메뉴 건너뛰기




Volumn 1, Issue 3, 2000, Pages 234-238

Impaired immune responses and altered peptide repertoire in tapasin-deficient mice

Author keywords

[No Author keywords available]

Indexed keywords

ANTIPORTER; CARRIER PROTEIN; H 2KB PROTEIN, MOUSE; H-2KB PROTEIN, MOUSE; H2 ANTIGEN; HISTOCOMPATIBILITY ANTIGEN H 2D(B); HISTOCOMPATIBILITY ANTIGEN H-2D(B); HLA ANTIGEN CLASS 1; IMMUNOGLOBULIN; PEPTIDE; TAPASIN;

EID: 0034279712     PISSN: 15292908     EISSN: None     Source Type: Journal    
DOI: 10.1038/79775     Document Type: Article
Times cited : (170)

References (42)
  • 1
    • 0031978551 scopus 로고    scopus 로고
    • Generation and TAP-mediated transport of peptides for major histocompatibility complex class I molecules
    • Momburg, F. & Hammerling, G.J. Generation and TAP-mediated transport of peptides for major histocompatibility complex class I molecules. Adv. Immunol. 68, 191-256 (1998).
    • (1998) Adv. Immunol. , vol.68 , pp. 191-256
    • Momburg, F.1    Hammerling, G.J.2
  • 2
    • 0030217926 scopus 로고    scopus 로고
    • Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP
    • Sadasivan, B. et al. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 5, 103-114 (1996).
    • (1996) Immunity , vol.5 , pp. 103-114
    • Sadasivan, B.1
  • 3
    • 0032522392 scopus 로고    scopus 로고
    • ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly
    • Lindquist, J.A., Jensen, O.N., Mann, M. & Hammerling, G. J. ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly. EMBO J. 17, 2186-2195 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2186-2195
    • Lindquist, J.A.1    Jensen, O.N.2    Mann, M.3    Hammerling, G.J.4
  • 4
    • 0032482385 scopus 로고    scopus 로고
    • A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
    • Morrice, N.A. & Powis, S.J. A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules. Curr. Biol. 8, 713-716 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 713-716
    • Morrice, N.A.1    Powis, S.J.2
  • 5
    • 0032482384 scopus 로고    scopus 로고
    • The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex
    • Hughes, E.A. & Cresswell, P. The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex. Curr. Biol. 8, 709-712 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 709-712
    • Hughes, E.A.1    Cresswell, P.2
  • 6
    • 0031938409 scopus 로고    scopus 로고
    • Genomic analysis of the Tapasin gene, located close to the TAP loci in the MHC
    • Herberg, J.A. et al. Genomic analysis of the Tapasin gene, located close to the TAP loci in the MHC. Eur. J. Immunol. 28, 459-467 (1998).
    • (1998) Eur. J. Immunol. , vol.28 , pp. 459-467
    • Herberg, J.A.1
  • 7
    • 0031669589 scopus 로고    scopus 로고
    • Sequence, linkage to H2-K, and function of mouse tapasin in MHC class I assembly
    • Grandea, A. G., 3rd et al. Sequence, linkage to H2-K, and function of mouse tapasin in MHC class I assembly. Immunogenetics 48, 260-265 (1998).
    • (1998) Immunogenetics , vol.48 , pp. 260-265
    • Grandea III, A.G.1
  • 8
    • 0030865333 scopus 로고    scopus 로고
    • A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes
    • Ortmann, B. et al. A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes. Science 277, 1306-1309 (1997).
    • (1997) Science , vol.277 , pp. 1306-1309
    • Ortmann, B.1
  • 9
    • 0028858641 scopus 로고
    • TAP associates with a unique class I conformation, whereas calnexin associates with multiple class I forms in mouse and man
    • Carreno, B. M. et al. TAP associates with a unique class I conformation, whereas calnexin associates with multiple class I forms in mouse and man. J. Immunol. 155, 4726-4733 (1995).
    • (1995) J. Immunol. , vol.155 , pp. 4726-4733
    • Carreno, B.M.1
  • 10
    • 0027988164 scopus 로고
    • Novel allele-specific, post-translational reduction in HLA class I surface expression in a mutant human B cell line
    • Greenwood, R., Shimizu, Y., Sekhon, G. S. & DeMars, R. Novel allele-specific, post-translational reduction in HLA class I surface expression in a mutant human B cell line. J. Immunol. 153, 5525-5536 (1994).
    • (1994) J. Immunol. , vol.153 , pp. 5525-5536
    • Shimizu, Y.1    Sekhon, G.S.2    DeMars, R.3
  • 11
    • 0028817950 scopus 로고
    • Dependence of peptide binding by MHC class I molecules on their interaction with TAP
    • Grandea III, A. G. et al. Dependence of peptide binding by MHC class I molecules on their interaction with TAP. Science 270, 105-108 (1995).
    • (1995) Science , vol.270 , pp. 105-108
    • Grandea III, A.G.1
  • 12
    • 0032076171 scopus 로고    scopus 로고
    • HLA-B27-restricted antigen presentation in the absence of tapasin reveals polymorphism in mechanisms of HLA class I peptide loading
    • Peh, C.A. et al. HLA-B27-restricted antigen presentation in the absence of tapasin reveals polymorphism in mechanisms of HLA class I peptide loading. Immunity 8, 531-542 (1998).
    • (1998) Immunity , vol.8 , pp. 531-542
    • Peh, C.A.1
  • 13
    • 0344096462 scopus 로고    scopus 로고
    • Retention of empty MHC class I molecules by tapasin is essential to reconstitute antigen presentation in invertebrate cells
    • Schoenhals, G.J. et al. Retention of empty MHC class I molecules by tapasin is essential to reconstitute antigen presentation in invertebrate cells. Embo J. 18, 743-753 (1999).
    • (1999) Embo J. , vol.18 , pp. 743-753
    • Schoenhals, G.J.1
  • 14
    • 0032529393 scopus 로고    scopus 로고
    • Assembly of MHC class I molecules with biosynthesized endoplasmic reticulum-targeted peptides is inefficient in insect cells and can be enhanced by protease inhibitors
    • Deng, Y. et al. Assembly of MHC class I molecules with biosynthesized endoplasmic reticulum-targeted peptides is inefficient in insect cells and can be enhanced by protease inhibitors. J. Immunol. 161, 1677-1685 (1998).
    • (1998) J. Immunol. , vol.161 , pp. 1677-1685
    • Deng, Y.1
  • 15
    • 0033615726 scopus 로고    scopus 로고
    • Tapasin enhances assembly of transporters associated with antigen processing-dependent and -independent peptides with HLA-A2 and HLA-B27 expressed in insect cells
    • Lauvau, G. et al. Tapasin enhances assembly of transporters associated with antigen processing-dependent and -independent peptides with HLA-A2 and HLA-B27 expressed in insect cells. J. Biol. Chem. 274, 31349-31358 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 31349-31358
    • Lauvau, G.1
  • 16
    • 0029974597 scopus 로고    scopus 로고
    • Allele-specific differences in the interaction of MHC class I molecules with transporters associated with antigen processing
    • Neisig, A. et al. Allele-specific differences in the interaction of MHC class I molecules with transporters associated with antigen processing. J. Immunol. 156, 3196-3206 (1996).
    • (1996) J. Immunol. , vol.156 , pp. 3196-3206
    • Neisig, A.1
  • 17
    • 0031595997 scopus 로고    scopus 로고
    • HLA-A*0201 presents TAP-dependent peptide epitopes to cytotoxic T lymphocytes in the absence of tapasin
    • Lewis, J.W., Sewell, A., Price, D. & Elliott, T. HLA-A*0201 presents TAP-dependent peptide epitopes to cytotoxic T lymphocytes in the absence of tapasin. Eur. J. Immunol. 28, 3214-3220 (1998).
    • (1998) Eur. J. Immunol. , vol.28 , pp. 3214-3220
    • Lewis, J.W.1    Sewell, A.2    Price, D.3    Elliott, T.4
  • 18
    • 0032005348 scopus 로고    scopus 로고
    • Soluble tapasin restores MHC class I expression and function in the tapasin-negative cell line .220
    • Lehner, P.J., Surman, M.J. & Cresswell, P. Soluble tapasin restores MHC class I expression and function in the tapasin-negative cell line .220. Immunity 8, 221-231 (1998).
    • (1998) Immunity , vol.8 , pp. 221-231
    • Lehner, P.J.1    Surman, M.J.2    Cresswell, P.3
  • 19
    • 0031768524 scopus 로고    scopus 로고
    • Elucidation of the genetic basis of the antigen presentation defects in the mutant cell line .220 reveals polymorphism and alternative splicing of the tapasin gene
    • Copeman, J., Bangia, N., Cross, J. C. & Cresswell, P. Elucidation of the genetic basis of the antigen presentation defects in the mutant cell line .220 reveals polymorphism and alternative splicing of the tapasin gene. Eur. J. Immunol. 28, 3783-3791 (1998).
    • (1998) Eur. J. Immunol. , vol.28 , pp. 3783-3791
    • Copeman, J.1    Bangia, N.2    Cross, J.C.3    Cresswell, P.4
  • 21
    • 0031030792 scopus 로고    scopus 로고
    • Constitutive macropinocytosis allows TAP-dependent major histocompatibility complex class I presentation of exogenous soluble antigen by bone marrow-derived dendritic cells
    • Norbury, C.C. et al. Constitutive macropinocytosis allows TAP-dependent major histocompatibility complex class I presentation of exogenous soluble antigen by bone marrow-derived dendritic cells. Eur. J. Immunol. 27, 280-288 (1997).
    • (1997) Eur. J. Immunol. , vol.27 , pp. 280-288
    • Norbury, C.C.1
  • 22
    • 0033522179 scopus 로고    scopus 로고
    • Cytotoxic T-cell immunity to virus-infected nonhaematopoietic cells requires presentation of exogenous antigen
    • Sigal, L.J., Crotty, S., Andino, R. & Rock, K.L. Cytotoxic T-cell immunity to virus-infected nonhaematopoietic cells requires presentation of exogenous antigen. Nature 398, 77-80 (1999).
    • (1999) Nature , vol.398 , pp. 77-80
    • Sigal, L.J.1    Crotty, S.2    Andino, R.3    Rock, K.L.4
  • 23
    • 0031726905 scopus 로고    scopus 로고
    • + T-cell tolerance by cross-presentation of self antigens
    • + T-cell tolerance by cross-presentation of self antigens. Immunol. Rev. 165, 267-277 (1998).
    • (1998) Immunol. Rev. , vol.165 , pp. 267-277
    • Miller, J.F.1
  • 24
    • 0025076114 scopus 로고
    • Empty MHC class I molecules come out in the cold
    • Ljunggren, H.G. et al. Empty MHC class I molecules come out in the cold. Nature 346, 476-480 (1990).
    • (1990) Nature , vol.346 , pp. 476-480
    • Ljunggren, H.G.1
  • 25
    • 0025006862 scopus 로고
    • Direct binding of peptide to empty MHC class I molecules on intact cells and in vitro
    • Schumacher, T.N. et al. Direct binding of peptide to empty MHC class I molecules on intact cells and in vitro. Cell 62, 563-567 (1990).
    • (1990) Cell , vol.62 , pp. 563-567
    • Schumacher, T.N.1
  • 26
    • 0019795661 scopus 로고
    • Cooperative interaction of B lymphocytes with antigen-specific helper T lymphocytes is MHC restricted
    • Jones, B. & Janeway, C.A. Jr Cooperative interaction of B lymphocytes with antigen-specific helper T lymphocytes is MHC restricted. Nature 292, 547-549 (1981).
    • (1981) Nature , vol.292 , pp. 547-549
    • Jones, B.1    Janeway Jr., C.A.2
  • 27
    • 0025763385 scopus 로고
    • Surface appearance and instability of empty H-2 class I molecules under physiological conditions
    • Ortiz-Navarrete, V. & Hammerling, G.J. Surface appearance and instability of empty H-2 class I molecules under physiological conditions. Proc. Natl. Acad. Sci. USA 88, 3594-3597 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3594-3597
    • Ortiz-Navarrete, V.1    Hammerling, G.J.2
  • 28
    • 0026556408 scopus 로고
    • The fate of the three subunits of major histocompatibility complex class I molecules
    • Neefjes, J.J., Smit, L., Gehrmann, M. & Ploegh, H. L. The fate of the three subunits of major histocompatibility complex class I molecules. Eur. J. Immunol. 22, 1609-1614 (1992).
    • (1992) Eur. J. Immunol. , vol.22 , pp. 1609-1614
    • Neefjes, J.J.1    Smit, L.2    Gehrmann, M.3    Ploegh, H.L.4
  • 29
    • 0027260418 scopus 로고
    • TAP2-defective RMA-S cells present Sendai virus antigen to cytotoxic T lymphocytes
    • Zhou, X. et al. TAP2-defective RMA-S cells present Sendai virus antigen to cytotoxic T lymphocytes. Eur. J. Immunol. 23, 1796-1801 (1993).
    • (1993) Eur. J. Immunol. , vol.23 , pp. 1796-1801
    • Zhou, X.1
  • 30
    • 0029813510 scopus 로고    scopus 로고
    • MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains
    • Suh, W.K. et al. MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains. J. Exp. Med. 184, 337-348 (1996).
    • (1996) J. Exp. Med. , vol.184 , pp. 337-348
    • Suh, W.K.1
  • 32
    • 0030049563 scopus 로고    scopus 로고
    • + T cell repertoire that displays both diversity and peptide specificity
    • + T cell repertoire that displays both diversity and peptide specificity. Eur. J. Immunol. 26, 288-293 (1996).
    • (1996) Eur. J. Immunol. , vol.26 , pp. 288-293
    • Sandberg, J.K.1
  • 33
    • 0029826130 scopus 로고    scopus 로고
    • Natural killer cells in MHC class I deficient mice
    • Salcedo, M. & Ljunggren, H. G. Natural killer cells in MHC class I deficient mice. Chem. Immunol. 64, 44-58 (1996).
    • (1996) Chem. Immunol. , vol.64 , pp. 44-58
    • Salcedo, M.1    Ljunggren, H.G.2
  • 34
    • 0032587063 scopus 로고    scopus 로고
    • +T cell repertoire and anti-lymphocytic choriomeningitis virus cytolytic responses
    • +T cell repertoire and anti-lymphocytic choriomeningitis virus cytolytic responses. Eur. J. Immunol. 29, 1243-1252 (1999).
    • (1999) Eur. J. Immunol. , vol.29 , pp. 1243-1252
    • Perarnau, B.1
  • 35
    • 0031080953 scopus 로고    scopus 로고
    • How HLA-DM edits the MHC class II peptide repertoire: Survival of the fittest?
    • Kropshofer, H., Hammerling, G.J. & Vogt, A. B. How HLA-DM edits the MHC class II peptide repertoire: survival of the fittest? Immunol. Today 18, 77-82 (1997).
    • (1997) Immunol. Today , vol.18 , pp. 77-82
    • Kropshofer, H.1    Hammerling, G.J.2    Vogt, A.B.3
  • 36
    • 0033452836 scopus 로고    scopus 로고
    • The impact of the non-classical MHC proteins HLA-DM and HLA-DO on loading of MHC class II molecules
    • Kropshofer, H., Hammerling, G. J. & Vogt, A. B. The impact of the non-classical MHC proteins HLA-DM and HLA-DO on loading of MHC class II molecules. Immunol. Rev. 172, 267-278 (1999).
    • (1999) Immunol. Rev. , vol.172 , pp. 267-278
    • Kropshofer, H.1    Hammerling, G.J.2    Vogt, A.B.3
  • 37
    • 0033405694 scopus 로고    scopus 로고
    • Resistance of young gelatinase B-deficient mice to experimental autoimmune encephalomyelitis and necrotizing tail lesions
    • Dubois, B. et al. Resistance of young gelatinase B-deficient mice to experimental autoimmune encephalomyelitis and necrotizing tail lesions. J. Clin. Invest. 104, 1507-1515 (1999).
    • (1999) J. Clin. Invest. , vol.104 , pp. 1507-1515
    • Dubois, B.1
  • 38
    • 0032101695 scopus 로고    scopus 로고
    • A role for HLA-DO as a co-chaperone of HLA-DM in peptide loading of MHC class II molecules
    • Kropshofer, H. et al. A role for HLA-DO as a co-chaperone of HLA-DM in peptide loading of MHC class II molecules. Embo J 17, 2971-2981 (1998).
    • (1998) Embo J , vol.17 , pp. 2971-2981
    • Kropshofer, H.1
  • 39
    • 0030273745 scopus 로고    scopus 로고
    • Triggering of natural killer cells by the costimulatory molecule CD80 (B7-1)
    • Chambers, B. J., Salcedo, M. & Ljunggren, H. G. Triggering of natural killer cells by the costimulatory molecule CD80 (B7-1). Immunity 5, 311-317 (1996).
    • (1996) Immunity , vol.5 , pp. 311-317
    • Chambers, B.J.1    Salcedo, M.2    Ljunggren, H.G.3
  • 40
    • 0033012030 scopus 로고    scopus 로고
    • An advanced culture method for generating large quantities of highly pure dendritic cells from mouse bone marrow
    • Lutz, M. B. et al. An advanced culture method for generating large quantities of highly pure dendritic cells from mouse bone marrow. J Immunol. Methods 223, 77-92 (1999).
    • (1999) J Immunol. Methods , vol.223 , pp. 77-92
    • Lutz, M.B.1
  • 41
    • 0028224014 scopus 로고
    • LacZ inducible, antigen/MHC-specific T cell hybrids
    • Sanderson, S. & Shastri, N. LacZ inducible, antigen/MHC-specific T cell hybrids. Int. Immunol. 6, 369-376 (1994).
    • (1994) Int. Immunol. , vol.6 , pp. 369-376
    • Sanderson, S.1    Shastri, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.