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Volumn 30, Issue 4, 2000, Pages 1203-1213

Increased efficiency of folding and peptide loading of mutant MHC class I molecules

Author keywords

Antigen presentation; MHC class I; Peptide loading complex; TAP; Tapasin

Indexed keywords

CALRETICULIN; HLA A2 ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PEPTIDE; TAPASIN;

EID: 0342700196     PISSN: 00142980     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1521-4141(200004)30:4<1203::AID-IMMU1203>3.0.CO;2-L     Document Type: Article
Times cited : (20)

References (48)
  • 1
    • 0031895637 scopus 로고    scopus 로고
    • Mechanisms of MHC class I-restricted antigen processing
    • Pamer, E. and Cresswell, P., Mechanisms of MHC class I-restricted antigen processing. Annu. Rev. Immunol. 1998. 16: 323-358.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 323-358
    • Pamer, E.1    Cresswell, P.2
  • 2
    • 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. and Hämmerling, G. J., ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly. EMBO J. 1998. 17: 2186-2195.
    • (1998) EMBO J. , vol.17 , pp. 2186-2195
    • Lindquist, J.A.1    Jensen, O.N.2    Mann, M.3    Hämmerling, G.J.4
  • 3
    • 0032482384 scopus 로고    scopus 로고
    • The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex
    • Hughes, E. A. and Cresswell, P., The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex. Curr. Biol. 1998. 8: 709-712.
    • (1998) Curr. Biol. , vol.8 , pp. 709-712
    • Hughes, E.A.1    Cresswell, P.2
  • 4
    • 0032482385 scopus 로고    scopus 로고
    • A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecule
    • Morrice, N. A. and Powis, S. J., A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecule. Curr. Biol. 1998. 8: 713-716.
    • (1998) Curr. Biol. , vol.8 , pp. 713-716
    • Morrice, N.A.1    Powis, S.J.2
  • 5
    • 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., Lehner, P. J., Ortmann, B., Spies, T. and Cresswell, P., Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 1996. 5: 103-114.
    • (1996) Immunity , vol.5 , pp. 103-114
    • Sadasivan, B.1    Lehner, P.J.2    Ortmann, B.3    Spies, T.4    Cresswell, P.5
  • 7
    • 0030871305 scopus 로고    scopus 로고
    • Cloning and functional characterization of a subunit of the transporter associated with antigen processing
    • Li, S., Sjogren, H. O., Hellman, U., Pettersson, R. F., Wang, P., Cloning and functional characterization of a subunit of the transporter associated with antigen processing. Proc. Natl. Acad. Sci. USA 1997. 94: 8708-8713.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8708-8713
    • Li, S.1    Sjogren, H.O.2    Hellman, U.3    Pettersson, R.F.4    Wang, P.5
  • 8
    • 0028282108 scopus 로고
    • MHC class I/ beta 2-microglobulin complexes associate with TAP transporters before peptide binding
    • Ortmann, B., Androlwicz, M. J. and Cresswell, P., MHC class I/ beta 2-microglobulin complexes associate with TAP transporters before peptide binding. Nature 1994. 368: 864-867.
    • (1994) Nature , vol.368 , pp. 864-867
    • Ortmann, B.1    Androlwicz, M.J.2    Cresswell, P.3
  • 9
    • 0028239443 scopus 로고
    • Interaction of MHC class I molecules with the transporter associated with antigen processing
    • Sun, W. K., Cohen-Doyle, M. F., Fruh, K., Wang, K., Peterson, P. A. and Williams, D. B., Interaction of MHC class I molecules with the transporter associated with antigen processing. Science 1994. 264: 1322-1326.
    • (1994) Science , vol.264 , pp. 1322-1326
    • Sun, W.K.1    Cohen-Doyle, M.F.2    Fruh, K.3    Wang, K.4    Peterson, P.A.5    Williams, D.B.6
  • 10
    • 0028817950 scopus 로고
    • Dependence of peptide binding by MHC class I molecules on their interaction with TAP
    • Grandea, A. G. r., Androlewicz, M. J., Athwal, R. S., Geraghty, D. E. and Spies, T., Dependence of peptide binding by MHC class I molecules on their interaction with TAP. Science 1995. 270: 105-108.
    • (1995) Science , vol.270 , pp. 105-108
    • Grandea, A.G.R.1    Androlewicz, M.J.2    Athwal, R.S.3    Geraghty, D.E.4    Spies, T.5
  • 11
    • 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. and Cresswell, P., Soluble tapasin restores MHC class I expression and function in the tapasin-negative cell line .220. Immunity 1998. 8: 221-231.
    • (1998) Immunity , vol.8 , pp. 221-231
    • Lehner, P.J.1    Surman, M.J.2    Cresswell, P.3
  • 12
    • 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., Solheim, J. C., Harris, M., Stroynowski, I., Connolly, J. M. and Hansen, T. H., TAP associates with a unique class I conformation, whereas calnexin associates with multiple class I forms in mouse and man. J. Immunol. 1995. 155: 4726-4733.
    • (1995) J. Immunol. , vol.155 , pp. 4726-4733
    • Carreno, B.M.1    Solheim, J.C.2    Harris, M.3    Stroynowski, I.4    Connolly, J.M.5    Hansen, T.H.6
  • 13
    • 0029813510 scopus 로고    scopus 로고
    • MHC class I molecules from ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains
    • Suh, W. K., Mitchell, E. K., Yang, Y, Peterson, P. A., Waneck, G. L. and Williams, D. B., MHC class I molecules from ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains. J. Exp. Med. 1996. 184: 337-348.
    • (1996) J. Exp. Med. , vol.184 , pp. 337-348
    • Suh, W.K.1    Mitchell, E.K.2    Yang, Y.3    Peterson, P.A.4    Waneck, G.L.5    Williams, D.B.6
  • 14
    • 0033083288 scopus 로고    scopus 로고
    • Interaction of murine MHC class I molecules with tapasin and TAP enhances peptide loading and involves the heavy chain alphas domain
    • Suh, W. K., Derby, M. A., Cohen-Doyle, M. F., Schoenhals, G. J., Fruh, K., Berzofsky, J. A. and Williams, D. B., Interaction of murine MHC class I molecules with tapasin and TAP enhances peptide loading and involves the heavy chain alphas domain. J. Immunol. 1999. 162: 1530-1540.
    • (1999) J. Immunol. , vol.162 , pp. 1530-1540
    • Suh, W.K.1    Derby, M.A.2    Cohen-Doyle, M.F.3    Schoenhals, G.J.4    Fruh, K.5    Berzofsky, J.A.6    Williams, D.B.7
  • 15
    • 0032536790 scopus 로고    scopus 로고
    • Physical and functional association of the major histocompatibility complex class I heavy chain alpha3 domain with the transporter associated with antigen processing
    • Kulig, K., Nandi, D., Bacik, I., Monaco, J. J. and Vukmanovic, S., Physical and functional association of the major histocompatibility complex class I heavy chain alpha3 domain with the transporter associated with antigen processing. J. Exp. Med. 1998. 187: 865-874.
    • (1998) J. Exp. Med. , vol.187 , pp. 865-874
    • Kulig, K.1    Nandi, D.2    Bacik, I.3    Monaco, J.J.4    Vukmanovic, S.5
  • 16
    • 0030152620 scopus 로고    scopus 로고
    • A point mutation in HLA-A*0201 results in failure to bind the TAP complex and to present virus-derived peptides to CLT
    • Peace-Brewer, A. L., Tussey, L. G., Matsui, M., Li, G., Quinn, D. G. and Frelinger, J. A., A point mutation in HLA-A*0201 results in failure to bind the TAP complex and to present virus-derived peptides to CLT. Immunity 1996. 4: 505-514.
    • (1996) Immunity , vol.4 , pp. 505-514
    • Peace-Brewer, A.L.1    Tussey, L.G.2    Matsui, M.3    Li, G.4    Quinn, D.G.5    Frelinger, J.A.6
  • 17
    • 0030198868 scopus 로고    scopus 로고
    • Point mutations in the alpha 2 domain of HLA-A2.1 define a functionally relevant interaction with TAP
    • Lewis, J. W., Neisig, A., Neefjes, J. and Elliott, T., Point mutations in the alpha 2 domain of HLA-A2.1 define a functionally relevant interaction with TAP. Curr. Biol. 1996. 6: 873-883.
    • (1996) Curr. Biol. , vol.6 , pp. 873-883
    • Lewis, J.W.1    Neisig, A.2    Neefjes, J.3    Elliott, T.4
  • 18
    • 0032482319 scopus 로고    scopus 로고
    • Evidence for successive peptide binding and quality control stages during MHC class I assembly
    • Lewis, W. L. and Elliott, T., Evidence for successive peptide binding and quality control stages during MHC class I assembly. Curr. Biol. 1998. 8: 717-720.
    • (1998) Curr. Biol. , vol.8 , pp. 717-720
    • Lewis, W.L.1    Elliott, T.2
  • 19
    • 0028838283 scopus 로고
    • Interaction between CD8 and major histocompatibility complex (MHC) class I mediated by multiple contact surfaces that include the alpha 2 and alpha 3 domains of MHC class I
    • Sun, J., Leahy, D. J. and Kavathas, P. B., Interaction between CD8 and major histocompatibility complex (MHC) class I mediated by multiple contact surfaces that include the alpha 2 and alpha 3 domains of MHC class I. J. Exp. Med. 1995. 182: 1275-1280.
    • (1995) J. Exp. Med. , vol.182 , pp. 1275-1280
    • Sun, J.1    Leahy, D.J.2    Kavathas, P.B.3
  • 20
    • 0032400955 scopus 로고    scopus 로고
    • MHC class I molecules compete in the endoplasmid reticulum for access to transporter associated with antigen processing
    • Knittler, M. R., Gülow, K., Seelig, A. and Howard, J. C., MHC class I molecules compete in the endoplasmid reticulum for access to transporter associated with antigen processing. J. Immunol. 1998. 161: 5967-5977.
    • (1998) J. Immunol. , vol.161 , pp. 5967-5977
    • Knittler, M.R.1    Gülow, K.2    Seelig, A.3    Howard, J.C.4
  • 21
    • 0026511275 scopus 로고
    • Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T-and B-cell antigen receptors and major histocompatibility complex antigens during their assembly
    • Hochstenbach, F., David, V., Watkins, S. and Brennner, M. B., Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T-and B-cell antigen receptors and major histocompatibility complex antigens during their assembly. Proc. Natl. Acad. Sci. USA 1992. 89: 4734-4738.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4734-4738
    • Hochstenbach, F.1    David, V.2    Watkins, S.3    Brennner, M.B.4
  • 23
    • 0026576422 scopus 로고
    • HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides
    • Wei, M. L. and Cresswell, P., HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides. Nature 1992. 356: 443-446.
    • (1992) Nature , vol.356 , pp. 443-446
    • Wei, M.L.1    Cresswell, P.2
  • 25
    • 0029965803 scopus 로고    scopus 로고
    • The protease inhibitor, N-acetyl-L-leucyl-L-leucyl-leucyl-L-norleucinal, decreases the pool of major histocompatibility complex class I-binding peptides and inhibits peptide trimming in the endoplasmic reticulum
    • Hughes, E. A., Ortmann, B., Surman, M. and Cresswell, P., The protease inhibitor, N-acetyl-L-leucyl-L-leucyl-leucyl-L-norleucinal, decreases the pool of major histocompatibility complex class I-binding peptides and inhibits peptide trimming in the endoplasmic reticulum. J. Exp. Med. 1996. 183: 1569-1578.
    • (1996) J. Exp. Med. , vol.183 , pp. 1569-1578
    • Hughes, E.A.1    Ortmann, B.2    Surman, M.3    Cresswell, P.4
  • 26
    • 0033598171 scopus 로고    scopus 로고
    • Nucleotide binding by TAP mediates association with peptide and relase of assembled MHC class I molecules
    • Knittler, M. R., Alberts, P., Deverson, E. V. and Howard, J. C., Nucleotide binding by TAP mediates association with peptide and relase of assembled MHC class I molecules. Curr. Biol. 1999. 9: 999-1008.
    • (1999) Curr. Biol. , vol.9 , pp. 999-1008
    • Knittler, M.R.1    Alberts, P.2    Deverson, E.V.3    Howard, J.C.4
  • 27
    • 0030981737 scopus 로고    scopus 로고
    • Regulation of MHC class I heterodimer stability and interaction with TAP by tapasin
    • Grandea, A. G. r., Lehner, P. J., Cresswell, P. and Spies, T., Regulation of MHC class I heterodimer stability and interaction with TAP by tapasin. Immunogenetics 1997. 46: 477-483.
    • (1997) Immunogenetics , vol.46 , pp. 477-483
    • Grandea, A.G.R.1    Lehner, P.J.2    Cresswell, P.3    Spies, T.4
  • 28
    • 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., Burrows, S. R., Barnden, M., Khanna, R., Cresswell, P., Moss, D. J. and McCluskey, J., HLA-B27-restricted antigen presentation in the absence of tapasin reveals polymorphism in mechanisms of HLA class I peptide loading. Immunity 1998. 8: 531-542.
    • (1998) Immunity , vol.8 , pp. 531-542
    • Peh, C.A.1    Burrows, S.R.2    Barnden, M.3    Khanna, R.4    Cresswell, P.5    Moss, D.J.6    McCluskey, J.7
  • 29
    • 0028867421 scopus 로고
    • The membrane-bound and soluble forms of HLA-G bind identical sets of endogenous peptides but differ with respect to tap association
    • Lee, N., Malacko, A. R., Ishitani, A., Chen, M. C., Bajorath, J., Marquardt, H. and Geraghty, D. E., The membrane-bound and soluble forms of HLA-G bind identical sets of endogenous peptides but differ with respect to TAP association. Immunity 1995. 3: 591-600.
    • (1995) Immunity , vol.3 , pp. 591-600
    • Lee, N.1    Malacko, A.R.2    Ishitani, A.3    Chen, M.C.4    Bajorath, J.5    Marquardt, H.6    Geraghty, D.E.7
  • 30
    • 0021952907 scopus 로고
    • Genes regulating HLA class I antigen expression in T-B lymphoblast hybrids
    • Salter, R. D., Howell, D. N. and Cresswell, P., Genes regulating HLA class I antigen expression in T-B lymphoblast hybrids. Immunogenetics 1985. 21: 235-246.
    • (1985) Immunogenetics , vol.21 , pp. 235-246
    • Salter, R.D.1    Howell, D.N.2    Cresswell, P.3
  • 31
    • 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. and Elliott, T., HLA-A*0201 presents TAP-dependent peptide epitopes to cytotoxic T lymphocytes in the absence of tapasin. Eur. J. Immunol. 1998. 28: 3214-3220.
    • (1998) Eur. J. Immunol. , vol.28 , pp. 3214-3220
    • Lewis, J.W.1    Sewell, A.2    Price, D.3    Elliott, T.4
  • 32
    • 0029974597 scopus 로고    scopus 로고
    • Allele-specific differences in the interaction of MHC class I molecules with transporters associated with antigen processing
    • Neisig, A., Wubbolts, R., Zang, X., Melief, C. and Neefjes, J., Allele-specific differences in the interaction of MHC class I molecules with transporters associated with antigen processing. J. Immunol. 1996. 156: 3196-3206.
    • (1996) J. Immunol. , vol.156 , pp. 3196-3206
    • Neisig, A.1    Wubbolts, R.2    Zang, X.3    Melief, C.4    Neefjes, J.5
  • 35
    • 0029552627 scopus 로고
    • Assembly, peptide laoding, and transport of MHC class I molecules in a calnexin-negative cell line
    • Sadasivan, B. K., Cariappa, A., Waneck, G. L. and Cresswell, P., Assembly, peptide laoding, and transport of MHC class I molecules in a calnexin-negative cell line. Cold Spring Harb. Symp. Quant. Biol. 1995. 60: 267-275.
    • (1995) Cold Spring Harb. Symp. Quant. Biol. , vol.60 , pp. 267-275
    • Sadasivan, B.K.1    Cariappa, A.2    Waneck, G.L.3    Cresswell, P.4
  • 36
    • 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., Krishna, R. M., Grandea, A. G. R., Spies, T., Peterson, P. A., Yang, Y. and Fruh, K., Retention of empty MHC class I molecules by tapasin is essential to reconstitute antigen presentation in invertebrate cells. EMBO J. 1999. 18: 743-753.
    • (1999) EMBO J. , vol.18 , pp. 743-753
    • Schoenhals, G.J.1    Krishna, R.M.2    Grandea, A.G.R.3    Spies, T.4    Peterson, P.A.5    Yang, Y.6    Fruh, K.7
  • 38
    • 0025831493 scopus 로고
    • Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution
    • Saper, M. A., Bjorkman, P. J. and Wiley, D. C., Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution. J. Mol. Biol. 1991. 219: 277-319.
    • (1991) J. Mol. Biol. , vol.219 , pp. 277-319
    • Saper, M.A.1    Bjorkman, P.J.2    Wiley, D.C.3
  • 40
    • 0026521967 scopus 로고
    • 1B "negative" mutant cell line C1R expresses a novel HLA-B35 allele, which also has a point mutation in the translation initiation codon
    • 1B "negative" mutant cell line C1R expresses a novel HLA-B35 allele, which also has a point mutation in the translation initiation codon. J. Immunol. 1992. 148: 1941-1948.
    • (1992) J. Immunol. , vol.148 , pp. 1941-1948
    • Zemmour, J.1    Little, A.M.2    Schendel, D.J.3    Parham, P.4
  • 41
    • 0023113151 scopus 로고
    • An epitope common to HLA class I and class II antigens, Ig light chains, and beta 2-microglobulin
    • Lutz, P. M. and Cresswell, P., An epitope common to HLA class I and class II antigens, Ig light chains, and beta 2-microglobulin. Immunogenetics 1987. 25: 228-233.
    • (1987) Immunogenetics , vol.25 , pp. 228-233
    • Lutz, P.M.1    Cresswell, P.2
  • 42
    • 0019806243 scopus 로고
    • Partial purification and some properties of BB7.2. A cytotoxic monoclonal antibody with specificity for HLA-A2 and a variant of HLA-A28
    • Parham, P. and Brodsky, F. M., Partial purification and some properties of BB7.2. A cytotoxic monoclonal antibody with specificity for HLA-A2 and a variant of HLA-A28. Hum. Immunol. 1981. 3: 277-299.
    • (1981) Hum. Immunol. , vol.3 , pp. 277-299
    • Parham, P.1    Brodsky, F.M.2
  • 43
    • 0019285686 scopus 로고
    • A monoclonal antibody that recognizes an antigenic determinant shared by HLA A2 and B17
    • McMichael, A. J., Parham, P., Rust, N. and Brodsky, F., A monoclonal antibody that recognizes an antigenic determinant shared by HLA A2 and B17. Hum. Immunol. 1980. 1: 121-129.
    • (1980) Hum. Immunol. , vol.1 , pp. 121-129
    • McMichael, A.J.1    Parham, P.2    Rust, N.3    Brodsky, F.4
  • 44
    • 0026500826 scopus 로고
    • Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer
    • Spies, T., Cerundolo, V., Colonna, M., Cresswell, P., Townsend, A. and DeMars, R., Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer. Nature 1992. 355: 644-646.
    • (1992) Nature , vol.355 , pp. 644-646
    • Spies, T.1    Cerundolo, V.2    Colonna, M.3    Cresswell, P.4    Townsend, A.5    DeMars, R.6
  • 45
    • 0033060098 scopus 로고    scopus 로고
    • The N-terminal region of tapasin is required to stabilize the MHC class I loading complex
    • Bangia, N., Lehner, P. J., Hughes, E. A., Surman, M., Cresswell, P., The N-terminal region of tapasin is required to stabilize the MHC class I loading complex. Eur. J. Immunol. 1999. 29: 1858-1870.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 1858-1870
    • Bangia, N.1    Lehner, P.J.2    Hughes, E.A.3    Surman, M.4    Cresswell, P.5
  • 47
    • 0024079259 scopus 로고
    • BRAGI: A comprehensive protein-modelling programme system
    • Schomburg, D., Reichelt, J., BRAGI: A comprehensive protein-modelling programme system. J. Mol. Graph. 1988. 6: 161-165.
    • (1988) J. Mol. Graph. , vol.6 , pp. 161-165
    • Schomburg, D.1    Reichelt, J.2
  • 48
    • 0021167161 scopus 로고
    • Homozygous deletions that simultaneously eliminate expressions of class I and class II antigens of EBV-transformed B-lymphoblastoid cells. I. Reduced proliferance responses of autologous and allogeneic T cells that have decreased expression of class II antigens
    • DeMars, R., Chang, C. C., Shaw, S., Reitnauer, P. J. and Sondel, P. M., Homozygous deletions that simultaneously eliminate expressions of class I and class II antigens of EBV-transformed B-lymphoblastoid cells. I. Reduced proliferance responses of autologous and allogeneic T cells that have decreased expression of class II antigens. Hum. Immunol. 1984. 11: 77-97.
    • (1984) Hum. Immunol. , vol.11 , pp. 77-97
    • DeMars, R.1    Chang, C.C.2    Shaw, S.3    Reitnauer, P.J.4    Sondel, P.M.5


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