) Nat Med , vol.6 , pp. 435-442
    • Asea, A.1
  • 55
    • 0035903158 scopus 로고    scopus 로고
    • Endocytosed heat shock protein 60s use TLR2 and TLR4 to activate the toll/interleukin-1 receptor signaling pathway in innate immune cells
    • Vabulas RM, et al. Endocytosed heat shock protein 60s use TLR2 and TLR4 to activate the toll/interleukin-1 receptor signaling pathway in innate immune cells. J Biol Chem 2001;276:31332-31339.
    • (2001) J Biol Chem , vol.276 , pp. 31332-31339
    • Vabulas, R.M.1
  • 56
    • 0034252620 scopus 로고    scopus 로고
    • CD91: A receptor for heat shock protein gp96
    • Binder RJ, Han DK, Srivastava P. CD91: a receptor for heat shock protein gp96. Nat Immunol 2000;1:151-155.
    • (2000) Nat Immunol , vol.1 , pp. 151-155
    • Binder, R.J.1    Han, D.K.2    Srivastava, P.3
  • 57
    • 0035070198 scopus 로고    scopus 로고
    • CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin
    • Basu S, Binder RJ, Ramalingam T, Srivastava P. CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity 2001;14:303-313.
    • (2001) Immunity , vol.14 , pp. 303-313
    • Basu, S.1    Binder, R.J.2    Ramalingam, T.3    Srivastava, P.4
  • 58
    • 18644364531 scopus 로고    scopus 로고
    • Involvement of LOX-1 in dendritic cell-mediated antigen cross-presentation
    • Delneste Y, et al. Involvement of LOX-1 in dendritic cell-mediated antigen cross-presentation. Immunity 2002;17:353-362.
    • (2002) Immunity , vol.17 , pp. 353-362
    • Delneste, Y.1
  • 59
    • 7344240408 scopus 로고    scopus 로고
    • Homogeneous Escherichia coli chaperonin 60 induces IL-1b and IL-6 gene expression in human monocytes by a mechanism independent of protein conformation
    • Tabona P, et al. Homogeneous Escherichia coli chaperonin 60 induces IL-1b and IL-6 gene expression in human monocytes by a mechanism independent of protein conformation. J Immunol 1998;161:1414-1421.
    • (1998) J Immunol , vol.161 , pp. 1414-1421
    • Tabona, P.1
  • 60
    • 0033545932 scopus 로고    scopus 로고
    • Heat shock protein 90 mediates macrophage activation by Taxol and bacterial lipopolysaccharide
    • Byrd CA, et al. Heat shock protein 90 mediates macrophage activation by Taxol and bacterial lipopolysaccharide. Proc Natl Acad Sci USA 1999;96:5645-5650.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5645-5650
    • Byrd, C.A.1
  • 61
    • 0033557202 scopus 로고    scopus 로고
    • Chlamydial and human heat shock protein 60s activate human vascular endothelium, smooth muscle cells, and macrophages
    • Kol A, Bourcier T, Lichtman AH, Libby P. Chlamydial and human heat shock protein 60s activate human vascular endothelium, smooth muscle cells, and macrophages. J Clin Invest 1999;103:571-577.
    • (1999) J Clin Invest , vol.103 , pp. 571-577
    • Kol, A.1    Bourcier, T.2    Lichtman, A.H.3    Libby, P.4
  • 63
    • 0033839045 scopus 로고    scopus 로고
    • The heat shock protein gp96 induces maturation of dendritic cells and down-regulation of its receptor
    • Singh JH, et al. The heat shock protein gp96 induces maturation of dendritic cells and down-regulation of its receptor. Eur J Immunol 2000;30:2211-2215.
    • (2000) Eur J Immunol , vol.30 , pp. 2211-2215
    • Singh, J.H.1
  • 65
    • 0033179274 scopus 로고    scopus 로고
    • Heat shock protein 70 induced during tumor cell killing induces Th1 cytokines and targets immature dendritic cell precursors to enhance antigen uptake
    • Todryk S, et al. Heat shock protein 70 induced during tumor cell killing induces Th1 cytokines and targets immature dendritic cell precursors to enhance antigen uptake. J Immunol 1999;163:1398-1408.
    • (1999) J Immunol , vol.163 , pp. 1398-1408
    • Todryk, S.1
  • 66
    • 0033976502 scopus 로고    scopus 로고
    • Heat shock proteins generate b-chemokines which function as innate adjuvants enhancing adaptive immunity
    • Lehner T, Bergmeier LA, Wang Y, Tao L, Sing M, Spallek R, van der Zee R. Heat shock proteins generate b-chemokines which function as innate adjuvants enhancing adaptive immunity. Eur J Immunol 2000;30:594-603.
    • (2000) Eur J Immunol , vol.30 , pp. 594-603
    • Lehner, T.1    Bergmeier, L.A.2    Wang, Y.3    Tao, L.4    Sing, M.5    Spallek, R.6    Van Der Zee, R.7
  • 67
    • 0037087398 scopus 로고    scopus 로고
    • Heat shock proteins gp96 and hsp70 activate the release of nitric oxide by APCs
    • Panjwani NN, Popova L, Srivastava P. Heat shock proteins gp96 and hsp70 activate the release of nitric oxide by APCs. J Immunol 2002;168:2997-3003.
    • (2002) J Immunol , vol.168 , pp. 2997-3003
    • Panjwani, N.N.1    Popova, L.2    Srivastava, P.3
  • 68
    • 0033559130 scopus 로고    scopus 로고
    • In vivo and in vitro activation of T cells after administration of Ag-negative heat shock proteins
    • Breloer M, Fleischer B, Von Bonin A. In vivo and in vitro activation of T cells after administration of Ag-negative heat shock proteins. J Immunol 1999;162:3141-3147.
    • (1999) J Immunol , vol.162 , pp. 3141-3147
    • Breloer, M.1    Fleischer, B.2    Von Bonin, A.3
  • 69
    • 0023192503 scopus 로고
    • Identification of a peptide-binding protein having a role in antigen presentation
    • Lakey EK, Margoliash E, Pierce SK. Identification of a peptide-binding protein having a role in antigen presentation. Proc Natl Acad Sci USA 1987;84:1659-1667.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 1659-1667
    • Lakey, E.K.1    Margoliash, E.2    Pierce, S.K.3
  • 70
    • 0025981503 scopus 로고
    • Cellular and subcellular distribution of PBP72/74, a peptide- binding protein that plays a role in antigen processing
    • VanBuskirk AM, DeNagel DC, Guagliardi LE, Brodsky FM, Pierce SK. Cellular and subcellular distribution of PBP72/74, a peptide- binding protein that plays a role in antigen processing. J Immunol 1991;146:500-506.
    • (1991) J Immunol , vol.146 , pp. 500-506
    • VanBuskirk, A.M.1    DeNagel, D.C.2    Guagliardi, L.E.3    Brodsky, F.M.4    Pierce, S.K.5
  • 71
    • 0027263325 scopus 로고
    • Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family
    • Domanico SZ, DeNagel DC, Dahlseid JN, Green JM, Pierce SK. Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family. Mol Cell Biol 1993;13:3598-3610.
    • (1993) Mol Cell Biol , vol.13 , pp. 3598-3610
    • Domanico, S.Z.1    DeNagel, D.C.2    Dahlseid, J.N.3    Green, J.M.4    Pierce, S.K.5
  • 72
    • 0033566936 scopus 로고    scopus 로고
    • The HSC73 molecular chaperone: Involvement in MHC class II antigen presentation
    • Panjwani N, Akbari O, Garcia S, Brazil M, Stockinger B. The HSC73 molecular chaperone: involvement in MHC class II antigen presentation. J Immunol 1999;163:1936-1942.
    • (1999) J Immunol , vol.163 , pp. 1936-1942
    • Panjwani, N.1    Akbari, O.2    Garcia, S.3    Brazil, M.4    Stockinger, B.5
  • 73
    • 0028313992 scopus 로고
    • Assembly, transport, and function of MHC class II molecules
    • Cresswell P. Assembly, transport, and function of MHC class II molecules. Annu Rev Immunol 1994;12:259-294.
    • (1994) Annu Rev Immunol , vol.12 , pp. 259-294
    • Cresswell, P.1
  • 74
    • 0030451002 scopus 로고    scopus 로고
    • Distinct antigen MHC class II complexes generated by separate processing pathways
    • Lindner R, Unanue ER, Distinct antigen MHC class II complexes generated by separate processing pathways. EMBO J 1996;15:6910-6920.
    • (1996) EMBO J , vol.15 , pp. 6910-6920
    • Lindner, R.1    Unanue, E.R.2
  • 75
    • 0030636722 scopus 로고    scopus 로고
    • Receptor-mediated endocytosis of antigens overcomes the requirement for HLA-DM in class II-restricted antigen presentation
    • Ma C, Blum JS. Receptor-mediated endocytosis of antigens overcomes the requirement for HLA-DM in class II-restricted antigen presentation. J Immunol 1997;158:1-4.
    • (1997) J Immunol , vol.158 , pp. 1-4
    • Ma, C.1    Blum, J.S.2
  • 76
    • 0141832121 scopus 로고    scopus 로고
    • MHC-guided processing: Binding of large antigen fragments
    • Sercarz EE, Maverakis E. MHC-guided processing: binding of large antigen fragments. Nat Rev Immunol 2003;3:621-629.
    • (2003) Nat Rev Immunol , vol.3 , pp. 621-629
    • Sercarz, E.E.1    Maverakis, E.2
  • 77
    • 0035907379 scopus 로고    scopus 로고
    • Heat shock protein-chaperoned peptides but not free peptides introduced into the cytosol are presented efficiently by MHC I molecules
    • Binder RJ, Blachere NE, Srivastava P. Heat shock protein-chaperoned peptides but not free peptides introduced into the cytosol are presented efficiently by MHC I molecules. J Biol Chem 2001;276:17163-17171.
    • (2001) J Biol Chem , vol.276 , pp. 17163-17171
    • Binder, R.J.1    Blachere, N.E.2    Srivastava, P.3
  • 78
    • 0033083413 scopus 로고    scopus 로고
    • Isolation of MHC class I-restricted tumor antigen peptide and its precursors associated with heat shock proteins hsp70, hsp90, and gp96
    • Ishii T, et al. Isolation of MHC class I-restricted tumor antigen peptide and its precursors associated with heat shock proteins hsp70, hsp90, and gp96. J Immunol 1999;162:1303-1309.
    • (1999) J Immunol , vol.162 , pp. 1303-1309
    • Ishii, T.1
  • 79
    • 0029981741 scopus 로고    scopus 로고
    • Expression levels of stress protein gp96 are not limiting for major histocompatibility complex class I-restricted antigen presentation
    • Lammert E, Arnold-Schild D, Rammensee HG, Schild H. Expression levels of stress protein gp96 are not limiting for major histocompatibility complex class I-restricted antigen presentation. Eur J Immunol 1996;26:875-879.
    • (1996) Eur J Immunol , vol.26 , pp. 875-879
    • Lammert, E.1    Arnold-Schild, D.2    Rammensee, H.G.3    Schild, H.4
  • 80
    • 0028979675 scopus 로고
    • A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides
    • Suto R, Srivastava P. A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science 1995;269:1585-1588.
    • (1995) Science , vol.269 , pp. 1585-1588
    • Suto, R.1    Srivastava, P.2
  • 81
    • 0037111445 scopus 로고    scopus 로고
    • + T cells in vivo
    • + T cells in vivo. J Immunol 2002;169:5622-5629.
    • (2002) J Immunol , vol.169 , pp. 5622-5629
    • Harmala, L.A.1
  • 82
    • 0345299172 scopus 로고    scopus 로고
    • The dual nature of specific immunological activity of tumor-derived gp96 preparations
    • Chandawarkar RY, Wagh MS, Srivastava P. The dual nature of specific immunological activity of tumor-derived gp96 preparations. J Exp Med 1999;189:1437-1442.
    • (1999) J Exp Med , vol.189 , pp. 1437-1442
    • Chandawarkar, R.Y.1    Wagh, M.S.2    Srivastava, P.3
  • 84
    • 0030016520 scopus 로고    scopus 로고
    • Synthetic peptides non-covalendy bound to bacterial hsp70 elicit peptide-specific T-cell responses in vivo
    • Roman E, Moreno C. Synthetic peptides non-covalendy bound to bacterial hsp70 elicit peptide-specific T-cell responses in vivo. Immunology 1996;88:487-492.
    • (1996) Immunology , vol.88 , pp. 487-492
    • Roman, E.1    Moreno, C.2
  • 85
    • 0030877759 scopus 로고    scopus 로고
    • Generation of heat shock protein-based vaccines by intracellular loading of gp96 with antigenic peptides
    • Heikema A, Agsteribbe E, Wilschut J, Huckriede A. Generation of heat shock protein-based vaccines by intracellular loading of gp96 with antigenic peptides. Immunol Lett 1997;57:69-74.
    • (1997) Immunol Lett , vol.57 , pp. 69-74
    • Heikema, A.1    Agsteribbe, E.2    Wilschut, J.3    Huckriede, A.4
  • 86
    • 0032473485 scopus 로고    scopus 로고
    • Immunization with a lymphocytic choriomeningitis virus peptide mixed with heat shock protein 70 results in protective antiviral immunity and specific cytotoxic T lymphocytes
    • Ciupitu AM, et al. Immunization with a lymphocytic choriomeningitis virus peptide mixed with heat shock protein 70 results in protective antiviral immunity and specific cytotoxic T lymphocytes. J Exp Med 1998;187:685-691.
    • (1998) J Exp Med , vol.187 , pp. 685-691
    • Ciupitu, A.M.1
  • 87
    • 0035901097 scopus 로고    scopus 로고
    • HBV-specific peptide associated with heat-shock protein gp96
    • Meng SD, Gao T, Gao GF, Tien P. HBV-specific peptide associated with heat-shock protein gp96. Lancet 2001;357:528-529.
    • (2001) Lancet , vol.357 , pp. 528-529
    • Meng, S.D.1    Gao, T.2    Gao, G.F.3    Tien, P.4
  • 88
    • 0036133062 scopus 로고    scopus 로고
    • Immunization with chaperone-peptide complex induces low-avidity cytotoxic T lymphocytes providing transient protection against herpes simplex virus infection
    • Kumaraguru U, Gierynska M, Norman S, Bruce BD, Rouse BT. Immunization with chaperone-peptide complex induces low-avidity cytotoxic T lymphocytes providing transient protection against herpes simplex virus infection. J Virol 2002;76:136-141.
    • (2002) J Virol , vol.76 , pp. 136-141
    • Kumaraguru, U.1    Gierynska, M.2    Norman, S.3    Bruce, B.D.4    Rouse, B.T.5
  • 89
    • 0027260585 scopus 로고
    • Heat shock protein 70-associated peptides elicit specific cancer immunity
    • Udono H, Srivastava P. Heat shock protein 70-associated peptides elicit specific cancer immunity. J Exp Med 1993;178:1391-1396.
    • (1993) J Exp Med , vol.178 , pp. 1391-1396
    • Udono, H.1    Srivastava, P.2
  • 90
    • 0028301079 scopus 로고
    • Comparison of tumor-specific immunogenicity of stress-induced protein gp96, hsp90, and hsp70
    • Udono H, Srivastava P. Comparison of tumor-specific immunogenicity of stress-induced protein gp96, hsp90, and hsp70. J Immunol 1994;152:5398-5403.
    • (1994) J Immunol , vol.152 , pp. 5398-5403
    • Udono, H.1    Srivastava, P.2
  • 91
    • 0028811321 scopus 로고
    • Molecular heterogeneity of tumor rejection antigen/heat shock protein GP96
    • Feldweg AM, Srivastava P. Molecular heterogeneity of tumor rejection antigen/heat shock protein GP96. Int J Cancer 1995;63:310-314.
    • (1995) Int J Cancer , vol.63 , pp. 310-314
    • Feldweg, A.M.1    Srivastava, P.2
  • 92
    • 0030775140 scopus 로고    scopus 로고
    • Heat shock protein-peptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T lymphocyte response and tumor immunity
    • Blachere NE, et al. Heat shock protein-peptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T lymphocyte response and tumor immunity. J Exp Med 1997;186:1315-1322.
    • (1997) J Exp Med , vol.186 , pp. 1315-1322
    • Blachere, N.E.1
  • 93
    • 0035167866 scopus 로고    scopus 로고
    • Characterization of heat shock protein 110 and glucose-regulated protein 170 as cancer vaccines and the effect of fever-range hyperthermia on vaccine activity
    • Wang XY, Kazim L, Repasky EA, Subjeck JR. Characterization of heat shock protein 110 and glucose-regulated protein 170 as cancer vaccines and the effect of fever-range hyperthermia on vaccine activity. J Immunol 2001;166:490-497.
    • (2001) J Immunol , vol.166 , pp. 490-497
    • Wang, X.Y.1    Kazim, L.2    Repasky, E.A.3    Subjeck, J.R.4
  • 94
    • 0041408691 scopus 로고    scopus 로고
    • Cell surface expression of heat shock protein gp96 enhances cross-presentation of cellular antigens and the generation of tumor-specific T cell memory
    • Dai J, et al. Cell surface expression of heat shock protein gp96 enhances cross-presentation of cellular antigens and the generation of tumor-specific T cell memory. Cancer Immun 2003;3:1-11.
    • (2003) Cancer Immun , vol.3 , pp. 1-11
    • Dai, J.1
  • 95
    • 0034661654 scopus 로고    scopus 로고
    • Involvement of an ATP-dependent peptide chaperone in cross-presentation after DNA immunization
    • Kumaraguru U, Rouse RJ, Nair SK, Bruce BD, Rouse BT. Involvement of an ATP-dependent peptide chaperone in cross-presentation after DNA immunization. J Immunol 2000;165:750-759.
    • (2000) J Immunol , vol.165 , pp. 750-759
    • Kumaraguru, U.1    Rouse, R.J.2    Nair, S.K.3    Bruce, B.D.4    Rouse, B.T.5
  • 96
    • 0040089526 scopus 로고    scopus 로고
    • Molecular characterization of dendritic cell-derived exosomes. Selective accumulation of the heat shock protein hsc73
    • Thery C, et al. Molecular characterization of dendritic cell-derived exosomes. Selective accumulation of the heat shock protein hsc73. J Cell Biol 1999;147:599-610.
    • (1999) J Cell Biol , vol.147 , pp. 599-610
    • Thery, C.1
  • 97
    • 0033747044 scopus 로고    scopus 로고
    • Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-kappa B pathway
    • Basu S, Binder RJ, Suto R, Anderson KM, Srivastava PK. Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-kappa B pathway. Int Immunol 2000;12:1539-1546.
    • (2000) Int Immunol , vol.12 , pp. 1539-1546
    • Basu, S.1    Binder, R.J.2    Suto, R.3    Anderson, K.M.4    Srivastava, P.K.5
  • 99
    • 0003160189 scopus 로고
    • Selective degradation of cytosolic proteins by lysosomes
    • Ciechanover AJ, Schwartz AS, eds. New York: Wiley-liss
    • Dice JF, Terlecky SR. Selective degradation of cytosolic proteins by lysosomes. In: Ciechanover AJ, Schwartz AS, eds. Cellular Proteolytic Systems. New York: Wiley-liss, 1994: 55-64.
    • (1994) Cellular Proteolytic Systems , pp. 55-64
    • Dice, J.F.1    Terlecky, S.R.2
  • 100
    • 0030052910 scopus 로고    scopus 로고
    • Roles of molecular chaperones in protein degradation
    • Hayes SA, Dice JF. Roles of molecular chaperones in protein degradation. J Cell Biol 1996;132:255-258.
    • (1996) J Cell Biol , vol.132 , pp. 255-258
    • Hayes, S.A.1    Dice, J.F.2
  • 101
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • Cuervo AM, Dice JF. A receptor for the selective uptake and degradation of proteins by lysosomes. Science 1996;273:501-503.
    • (1996) Science , vol.273 , pp. 501-503
    • Cuervo, A.M.1    Dice, J.F.2
  • 103
    • 0036986253 scopus 로고    scopus 로고
    • Selective expression of immunogenic, VIP-derived epitopes binding antibodies
    • El Kholy S, Riedl P, Kwissa M, Reimann J, Schirmbeck R. Selective expression of immunogenic, VIP-derived epitopes binding antibodies. Intervirology 2002;45:251-259.
    • (2002) Intervirology , vol.45 , pp. 251-259
    • El Kholy, S.1    Riedl, P.2    Kwissa, M.3    Reimann, J.4    Schirmbeck, R.5
  • 104
    • 0029956512 scopus 로고    scopus 로고
    • Gene vaccination with naked plasmid DNA: Mechanism of CTL priming
    • Corr M, Lee DJ, Carson DA, Tighe H. Gene vaccination with naked plasmid DNA: mechanism of CTL priming. J Exp Med 1996;184:1555-1560.
    • (1996) J Exp Med , vol.184 , pp. 1555-1560
    • Corr, M.1    Lee, D.J.2    Carson, D.A.3    Tighe, H.4
  • 105
    • 0029737350 scopus 로고    scopus 로고
    • Induction of cytotoxic T lymphocytes by intramuscular immunization with plasmid DNA is facilitated by bone marrow-derived cells
    • Doe B, Selby M, Barnett S, Baenziger J, Walker CM. Induction of cytotoxic T lymphocytes by intramuscular immunization with plasmid DNA is facilitated by bone marrow-derived cells. Proc Natl Acad Sci USA 1996;93:8578-8583.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8578-8583
    • Doe, B.1    Selby, M.2    Barnett, S.3    Baenziger, J.4    Walker, C.M.5
  • 106
    • 0029789751 scopus 로고    scopus 로고
    • Generation of MHC class I-restricted cytotoxic T lymphocytes by expression of a viral protein in muscle cells: Antigen presentation by non-muscle cells
    • Ulmer JB, Deck RR, DeWitt CM, Donnhly JI, Liu MA. Generation of MHC class I-restricted cytotoxic T lymphocytes by expression of a viral protein in muscle cells: antigen presentation by non-muscle cells. Immunology 1996;89:59-67.
    • (1996) Immunology , vol.89 , pp. 59-67
    • Ulmer, J.B.1    Deck, R.R.2    DeWitt, C.M.3    Donnhly, J.I.4    Liu, M.A.5
  • 107
    • 0030820743 scopus 로고    scopus 로고
    • Priming of cytotoxic T lymphocytes by DNA vaccines: Requirement for professional antigen presenting cells and evidence for antigen transfer from myocytes
    • Fu TM, et al. Priming of cytotoxic T lymphocytes by DNA vaccines: requirement for professional antigen presenting cells and evidence for antigen transfer from myocytes. Mol Med 1997;3:362-371.
    • (1997) Mol Med , vol.3 , pp. 362-371
    • Fu, T.M.1
  • 108
    • 0031178797 scopus 로고    scopus 로고
    • The dominant role of bone marrow-derived cells in CTL induction following plasmid DNA immunization at different sites
    • Iwasaki A, Torres CA, Ohashi PS, Robinson HL, Barber BH. The dominant role of bone marrow-derived cells in CTL induction following plasmid DNA immunization at different sites. J Immunol 1997;159:11-14.
    • (1997) J Immunol , vol.159 , pp. 11-14
    • Iwasaki, A.1    Torres, C.A.2    Ohashi, P.S.3    Robinson, H.L.4    Barber, B.H.5
  • 109
    • 0032711215 scopus 로고    scopus 로고
    • In vivo priming by DNA injection occurs predominantly by antigen transfer
    • Corr M, von-Damm A, Lee DJ, Tighe H. In vivo priming by DNA injection occurs predominantly by antigen transfer. J Immunol 1999;163:4721-4727.
    • (1999) J Immunol , vol.163 , pp. 4721-4727
    • Corr, M.1    Von-Damm, A.2    Lee, D.J.3    Tighe, H.4
  • 111
    • 0028863527 scopus 로고
    • Protection against mycoplasma infection using expression-library immunization
    • Barry MA, Lai WC, Johnston SA. Protection against mycoplasma infection using expression-library immunization. Nature 1995;377:632-635.
    • (1995) Nature , vol.377 , pp. 632-635
    • Barry, M.A.1    Lai, W.C.2    Johnston, S.A.3
  • 112
    • 0033178998 scopus 로고    scopus 로고
    • Protective immune responses induced by vaccination with an expression genomic library of Leishmania major
    • Piedrafita D, Xu D, Hunter D, Harrison RA, Liew FY. Protective immune responses induced by vaccination with an expression genomic library of Leishmania major. J Immunol 1999;163:1467-1472.
    • (1999) J Immunol , vol.163 , pp. 1467-1472
    • Piedrafita, D.1    Xu, D.2    Hunter, D.3    Harrison, R.A.4    Liew, F.Y.5
  • 113
    • 0027170483 scopus 로고
    • Induction of virus-specific cytotoxic T lymphocytes in vivo by liposome-entrapped mRNA
    • Martinon F, et al. Induction of virus-specific cytotoxic T lymphocytes in vivo by liposome-entrapped mRNA. Eur J Immunol 1993;23:1719-1722.
    • (1993) Eur J Immunol , vol.23 , pp. 1719-1722
    • Martinon, F.1
  • 114
    • 0027226028 scopus 로고
    • Induction of antibodies to a κV region by gene immunization
    • Watanabe A, et al. Induction of antibodies to a κV region by gene immunization. J Immunol 1993;151:2871-2876.
    • (1993) J Immunol , vol.151 , pp. 2871-2876
    • Watanabe, A.1
  • 115
    • 0028364706 scopus 로고
    • Idiotypic vaccination against human B-cell lymphoma. Rescue of variable region gene sequences from biopsy material for assembly as single-chain Fv personal vaccines
    • Hawkins RE, et al. Idiotypic vaccination against human B-cell lymphoma. Rescue of variable region gene sequences from biopsy material for assembly as single-chain Fv personal vaccines. Blood 1994;83:3279-3288.
    • (1994) Blood , vol.83 , pp. 3279-3288
    • Hawkins, R.E.1
  • 116
    • 0030589822 scopus 로고    scopus 로고
    • Induction of antibodies against human prion proteins (PrP) by DNA-mediated immunization of PrP0/0 mice
    • Krasemann S, Groschup M, Hunsmann G, Bodemer W. Induction of antibodies against human prion proteins (PrP) by DNA-mediated immunization of PrP0/0 mice. J Immunol Methods 1996;199:109-118.
    • (1996) J Immunol Methods , vol.199 , pp. 109-118
    • Krasemann, S.1    Groschup, M.2    Hunsmann, G.3    Bodemer, W.4
  • 117
    • 0029101242 scopus 로고
    • Nucleic acid vaccination primes hepatitis B surface antigen-specific cytotoxic T lymphocytes in nonresponder mice
    • Schirmbeck R, Böhm W, Ando K-I, Chisari FV, Reimann J. Nucleic acid vaccination primes hepatitis B surface antigen-specific cytotoxic T lymphocytes in nonresponder mice. J Virol 1995;69:5929-5934.
    • (1995) J Virol , vol.69 , pp. 5929-5934
    • Schirmbeck, R.1    Böhm, W.2    Ando, K.-I.3    Chisari, F.V.4    Reimann, J.5
  • 118
    • 0346121477 scopus 로고    scopus 로고
    • Breaking tolerance in hepatitis B surface antigen (HBsAg) transgenic mice by vaccination with cross-reactive, natural HBsAg variants
    • Schirmbeck R, et al. Breaking tolerance in hepatitis B surface antigen (HBsAg) transgenic mice by vaccination with cross-reactive, natural HBsAg variants. Eur J Immunol 2003;33:3342-3352.
    • (2003) Eur J Immunol , vol.33 , pp. 3342-3352
    • Schirmbeck, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.