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Volumn 5, Issue 4, 2003, Pages 291-299

TAP-independent antigen presentation on MHC class I molecules: Lessons from Epstein-Barr virus

Author keywords

Epstein Barr virus (EBV); Hydrophobicity; MHC class I processing; TAP independence

Indexed keywords

CD8 ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1;

EID: 0037386520     PISSN: 12864579     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1286-4579(03)00031-5     Document Type: Review
Times cited : (52)

References (50)
  • 1
    • 0031895637 scopus 로고    scopus 로고
    • Mechanisms of MHC class I-restricted antigen processing
    • Pamer E., Cresswell P. Mechanisms of MHC class I-restricted antigen processing. Annu. Rev. Immunol. 16:1998;323-358.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 323-358
    • Pamer, E.1    Cresswell, P.2
  • 2
    • 0036105538 scopus 로고    scopus 로고
    • The cell biology of MHC class I antigen presentation
    • Williams A., Peh C.A., Elliott T. The cell biology of MHC class I antigen presentation. Tissue Antigens. 59:2002;3-17.
    • (2002) Tissue Antigens , vol.59 , pp. 3-17
    • Williams, A.1    Peh, C.A.2    Elliott, T.3
  • 3
    • 0036776739 scopus 로고    scopus 로고
    • MHC class I antigen processing regulated by cytosolic proteolysis - Short cuts that alter peptide generation
    • Kessler B., Glas R., Ploegh H.L. MHC class I antigen processing regulated by cytosolic proteolysis - short cuts that alter peptide generation. Mol. Immunol. 39:2002;171-179.
    • (2002) Mol. Immunol. , vol.39 , pp. 171-179
    • Kessler, B.1    Glas, R.2    Ploegh, H.L.3
  • 4
    • 0031973735 scopus 로고    scopus 로고
    • The class I antigen-processing pathway for the membrane protein tyrosinase involves translation in the endoplasmic reticulum and processing in the cytosol
    • Mosse C.A., Meadows L., Luckey C.J., Kittlesen D.J., Huczko E.L., Slingluff C.L., Shabanowitz J., Hunt D.F., Engelhard V.H. The class I antigen-processing pathway for the membrane protein tyrosinase involves translation in the endoplasmic reticulum and processing in the cytosol. J. Exp. M. 187:1998;37-48.
    • (1998) J. Exp. M , vol.187 , pp. 37-48
    • Mosse, C.A.1    Meadows, L.2    Luckey, C.J.3    Kittlesen, D.J.4    Huczko, E.L.5    Slingluff, C.L.6    Shabanowitz, J.7    Hunt, D.F.8    Engelhard, V.H.9
  • 6
    • 0026576422 scopus 로고
    • HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides
    • Wei M.L., Cresswell P. HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides. Nature. 356:1992;443-446.
    • (1992) Nature , vol.356 , pp. 443-446
    • Wei, M.L.1    Cresswell, P.2
  • 9
    • 0028130237 scopus 로고
    • T cell recognition of an HLA-A2-restricted epitope derived from a cleaved signal sequence
    • Gueguen M., Biddison W.E., Long E.O. T cell recognition of an HLA-A2-restricted epitope derived from a cleaved signal sequence. J. Exp. M. 180:1994;1989-1994.
    • (1994) J. Exp. M , vol.180 , pp. 1989-1994
    • Gueguen, M.1    Biddison, W.E.2    Long, E.O.3
  • 11
    • 0028783818 scopus 로고
    • Strictly transporter of antigen presentation (TAP)-dependent presentation of an immunodominant cytotoxic T lymphocyte epitope in the signal sequence of a virus protein
    • Hombach J., Pircher H., Tonegawa S., Zinkernagel R.M. Strictly transporter of antigen presentation (TAP)-dependent presentation of an immunodominant cytotoxic T lymphocyte epitope in the signal sequence of a virus protein. J. Exp. M. 182:1995;1615-1619.
    • (1995) J. Exp. M , vol.182 , pp. 1615-1619
    • Hombach, J.1    Pircher, H.2    Tonegawa, S.3    Zinkernagel, R.M.4
  • 12
    • 0031963752 scopus 로고    scopus 로고
    • TAP- and tapasin-dependent HLA-E surface expression correlates with the binding of an MHC class I leader peptide
    • Braud V.M., Allan D.S.J., Wilson D., McMichael A.J. TAP- and tapasin-dependent HLA-E surface expression correlates with the binding of an MHC class I leader peptide. Curr. Biol. 8:1997;1-10.
    • (1997) Curr. Biol. , vol.8 , pp. 1-10
    • Braud, V.M.1    Allan, D.S.J.2    Wilson, D.3    McMichael, A.J.4
  • 13
    • 0029062090 scopus 로고
    • An epitope-selective, transporter associated with antigen presentation (TAP)-1/2-independent pathway and a more general TAP-1/2-dependent antigen-processing pathway allow recognition of the HIV-1 envelope glycoprotein by CD8+ CTL
    • Hammond S.A., Johnson R.P., Kalams S.A., Walker B.D., Takiguchi M., Safrit J.T., Koup R.A., Siliciano R.F. An epitope-selective, transporter associated with antigen presentation (TAP)-1/2-independent pathway and a more general TAP-1/2-dependent antigen-processing pathway allow recognition of the HIV-1 envelope glycoprotein by CD8+ CTL. J. Immunol. 154:1995;6140-6156.
    • (1995) J. Immunol. , vol.154 , pp. 6140-6156
    • Hammond, S.A.1    Johnson, R.P.2    Kalams, S.A.3    Walker, B.D.4    Takiguchi, M.5    Safrit, J.T.6    Koup, R.A.7    Siliciano, R.F.8
  • 14
    • 0032555922 scopus 로고    scopus 로고
    • Major histocompatibility complex class I viral antigen processing in the secretory pathway defined by the trans-Golgi network protease furin
    • Gil-Torregrosa B.C., Raul Castano A., Del Val M. Major histocompatibility complex class I viral antigen processing in the secretory pathway defined by the trans-Golgi network protease furin. J. Exp. M. 188:1998;1105-1116.
    • (1998) J. Exp. M , vol.188 , pp. 1105-1116
    • Gil-Torregrosa, B.C.1    Raul Castano, A.2    Del Val, M.3
  • 15
    • 0032936651 scopus 로고    scopus 로고
    • Intracellular delivery of a cytotoxic T-lymphocyte epitope peptide by pertussis toxin to major histocompatibility complex class I without involvement of the cytosolic class I antigen processing pathway
    • Carbonetti N.H., Irish T.J., Chen C.H., O'Connell C.B., Hadley G.A., McNamara U., Tuskan R.G., Lewis G.K. Intracellular delivery of a cytotoxic T-lymphocyte epitope peptide by pertussis toxin to major histocompatibility complex class I without involvement of the cytosolic class I antigen processing pathway. Infect. Immun. 67:1999;602-607.
    • (1999) Infect. Immun. , vol.67 , pp. 602-607
    • Carbonetti, N.H.1    Irish, T.J.2    Chen, C.H.3    O'Connell, C.B.4    Hadley, G.A.5    McNamara, U.6    Tuskan, R.G.7    Lewis, G.K.8
  • 16
    • 0035877241 scopus 로고    scopus 로고
    • TAP-independent presentation of CTL epitopes by trojan antigens
    • Lu J., Wettstein P.J., Higashimoto Y., Appella E., Celis E. TAP-independent presentation of CTL epitopes by trojan antigens. J. Immunol. 166:2001;7063-7071.
    • (2001) J. Immunol. , vol.166 , pp. 7063-7071
    • Lu, J.1    Wettstein, P.J.2    Higashimoto, Y.3    Appella, E.4    Celis, E.5
  • 17
    • 1842407159 scopus 로고    scopus 로고
    • Two novel routes of transporter associated with antigen processing (TAP)-independent major histocompatibility complex class I antigen processing
    • Snyder H.L., Bacik I., Bennink J.R., Kearns G.T., Behrens T.W., Bachi T., Orlowski M., Yewdell J.W. Two novel routes of transporter associated with antigen processing (TAP)-independent major histocompatibility complex class I antigen processing. J. Exp. M. 186:1997;1087-1098.
    • (1997) J. Exp. M , vol.186 , pp. 1087-1098
    • Snyder, H.L.1    Bacik, I.2    Bennink, J.R.3    Kearns, G.T.4    Behrens, T.W.5    Bachi, T.6    Orlowski, M.7    Yewdell, J.W.8
  • 18
    • 0030912070 scopus 로고    scopus 로고
    • Immediate early and early lytic cycle proteins are frequent targets of the Epstein-Barr virus-induced cytotoxic T cell response
    • Steven N.M., Annels N.E., Kumar A., Leese A.M., Kurilla M.G., Rickinson A.B. Immediate early and early lytic cycle proteins are frequent targets of the Epstein-Barr virus-induced cytotoxic T cell response. J. Exp. M. 185:1997;1605-1617.
    • (1997) J. Exp. M , vol.185 , pp. 1605-1617
    • Steven, N.M.1    Annels, N.E.2    Kumar, A.3    Leese, A.M.4    Kurilla, M.G.5    Rickinson, A.B.6
  • 19
    • 0033650989 scopus 로고    scopus 로고
    • Epstein-Barr virus latency: LMP2, a regulator or means for Epstein-Barr virus persistence?
    • Longnecker R. Epstein-Barr virus latency: LMP2, a regulator or means for Epstein-Barr virus persistence? Adv. Cancer Res. 79:2000;175-200.
    • (2000) Adv. Cancer Res. , vol.79 , pp. 175-200
    • Longnecker, R.1
  • 20
    • 0029811941 scopus 로고    scopus 로고
    • Transporter (TAP)-independent processing of a multiple membrane-spanning protein, the Epstein-Barr virus latent membrane protein 2
    • Lee S.P., Thomas W.A., Blake N.W., Rickinson A.B. Transporter (TAP)-independent processing of a multiple membrane-spanning protein, the Epstein-Barr virus latent membrane protein 2. Eur. J. Immunol. 26:1996;1875-1883.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 1875-1883
    • Lee, S.P.1    Thomas, W.A.2    Blake, N.W.3    Rickinson, A.B.4
  • 21
    • 0030013725 scopus 로고    scopus 로고
    • Peptide transporter (TAP-1 and TAP-2)-independent endogenous processing of Epstein-Barr virus (EBV) latent membrane protein 2A: Implications for cytotoxic T-lymphocyte control of EBV-associated malignancies
    • Khanna R., Burrows S.R., Moss D.J., Silins S.L. Peptide transporter (TAP-1 and TAP-2)-independent endogenous processing of Epstein-Barr virus (EBV) latent membrane protein 2A: implications for cytotoxic T-lymphocyte control of EBV-associated malignancies. J. Virol. 70:1996;5357-5362.
    • (1996) J. Virol. , vol.70 , pp. 5357-5362
    • Khanna, R.1    Burrows, S.R.2    Moss, D.J.3    Silins, S.L.4
  • 23
    • 0035886881 scopus 로고    scopus 로고
    • Processing of a multiple membrane spanning Epstein-Barr virus protein for CD8(+) T cell recognition reveals a proteasome-dependent, transporter associated with antigen processing-independent pathway
    • Lautscham G., Mayrhofer S., Taylor G., Haigh T., Leese A., Rickinson A., Blake N. Processing of a multiple membrane spanning Epstein-Barr virus protein for CD8(+) T cell recognition reveals a proteasome-dependent, transporter associated with antigen processing-independent pathway. J. Exp. M. 194:2001;1053-1068.
    • (2001) J. Exp. M , vol.194 , pp. 1053-1068
    • Lautscham, G.1    Mayrhofer, S.2    Taylor, G.3    Haigh, T.4    Leese, A.5    Rickinson, A.6    Blake, N.7
  • 26
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • Wiertz E.J., Tortorella D., Bogyo M., Yu J., Mothes W., Jones T.R., Rapoport T.A., Ploegh H.L. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature. 384:1996;432-438.
    • (1996) Nature , vol.384 , pp. 432-438
    • Wiertz, E.J.1    Tortorella, D.2    Bogyo, M.3    Yu, J.4    Mothes, W.5    Jones, T.R.6    Rapoport, T.A.7    Ploegh, H.L.8
  • 27
    • 0033725154 scopus 로고    scopus 로고
    • Export of antigenic peptides from the endoplasmic reticulum intersects with retrograde protein translocation through the Sec61p channel
    • Koopmann J.O., Albring J., Huter E., Bulbuc N., Spee P., Neefjes J., Hammerling G.J., Momburg F. Export of antigenic peptides from the endoplasmic reticulum intersects with retrograde protein translocation through the Sec61p channel. Immunity. 13:2000;117-127.
    • (2000) Immunity , vol.13 , pp. 117-127
    • Koopmann, J.O.1    Albring, J.2    Huter, E.3    Bulbuc, N.4    Spee, P.5    Neefjes, J.6    Hammerling, G.J.7    Momburg, F.8
  • 29
    • 0035076457 scopus 로고    scopus 로고
    • Frequent recognition of BCRF1, a late lytic cycle protein of Epstein-Barr virus, in the HLA-B*2705 context: Evidence for a TAP-independent processing
    • Saulquin X., Bodinier M., Peyrat M.A., Hislop A., Scotet E., Lang F., Bonneville M., Houssaint E. Frequent recognition of BCRF1, a late lytic cycle protein of Epstein-Barr virus, in the HLA-B*2705 context: evidence for a TAP-independent processing. Eur. J. Immunol. 31:2001;708-715.
    • (2001) Eur. J. Immunol. , vol.31 , pp. 708-715
    • Saulquin, X.1    Bodinier, M.2    Peyrat, M.A.3    Hislop, A.4    Scotet, E.5    Lang, F.6    Bonneville, M.7    Houssaint, E.8
  • 30
    • 0033522179 scopus 로고    scopus 로고
    • Cytotoxic T cell immunity to virus-infected non-haematopoietic cells requires presentation of exogenous antigen
    • Sigal L.J., Crotty S., Andino R., Rock K.L. Cytotoxic T cell immunity to virus-infected non-haematopoietic cells requires presentation of exogenous antigen. Nature. 398:1999;77-80.
    • (1999) Nature , vol.398 , pp. 77-80
    • Sigal, L.J.1    Crotty, S.2    Andino, R.3    Rock, K.L.4
  • 31
    • 0032546352 scopus 로고    scopus 로고
    • Dendritic cells and the control of immunity
    • Banchereau J., Steinman R.M. Dendritic cells and the control of immunity. Nature. 392:1998;245-252.
    • (1998) Nature , vol.392 , pp. 245-252
    • Banchereau, J.1    Steinman, R.M.2
  • 34
    • 0034671572 scopus 로고    scopus 로고
    • The importance of exogenous antigen in priming the human CD8+ T cell response: Lessons from the EBV nuclear antigen EBNA1
    • Blake N., Haigh T., Shaka'a G., Croom-Carter D., Rickinson A. The importance of exogenous antigen in priming the human CD8+ T cell response: lessons from the EBV nuclear antigen EBNA1. J. Immunol. 165:2000;7078-7087.
    • (2000) J. Immunol. , vol.165 , pp. 7078-7087
    • Blake, N.1    Haigh, T.2    Shaka'a, G.3    Croom-Carter, D.4    Rickinson, A.5
  • 35
    • 0028910938 scopus 로고
    • A phagosome-to-cytosol pathway for exogenous antigens presented on MHC class I molecules
    • Kovacsovics-Bankowski M., Rock K.L. A phagosome-to-cytosol pathway for exogenous antigens presented on MHC class I molecules. Science. 267:1995;243-246.
    • (1995) Science , vol.267 , pp. 243-246
    • Kovacsovics-Bankowski, M.1    Rock, K.L.2
  • 36
    • 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., Chambers B.J., Prescott A.R., Ljunggren H.G., Watts C. Constitutive macropinocytosis allows TAP-dependent major histocompatibility complex class I presentation of exogenous soluble antigen by bone marrow-derived dendritic cells. Eur. J. Immunol. 27:1997;280-288.
    • (1997) Eur. J. Immunol. , vol.27 , pp. 280-288
    • Norbury, C.C.1    Chambers, B.J.2    Prescott, A.R.3    Ljunggren, H.G.4    Watts, C.5
  • 37
    • 0029550235 scopus 로고
    • Class I MHC presentation of exogenous soluble antigen via macropinocytosis in bone marrow macrophages
    • Norbury C.C., Hewlett L.J., Prescott A., Shastri N., Watts C. Class I MHC presentation of exogenous soluble antigen via macropinocytosis in bone marrow macrophages. Immunity. 3:1995;783-791.
    • (1995) Immunity , vol.3 , pp. 783-791
    • Norbury, C.C.1    Hewlett, L.J.2    Prescott, A.3    Shastri, N.4    Watts, C.5
  • 38
    • 0036232611 scopus 로고    scopus 로고
    • Dendritic cells pulsed with exogenous hepatitis B surface antigen particles efficiently present epitopes to MHC class I-restricted cytotoxic T cells
    • Stober D., Trobonjaca Z., Reimann J., Schirmbeck R. Dendritic cells pulsed with exogenous hepatitis B surface antigen particles efficiently present epitopes to MHC class I-restricted cytotoxic T cells. Eur. J. Immunol. 32:2002;1099-1108.
    • (2002) Eur. J. Immunol. , vol.32 , pp. 1099-1108
    • Stober, D.1    Trobonjaca, Z.2    Reimann, J.3    Schirmbeck, R.4
  • 39
    • 0028937941 scopus 로고
    • Heat-inactivated Sendai virus can enter multiple MHC class I processing pathways and generate cytotoxic T lymphocyte responses in vivo
    • Liu T., Zhou A., Overall C., Lederer E., Ljunggren H.G., Jondal M. Heat-inactivated Sendai virus can enter multiple MHC class I processing pathways and generate cytotoxic T lymphocyte responses in vivo. J. Immunol. 154:1995;3147-3155.
    • (1995) J. Immunol. , vol.154 , pp. 3147-3155
    • Liu, T.1    Zhou, A.2    Overall, C.3    Lederer, E.4    Ljunggren, H.G.5    Jondal, M.6
  • 40
    • 0027511213 scopus 로고
    • Phagocytic processing of bacterial antigens for class I MHC presentation to T cells
    • Pfeifer J.D., Wick M.J., Roberts R.L., Findlay K., Normark S.J., Harding C.V. Phagocytic processing of bacterial antigens for class I MHC presentation to T cells. Nature. 361:1993;359-362.
    • (1993) Nature , vol.361 , pp. 359-362
    • Pfeifer, J.D.1    Wick, M.J.2    Roberts, R.L.3    Findlay, K.4    Normark, S.J.5    Harding, C.V.6
  • 42
    • 0028965525 scopus 로고
    • Hepatitus B virus small surface antigen particles are processed in a novel endosomal pathway for major histocompatability complex class I-restricted epitope presentation
    • Schirmbeck R., Melber K., Reimann J. Hepatitus B virus small surface antigen particles are processed in a novel endosomal pathway for major histocompatability complex class I-restricted epitope presentation. Eur. J. Immunol. 25:1995;1063-1070.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 1063-1070
    • Schirmbeck, R.1    Melber, K.2    Reimann, J.3
  • 45
    • 0036318698 scopus 로고    scopus 로고
    • The lytic cycle of Epstein-Barr virus is associated with decreased expression of cell surface major histocompatibility complex class I and class II molecules
    • Keating S., Prince S., Jones M., Rowe M. The lytic cycle of Epstein-Barr virus is associated with decreased expression of cell surface major histocompatibility complex class I and class II molecules. J. Virol. 76:2002;8179-8188.
    • (2002) J. Virol. , vol.76 , pp. 8179-8188
    • Keating, S.1    Prince, S.2    Jones, M.3    Rowe, M.4
  • 47
    • 0030881322 scopus 로고    scopus 로고
    • Downregulation of TAP1 in B lymphocytes by cellular and Epstein-Barr virus-encoded interleukin-10
    • Zeidler R., Eissner G., Meissner P., Uebel S., Tampe R., Lazis S., Hammerschmidt W. Downregulation of TAP1 in B lymphocytes by cellular and Epstein-Barr virus-encoded interleukin-10. Blood. 90:1997;2390-2397.
    • (1997) Blood , vol.90 , pp. 2390-2397
    • Zeidler, R.1    Eissner, G.2    Meissner, P.3    Uebel, S.4    Tampe, R.5    Lazis, S.6    Hammerschmidt, W.7


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