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Volumn 165, Issue 2, 2000, Pages 750-759

Involvement of an ATP-dependent peptide chaperone in cross-presentation after DNA immunization

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONE; DNA VACCINE; PLASMID DNA;

EID: 0034661654     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.165.2.750     Document Type: Article
Times cited : (37)

References (42)
  • 1
    • 0027213712 scopus 로고
    • Protection against a lethal influenza virus challenge by immunization with hemagglutinin-expressing plasmid DNA
    • Robinson, H. L., L. A. Hunt, and R. G. Webster. 1993. Protection against a lethal influenza virus challenge by immunization with hemagglutinin-expressing plasmid DNA. Vaccine 11:975.
    • (1993) Vaccine , vol.11 , pp. 975
    • Robinson, H.L.1    Hunt, L.A.2    Webster, R.G.3
  • 3
    • 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., M. Selby, S. Barnett, J. Baenziger, and C. M. Walker. 1996. Induction of cytotoxic T lymphocytes by intramuscular immunization with plasmid DNA is facilitated by bone marrow-derived cells. Proc. Natl. Acad. Sci. USA 93:8578.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8578
    • Doe, B.1    Selby, M.2    Barnett, S.3    Baenziger, J.4    Walker, C.M.5
  • 5
    • 0030698310 scopus 로고    scopus 로고
    • Antigen presentation by dendritic cells after immunization with DNA encoding a major histocompatibility complex class II-restricted viral epitope
    • Casares, S., K. Inaba, T.-D. Brumeanu, R. M. Steinman, and C. A. Bona. 1997. Antigen presentation by dendritic cells after immunization with DNA encoding a major histocompatibility complex class II-restricted viral epitope. J. Exp. Med. 186:1481.
    • (1997) J. Exp. Med. , vol.186 , pp. 1481
    • Casares, S.1    Inaba, K.2    Brumeanu, T.-D.3    Steinman, R.M.4    Bona, C.A.5
  • 6
    • 0028108773 scopus 로고
    • Induction of primary cytotoxic T lymphocyte responses with DNA encoding herpes simplex virus proteins
    • Rouse, R. J. D., S. K. Nair, S. Lydy, J. C. Bowen, and B. T. Rouse. 1994. Induction of primary cytotoxic T lymphocyte responses with DNA encoding herpes simplex virus proteins. J. Virol. 68:5685.
    • (1994) J. Virol. , vol.68 , pp. 5685
    • Rouse, R.J.D.1    Nair, S.K.2    Lydy, S.3    Bowen, J.C.4    Rouse, B.T.5
  • 7
    • 0031570044 scopus 로고    scopus 로고
    • Differential dependence on target site tissue for gene gun and intramuscular DNA immunizations
    • Torres, C. A. T., A. Iwasaki, B. H. Barber, and H. L. Robinson. 1997. Differential dependence on target site tissue for gene gun and intramuscular DNA immunizations. J. Immunol. 158:4529.
    • (1997) J. Immunol. , vol.158 , pp. 4529
    • Torres, C.A.T.1    Iwasaki, A.2    Barber, B.H.3    Robinson, H.L.4
  • 9
    • 0030016719 scopus 로고    scopus 로고
    • Dendritic cells and immune-based therapies
    • Steinman, R. M. 1996. Dendritic cells and immune-based therapies. Exp. Hematol. 24:859.
    • (1996) Exp. Hematol. , vol.24 , pp. 859
    • Steinman, R.M.1
  • 10
    • 0027157303 scopus 로고
    • Dendritic cells: Antigen presentation, accessory function and clinical relevance
    • Steinman, R. M., M. Witmer-Pack, and K. Inaba. 1993. Dendritic cells: antigen presentation, accessory function and clinical relevance. Adv. Exp. Med. Biol. 329:1.
    • (1993) Adv. Exp. Med. Biol. , vol.329 , pp. 1
    • Steinman, R.M.1    Witmer-Pack, M.2    Inaba, K.3
  • 11
    • 0031045622 scopus 로고    scopus 로고
    • Origin, maturation, and antigen presenting functions of dendritic cells
    • Cella, M., F. Sallusto, and A. Lanzavecchia. 1997. Origin, maturation, and antigen presenting functions of dendritic cells. Curr. Opin. Immunol. 9:10.
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 10
    • Cella, M.1    Sallusto, F.2    Lanzavecchia, A.3
  • 12
    • 0027326802 scopus 로고
    • Macrophages, but not dendritic cells, accumulate colloidal carbon following administration in situ
    • Witmer-Pack, M. D., M. T. Crowley, K. Inaba, and R. M. Steinman. 1993. Macrophages, but not dendritic cells, accumulate colloidal carbon following administration in situ. J. Cell Sci. 105:965.
    • (1993) J. Cell Sci. , vol.105 , pp. 965
    • Witmer-Pack, M.D.1    Crowley, M.T.2    Inaba, K.3    Steinman, R.M.4
  • 14
    • 0029162385 scopus 로고
    • Antigen presentation to cytotoxic T lymphocytes in vivo
    • Bevan, M. J. 1995. Antigen presentation to cytotoxic T lymphocytes in vivo. J. Exp. Med. 182:639.
    • (1995) J. Exp. Med. , vol.182 , pp. 639
    • Bevan, M.J.1
  • 15
    • 0027511213 scopus 로고
    • Phagocytic processing of bacterial antigens for class I MHC presentation to T cells
    • Pfeifer, J. D., M. J. Wick, R. L. Robert, K. Findlay, S. J. Mormark, and C. V. Harding. 1993. Phagocytic processing of bacterial antigens for class I MHC presentation to T cells. Nature 361:359.
    • (1993) Nature , vol.361 , pp. 359
    • Pfeifer, J.D.1    Wick, M.J.2    Robert, R.L.3    Findlay, K.4    Mormark, S.J.5    Harding, C.V.6
  • 16
    • 0032485487 scopus 로고    scopus 로고
    • Dendritic cells acquire antigen from apoptotic cells and induce class-I-restricted CTLs
    • Albert, M. L., B. Sauter, and N. Bhardwaj. 1998. Dendritic cells acquire antigen from apoptotic cells and induce class-I-restricted CTLs. Nature 392:86.
    • (1998) Nature , vol.392 , pp. 86
    • Albert, M.L.1    Sauter, B.2    Bhardwaj, N.3
  • 17
    • 0023821578 scopus 로고
    • Introduction of soluble protein into the class I pathway of antigen processing and presentation
    • Moore, M. W., F. R. Carbone, and M. J. Bevan. 1988. Introduction of soluble protein into the class I pathway of antigen processing and presentation. Cell 54:777.
    • (1988) Cell , vol.54 , pp. 777
    • Moore, M.W.1    Carbone, F.R.2    Bevan, M.J.3
  • 19
    • 0026585493 scopus 로고
    • Soluble proteins delivered to dendritic cells via pH-sensitive liposomes induce primary CTL responses in vivo
    • Nair, S. K., F. Zhou, R. Reddy, L. Huang, and B. T. Rouse. 1992. Soluble proteins delivered to dendritic cells via pH-sensitive liposomes induce primary CTL responses in vivo. J. Exp. Med. 175:609.
    • (1992) J. Exp. Med. , vol.175 , pp. 609
    • Nair, S.K.1    Zhou, F.2    Reddy, R.3    Huang, L.4    Rouse, B.T.5
  • 20
    • 0025300982 scopus 로고
    • Generation of class I MHC-restricted T-T hybridomas
    • Rock, K. L., L. Rothstein, and S. Gamble. 1990. Generation of class I MHC-restricted T-T hybridomas. J. Immunol. 145:804.
    • (1990) J. Immunol. , vol.145 , pp. 804
    • Rock, K.L.1    Rothstein, L.2    Gamble, S.3
  • 22
    • 0002450535 scopus 로고
    • Detection and analysis of protein expressed from cloned genes
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Detection and analysis of protein expressed from cloned genes. In Molecular Cloning: A Laboratory Manual. Vol. 3. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, pp. 18.56-18.57.
    • (1989) Molecular Cloning: A Laboratory Manual , vol.3 , pp. 1856-1857
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 23
    • 0022551217 scopus 로고
    • Substrate and inhibitor studies of thermolysin-like neutral metalloendopeptidase from kidney membrane fractions: Comparison with bacterial thermolysin
    • Pozsgay, M., C. Michaud, M. Liebman, and M. Oslowski. 1986. Substrate and inhibitor studies of thermolysin-like neutral metalloendopeptidase from kidney membrane fractions: comparison with bacterial thermolysin. Biochemistry 25:1292.
    • (1986) Biochemistry , vol.25 , pp. 1292
    • Pozsgay, M.1    Michaud, C.2    Liebman, M.3    Oslowski, M.4
  • 24
    • 0027527563 scopus 로고
    • Peptide binding heat-shock proteins in the endoplasmic reticulum: Role in immune response to cancer and in antigen presentation
    • Srivastava, P. K. 1993. Peptide binding heat-shock proteins in the endoplasmic reticulum: role in immune response to cancer and in antigen presentation. Adv. Cancer Res. 62:153.
    • (1993) Adv. Cancer Res. , vol.62 , pp. 153
    • Srivastava, P.K.1
  • 27
    • 0032526344 scopus 로고    scopus 로고
    • Specific immune induction following DNA-based immunization through in vivo transfection and activation of macrophages/antigen-presenting cells
    • Chattergoon, M. A., T. M. Robinson, J. D. Boyer, and D. B. Weiner. 1998. Specific immune induction following DNA-based immunization through in vivo transfection and activation of macrophages/antigen-presenting cells. J. Immunol. 160:5707.
    • (1998) J. Immunol. , vol.160 , pp. 5707
    • Chattergoon, M.A.1    Robinson, T.M.2    Boyer, J.D.3    Weiner, D.B.4
  • 28
    • 0033198048 scopus 로고    scopus 로고
    • Distribution fate and mechanism of immune modulation following mucosal delivery of plasmid DNA encoding IL-10
    • Chun, S., M. Daheshia, S. Lee, S. K. Eo, and B. T. Rouse. 1999. Distribution fate and mechanism of immune modulation following mucosal delivery of plasmid DNA encoding IL-10. J. Immunol. 163:2393.
    • (1999) J. Immunol. , vol.163 , pp. 2393
    • Chun, S.1    Daheshia, M.2    Lee, S.3    Eo, S.K.4    Rouse, B.T.5
  • 29
    • 0026481133 scopus 로고
    • Generation of large numbers of dendritic cells from mouse bone marrow cultures supplemented with granulocyte/macrophage colony-stimulating factor
    • Inaba, K., M. Inaba, N. Romani, H. Aya, M. Deguchi, S. Ikehara, S. Muramatsu, and R. M. Steinman. 1992. Generation of large numbers of dendritic cells from mouse bone marrow cultures supplemented with granulocyte/macrophage colony-stimulating factor. J. Exp. Med. 176:1693.
    • (1992) J. Exp. Med. , vol.176 , pp. 1693
    • Inaba, K.1    Inaba, M.2    Romani, N.3    Aya, H.4    Deguchi, M.5    Ikehara, S.6    Muramatsu, S.7    Steinman, R.M.8
  • 31
    • 0025753142 scopus 로고
    • Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein
    • Flaherty, K. M., D. B. McKay, W. Kabsch, and K. C. Holmes. 1991. Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. Prof. Natl. Acad. Sci. USA 88:5041.
    • (1991) Prof. Natl. Acad. Sci. USA , vol.88 , pp. 5041
    • Flaherty, K.M.1    McKay, D.B.2    Kabsch, W.3    Holmes, K.C.4
  • 32
    • 0024393778 scopus 로고
    • Peptide biding and release by proteins implicated as catalysts of protein assembly
    • Flynn, G. C., T. G. Chappell, and J. E. Rothman. 1989. Peptide biding and release by proteins implicated as catalysts of protein assembly. Science 245:385.
    • (1989) Science , vol.245 , pp. 385
    • Flynn, G.C.1    Chappell, T.G.2    Rothman, J.E.3
  • 34
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
    • Panaretou, B., C. Prodromou, S. M. Roe, R. O'Brien, J. E. Ladbury, P. W. Piper, and L. H. Pearl. 1998. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J. 17:4829.
    • (1998) EMBO J. , vol.17 , pp. 4829
    • Panaretou, B.1    Prodromou, C.2    Roe, S.M.3    O'Brien, R.4    Ladbury, J.E.5    Piper, P.W.6    Pearl, L.H.7
  • 36
    • 0031054687 scopus 로고    scopus 로고
    • Interaction of endoplasmic reticulum chaperone GRP94 with peptide substrates in adenine nucleotide-independent
    • Wearsch, P. A., and C. V. Nicchitta. 1997. Interaction of endoplasmic reticulum chaperone GRP94 with peptide substrates in adenine nucleotide-independent. J. Biol. Chem. 272:5152.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5152
    • Wearsch, P.A.1    Nicchitta, C.V.2
  • 38
    • 0032539709 scopus 로고    scopus 로고
    • Two chaperone sits in Hsp20 differing in substrate specificity and ATP dependence
    • Scheibel, T., T. Weikl, and J. Buchner. 1998. Two chaperone sits in Hsp20 differing in substrate specificity and ATP dependence. Proc. Natl. Acad. Sci. USA 95:1495.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1495
    • Scheibel, T.1    Weikl, T.2    Buchner, J.3
  • 39
    • 0028301079 scopus 로고
    • Comparison of tumor-specific immunogenicities of stress-induced proteins gp96, hsp90, and hsp70
    • Udono, H., and P. K. Srivastava. 1994. Comparison of tumor-specific immunogenicities of stress-induced proteins gp96, hsp90, and hsp70. J. Immunol. 152: 5398.
    • (1994) J. Immunol. , vol.152 , pp. 5398
    • Udono, H.1    Srivastava, P.K.2
  • 40
    • 0033103513 scopus 로고    scopus 로고
    • Calreticulin, a peptide-binding chaperone of the endoplasmic reticulum, elicits tumor and peptide specific immunity
    • Babu, S., and P. K. Srivastava. 1999. Calreticulin, a peptide-binding chaperone of the endoplasmic reticulum, elicits tumor and peptide specific immunity. J. Exp. Med. 189:797.
    • (1999) J. Exp. Med. , vol.189 , pp. 797
    • Babu, S.1    Srivastava, P.K.2
  • 41
    • 0033152788 scopus 로고    scopus 로고
    • Calreticulin displays in vivo peptide binding activity and can elicit cytotoxic T lymphocyte responses against bound peptides
    • Nair, S., P. A. Wearsch, D. A. Mitchell, J. J. Wassenberg, E. Gilboa, and C. V. Nicchitta. 1999. Calreticulin displays in vivo peptide binding activity and can elicit cytotoxic T lymphocyte responses against bound peptides. J. Immunol. 162:6426.
    • (1999) J. Immunol. , vol.162 , pp. 6426
    • Nair, S.1    Wearsch, P.A.2    Mitchell, D.A.3    Wassenberg, J.J.4    Gilboa, E.5    Nicchitta, C.V.6
  • 42
    • 0024392717 scopus 로고
    • A peptide binding protein having a role in antigen presentation is a member of the HSP70 heat shock family
    • Vanbuskirk, A., B. L. Crump, E. Margoliash, and S. K. Pierce. 1989. A peptide binding protein having a role in antigen presentation is a member of the HSP70 heat shock family. J. Exp. Med. 170:1799.
    • (1989) J. Exp. Med. , vol.170 , pp. 1799
    • Vanbuskirk, A.1    Crump, B.L.2    Margoliash, E.3    Pierce, S.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.