메뉴 건너뛰기




Volumn 204, Issue 3, 2007, Pages 525-532

Influence of translation efficiency of homologous viral proteins on the endogenous presentation of CD8+ T cell epitopes

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; EPITOPE; EPSTEIN BARR VIRUS ENCODED NUCLEAR ANTIGEN 1; GAMMA INTERFERON; GLYCINE; MAJOR HISTOCOMPATIBILITY ANTIGEN; POLYPEPTIDE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 33947411798     PISSN: 00221007     EISSN: 00221007     Source Type: Journal    
DOI: 10.1084/jem.20062508     Document Type: Article
Times cited : (39)

References (39)
  • 1
    • 17644393143 scopus 로고    scopus 로고
    • Understanding presentation of viral antigens to CD8+ T cells in vivo: The key to rational vaccine design
    • Yewdell, J.W., and S.M. Haeryfar. 2005. Understanding presentation of viral antigens to CD8+ T cells in vivo: the key to rational vaccine design. Annu. Rev. Immunol. 23:651-682.
    • (2005) Annu. Rev. Immunol , vol.23 , pp. 651-682
    • Yewdell, J.W.1    Haeryfar, S.M.2
  • 2
    • 0346521283 scopus 로고    scopus 로고
    • Making sense of mass destruction: Quantitating MHC class I antigen presentation
    • Yewdell, J.W., E. Reits, and J. Neefjes. 2003. Making sense of mass destruction: quantitating MHC class I antigen presentation. Nat. Rev. Immunol. 3:952-961.
    • (2003) Nat. Rev. Immunol , vol.3 , pp. 952-961
    • Yewdell, J.W.1    Reits, E.2    Neefjes, J.3
  • 3
    • 0035060172 scopus 로고    scopus 로고
    • At the crossroads of cell biology and immunology: DRiPs and other sources of peptide ligands for MHC class I molecules
    • Yewdell, J.W., U. Schubert, and J.R. Bennink. 2001. At the crossroads of cell biology and immunology: DRiPs and other sources of peptide ligands for MHC class I molecules. J. Cell Sci. 114:845-851.
    • (2001) J. Cell Sci , vol.114 , pp. 845-851
    • Yewdell, J.W.1    Schubert, U.2    Bennink, J.R.3
  • 4
    • 0036777957 scopus 로고    scopus 로고
    • The importance of the proteasome and subsequent proteolytic steps in the generation of antigenic peptides
    • Goldberg, A.L., P. Cascio, T. Saric, and K.L. Rock. 2002. The importance of the proteasome and subsequent proteolytic steps in the generation of antigenic peptides. Mol. Immunol. 39:147-164.
    • (2002) Mol. Immunol , vol.39 , pp. 147-164
    • Goldberg, A.L.1    Cascio, P.2    Saric, T.3    Rock, K.L.4
  • 5
    • 0026764311 scopus 로고
    • Proteolysis, proteasomes and antigen presentation
    • Goldberg, A.L., and K.L. Rock. 1992. Proteolysis, proteasomes and antigen presentation. Nature. 357:375-379.
    • (1992) Nature , vol.357 , pp. 375-379
    • Goldberg, A.L.1    Rock, K.L.2
  • 6
    • 0036218697 scopus 로고    scopus 로고
    • Producing nature's genechips: The generation of peptides for display by MHC class I molecules
    • Shastri, N., S. Schwab, and T. Serwold. 2002. Producing nature's genechips: the generation of peptides for display by MHC class I molecules. Annu. Rev. Immunol. 20:463-493.
    • (2002) Annu. Rev. Immunol , vol.20 , pp. 463-493
    • Shastri, N.1    Schwab, S.2    Serwold, T.3
  • 7
    • 0037341047 scopus 로고    scopus 로고
    • The calculus of immunity: Quantitating antigen processing
    • Lehner, P.J. 2003. The calculus of immunity: quantitating antigen processing. Immunity. 18:315-317.
    • (2003) Immunity , vol.18 , pp. 315-317
    • Lehner, P.J.1
  • 8
    • 0028069388 scopus 로고
    • CDR3 length in antigen-specific immune receptors
    • Rock, E.P., P.R. Sibbald, M.M. Davis, and Y.H. Chien. 1994. CDR3 length in antigen-specific immune receptors. J. Exp. Med. 179:323-328.
    • (1994) J. Exp. Med , vol.179 , pp. 323-328
    • Rock, E.P.1    Sibbald, P.R.2    Davis, M.M.3    Chien, Y.H.4
  • 9
    • 0031032422 scopus 로고    scopus 로고
    • The proteasome-specific inhibitor lactacystin blocks presentation of cytotoxic T lymphocyte epitopes in human and murine cells
    • Cerundolo, V., A. Benham, V. Braud, S. Mukherjee, K. Gould, B. Macino, J. Neefjes, and A. Townsend. 1997. The proteasome-specific inhibitor lactacystin blocks presentation of cytotoxic T lymphocyte epitopes in human and murine cells. Eur. J. Immunol. 27:336-341.
    • (1997) Eur. J. Immunol , vol.27 , pp. 336-341
    • Cerundolo, V.1    Benham, A.2    Braud, V.3    Mukherjee, S.4    Gould, K.5    Macino, B.6    Neefjes, J.7    Townsend, A.8
  • 11
    • 0041971307 scopus 로고    scopus 로고
    • Self-inhibition of synthesis and antigen presentation by Epstein-Barr virus-encoded EBNA1
    • Yin, Y., B. Manoury, and R. Fahraeus. 2003. Self-inhibition of synthesis and antigen presentation by Epstein-Barr virus-encoded EBNA1. Science. 301:1371-1374.
    • (2003) Science , vol.301 , pp. 1371-1374
    • Yin, Y.1    Manoury, B.2    Fahraeus, R.3
  • 12
    • 0030775380 scopus 로고    scopus 로고
    • Inhibition of ubiquitin/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1
    • Levitskaya, J., A. Sharipo, A. Leonchiks, A. Ciechanover, and M.G. Masucci. 1997. Inhibition of ubiquitin/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1. Proc. Natl. Acad. Sci. USA. 94:12616-12621.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12616-12621
    • Levitskaya, J.1    Sharipo, A.2    Leonchiks, A.3    Ciechanover, A.4    Masucci, M.G.5
  • 16
    • 0030239693 scopus 로고    scopus 로고
    • Defective ribosomal products (DRiPs): A major source of antigenic peptides for MHC class I molecules?
    • Yewdell, J.W., L.C. Anton, and J.R. Bennink. 1996. Defective ribosomal products (DRiPs): a major source of antigenic peptides for MHC class I molecules? J. Immunol. 157:1823-1826.
    • (1996) J. Immunol , vol.157 , pp. 1823-1826
    • Yewdell, J.W.1    Anton, L.C.2    Bennink, J.R.3
  • 17
    • 29144447995 scopus 로고    scopus 로고
    • Serendipity strikes twice: The discovery and rediscovery of defective ribosomal products (DRiPS)
    • Yewdell, J.W. 2005. Serendipity strikes twice: the discovery and rediscovery of defective ribosomal products (DRiPS). Cell. Mol. Biol. 51:635-641.
    • (2005) Cell. Mol. Biol , vol.51 , pp. 635-641
    • Yewdell, J.W.1
  • 18
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • Schubert, U., L.C. Anton, J. Gibbs, C.C. Norbury, J.W. Yewdell, and J.R. Bennink. 2000. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature. 404:770-774.
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 19
    • 0032866173 scopus 로고    scopus 로고
    • Inhibition of antigen presentation by the glycine/alanine repeat domain is not conserved in simian homologues of Epstein-Barr virus nuclear antigen 1
    • Blake, N.W., A. Moghaddam, P. Rao, A. Kaur, R. Glickman, Y.G. Cho, A. Marchini, T. Haigh, R.P. Johnson, A.B. Rickinson, and F. Wang. 1999. Inhibition of antigen presentation by the glycine/alanine repeat domain is not conserved in simian homologues of Epstein-Barr virus nuclear antigen 1. J. Virol. 73:7381-7389.
    • (1999) J. Virol , vol.73 , pp. 7381-7389
    • Blake, N.W.1    Moghaddam, A.2    Rao, P.3    Kaur, A.4    Glickman, R.5    Cho, Y.G.6    Marchini, A.7    Haigh, T.8    Johnson, R.P.9    Rickinson, A.B.10    Wang, F.11
  • 20
    • 0029113391 scopus 로고
    • Overexpression of an epitope-tagged beta-tubulin in Chinese hamster ovary cells causes an increase in endogenous alpha-tubulin synthesis
    • Gonzalez-Garay, M.L., and F. Cabral. 1995. Overexpression of an epitope-tagged beta-tubulin in Chinese hamster ovary cells causes an increase in endogenous alpha-tubulin synthesis. Cell Motil. Cytoskeleton. 31:259-272.
    • (1995) Cell Motil. Cytoskeleton , vol.31 , pp. 259-272
    • Gonzalez-Garay, M.L.1    Cabral, F.2
  • 21
    • 0030849769 scopus 로고    scopus 로고
    • Localization, quantitation, and in situ detection of specific peptide-MHC class I complexes using a monoclonal antibody
    • Porgador, A., J.W. Yewdell, Y. Deng, J.R. Bennink, and R.N. Germain. 1997. Localization, quantitation, and in situ detection of specific peptide-MHC class I complexes using a monoclonal antibody. Immunity. 6:715-726.
    • (1997) Immunity , vol.6 , pp. 715-726
    • Porgador, A.1    Yewdell, J.W.2    Deng, Y.3    Bennink, J.R.4    Germain, R.N.5
  • 23
    • 15244353816 scopus 로고    scopus 로고
    • Epstein-Barr virus with the latent infection nuclear antigen 3B completely deleted is still competent for B-cell growth transformation in vitro
    • Chen, A., M. Divisconte, X. Jiang, C. Quink, and F. Wang. 2005. Epstein-Barr virus with the latent infection nuclear antigen 3B completely deleted is still competent for B-cell growth transformation in vitro. J. Virol. 79:4506-4509.
    • (2005) J. Virol , vol.79 , pp. 4506-4509
    • Chen, A.1    Divisconte, M.2    Jiang, X.3    Quink, C.4    Wang, F.5
  • 24
    • 9644259300 scopus 로고    scopus 로고
    • Human cytomegalovirus: Clinical aspects, immune regulation, and emerging treatments
    • Gandhi, M.K., and R. Khanna. 2004. Human cytomegalovirus: clinical aspects, immune regulation, and emerging treatments. Lancet Infect. Dis. 4:725-738.
    • (2004) Lancet Infect. Dis , vol.4 , pp. 725-738
    • Gandhi, M.K.1    Khanna, R.2
  • 25
    • 5144233488 scopus 로고    scopus 로고
    • Strategies and mechanisms for host and pathogen survival in acute and persistent viral infections
    • Hilleman, M.R. 2004. Strategies and mechanisms for host and pathogen survival in acute and persistent viral infections. Proc. Natl. Acad. Sci. USA. 101(Suppl 2):14560-14566.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , Issue.SUPPL. 2 , pp. 14560-14566
    • Hilleman, M.R.1
  • 26
    • 20444463584 scopus 로고    scopus 로고
    • Applications of emerging immunotherapeutic strategies for Epstein-Barr virus-associated malignancies
    • Khanna, R., D.J. Moss, and M. Gandhi. 2005. Applications of emerging immunotherapeutic strategies for Epstein-Barr virus-associated malignancies. Nature Clinical Practice. Oncolcogy. 2:138-149.
    • (2005) Nature Clinical Practice. Oncolcogy , vol.2 , pp. 138-149
    • Khanna, R.1    Moss, D.J.2    Gandhi, M.3
  • 27
    • 0033758794 scopus 로고    scopus 로고
    • Role of cytotoxic T lymphocytes in Epstein-Barr virus-associated diseases
    • Khanna, R., and S.R. Burrows. 2000. Role of cytotoxic T lymphocytes in Epstein-Barr virus-associated diseases. Annu. Rev. Microbiol. 54:19-48.
    • (2000) Annu. Rev. Microbiol , vol.54 , pp. 19-48
    • Khanna, R.1    Burrows, S.R.2
  • 28
    • 5644295431 scopus 로고    scopus 로고
    • Epstein-Barr virus: Exploiting the immune system by interfering with defective ribosomal products
    • Apcher, S., R. Fahraeus, and B. Manoury. 2004. Epstein-Barr virus: exploiting the immune system by interfering with defective ribosomal products. Microbes Infect. 6:1212-1218.
    • (2004) Microbes Infect , vol.6 , pp. 1212-1218
    • Apcher, S.1    Fahraeus, R.2    Manoury, B.3
  • 29
    • 33745833084 scopus 로고    scopus 로고
    • The DRiP hypothesis decennial: Support, controversy, refinement and extension
    • Yewdell, J.W., and C.V. Nicchitta. 2006. The DRiP hypothesis decennial: support, controversy, refinement and extension. Trends Immunol. 27:368-373.
    • (2006) Trends Immunol , vol.27 , pp. 368-373
    • Yewdell, J.W.1    Nicchitta, C.V.2
  • 30
    • 0035500453 scopus 로고    scopus 로고
    • Cutting edge: Neosynthesis is required for the presentation of a T cell epitope from a long-lived viral protein
    • Khan, S., R. de Giuli, G. Schmidtke, M. Bruns, M. Buchmeier, M. van den Broek, and M. Groettrup. 2001. Cutting edge: neosynthesis is required for the presentation of a T cell epitope from a long-lived viral protein. J. Immunol. 167:4801-4804.
    • (2001) J. Immunol , vol.167 , pp. 4801-4804
    • Khan, S.1    de Giuli, R.2    Schmidtke, G.3    Bruns, M.4    Buchmeier, M.5    van den Broek, M.6    Groettrup, M.7
  • 32
    • 14044265100 scopus 로고    scopus 로고
    • Regulated folding of tyrosinase in the endoplasmic reticulum demonstrates that misfolded full-length proteins are efficient substrates for class I processing and presentation
    • Ostankovitch, M., V. Robila, and V.H. Engelhard. 2005. Regulated folding of tyrosinase in the endoplasmic reticulum demonstrates that misfolded full-length proteins are efficient substrates for class I processing and presentation. J. Immunol. 174:2544-2551.
    • (2005) J. Immunol , vol.174 , pp. 2544-2551
    • Ostankovitch, M.1    Robila, V.2    Engelhard, V.H.3
  • 33
    • 0036396551 scopus 로고    scopus 로고
    • Codon modified human papillomavirus type 16 E7 DNA vaccine enhances cytotoxic T-lymphocyte induction and anti-tumour activity
    • Liu, W.J., F. Gao, K.N. Zhao, W. Zhao, G.J. Fernando, R. Thomas, and I.H. Frazer. 2002. Codon modified human papillomavirus type 16 E7 DNA vaccine enhances cytotoxic T-lymphocyte induction and anti-tumour activity. Virology. 301:43-52.
    • (2002) Virology , vol.301 , pp. 43-52
    • Liu, W.J.1    Gao, F.2    Zhao, K.N.3    Zhao, W.4    Fernando, G.J.5    Thomas, R.6    Frazer, I.H.7
  • 34
    • 0035823481 scopus 로고    scopus 로고
    • Targeting of EBNA1 for rapid intracellular degradation overrides the inhibitory effects of the Gly-Ala repeat domain and restores CD8+ T cell recognition
    • Tellam, J., M. Sherritt, S. Thomson, R. Tellam, D.J. Moss, S.R. Burrows, E. Wiertz, and R. Khanna. 2001. Targeting of EBNA1 for rapid intracellular degradation overrides the inhibitory effects of the Gly-Ala repeat domain and restores CD8+ T cell recognition. J. Biol. Chem. 276:33353-33360.
    • (2001) J. Biol. Chem , vol.276 , pp. 33353-33360
    • Tellam, J.1    Sherritt, M.2    Thomson, S.3    Tellam, R.4    Moss, D.J.5    Burrows, S.R.6    Wiertz, E.7    Khanna, R.8
  • 36
    • 0025370022 scopus 로고
    • A cultured human renal epithelioid cell line responsive to vasoactive intestinal peptide
    • Simmons, N.L. 1990. A cultured human renal epithelioid cell line responsive to vasoactive intestinal peptide. Exp. Physiol. 75:309-319.
    • (1990) Exp. Physiol , vol.75 , pp. 309-319
    • Simmons, N.L.1
  • 39
    • 0026681729 scopus 로고
    • Localization of Epstein-Barr virus cytotoxic T cell epitopes using recombinant vaccinia: Implications for vaccine development
    • Khanna, R., S.R. Burrows, M.G. Kurilla, C.A. Jacob, I.S. Misko, T.B. Sculley, E. Kieff, and D.J. Moss. 1992. Localization of Epstein-Barr virus cytotoxic T cell epitopes using recombinant vaccinia: implications for vaccine development. J. Exp. Med. 176:169-176.
    • (1992) J. Exp. Med , vol.176 , pp. 169-176
    • Khanna, R.1    Burrows, S.R.2    Kurilla, M.G.3    Jacob, C.A.4    Misko, I.S.5    Sculley, T.B.6    Kieff, E.7    Moss, D.J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.