메뉴 건너뛰기




Volumn 46, Issue 5, 2016, Pages 1109-1118

CD8+ T cells of Listeria monocytogenes-infected mice recognize both linear and spliced proteasome products

Author keywords

CD8+ T cells; Listeria monocytogenes; MHC class I antigen processing; Proteasome; Proteasome catalyzed peptide splicing

Indexed keywords

PROTEASOME; EPITOPE; HLA ANTIGEN CLASS 1; PEPTIDE;

EID: 84960969183     PISSN: 00142980     EISSN: 15214141     Source Type: Journal    
DOI: 10.1002/eji.201545989     Document Type: Article
Times cited : (37)

References (48)
  • 1
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock, K. L., Gramm, C., Rothstein, L., Clark, K., Stein, R., Dick, L., Hwang, D. et al., Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 1994. 78: 761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7
  • 2
    • 79958772781 scopus 로고    scopus 로고
    • The role of the proteasome in the generation of MHC class I ligands and immune responses
    • Sijts, E. J. A. M. and Kloetzel, P. M., The role of the proteasome in the generation of MHC class I ligands and immune responses. Cell. Mol. Life Sci. 2011. 68: 1491-1502.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 1491-1502
    • Sijts, E.J.A.M.1    Kloetzel, P.M.2
  • 3
    • 0035873704 scopus 로고    scopus 로고
    • 26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide
    • Cascio, P., Hilton, C., Kisselev, A. F., Rock, K. L. and Goldberg, A. L., 26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide. EMBO J. 2001. 20: 2357-2366.
    • (2001) EMBO J. , vol.20 , pp. 2357-2366
    • Cascio, P.1    Hilton, C.2    Kisselev, A.F.3    Rock, K.L.4    Goldberg, A.L.5
  • 4
    • 0028179233 scopus 로고
    • Interferon-γ induces different subunit organizations and functional diversity of proteasomes
    • Aki, M., Shimbara, N., Takashina, M., Akiyama, K., Kagawa, S., Tamura, T., Tanahashi, N. et al., Interferon-γ induces different subunit organizations and functional diversity of proteasomes. J. Biochem. 1994. 115: 257-269.
    • (1994) J. Biochem. , vol.115 , pp. 257-269
    • Aki, M.1    Shimbara, N.2    Takashina, M.3    Akiyama, K.4    Kagawa, S.5    Tamura, T.6    Tanahashi, N.7
  • 6
    • 1142269466 scopus 로고    scopus 로고
    • Immune recognition of a human renal cancer antigen through post-translational protein splicing
    • Hanada, K., Yewdell, J. W. and Yang, J. C., Immune recognition of a human renal cancer antigen through post-translational protein splicing. Nature 2004. 427: 252-256.
    • (2004) Nature , vol.427 , pp. 252-256
    • Hanada, K.1    Yewdell, J.W.2    Yang, J.C.3
  • 7
    • 84896724501 scopus 로고    scopus 로고
    • A spliced antigenic peptide comprising a single spliced amino acid is produced in the proteasome by reverse splicing of a longer peptide fragment followed by trimming
    • Michaux, A., Larrieu, P., Stroobant, V., Fonteneau, J., Jotereau, F., Van Den Eynde, B. J., Moreau-Aubry, A. et al., A spliced antigenic peptide comprising a single spliced amino acid is produced in the proteasome by reverse splicing of a longer peptide fragment followed by trimming. J. Immunol. 2014. 192: 1962-1971.
    • (2014) J. Immunol. , vol.192 , pp. 1962-1971
    • Michaux, A.1    Larrieu, P.2    Stroobant, V.3    Fonteneau, J.4    Jotereau, F.5    Van Den Eynde, B.J.6    Moreau-Aubry, A.7
  • 11
    • 78650359178 scopus 로고    scopus 로고
    • Differences in the production of spliced antigenic peptides by the standard proteasome and the immunoproteasome
    • Dalet, A., Stroobant, V., Vigneron, N. and Van Den Eynde, B. J., Differences in the production of spliced antigenic peptides by the standard proteasome and the immunoproteasome. Eur. J. Immunol. 2011. 41: 39-46.
    • (2011) Eur. J. Immunol. , vol.41 , pp. 39-46
    • Dalet, A.1    Stroobant, V.2    Vigneron, N.3    Van Den Eynde, B.J.4
  • 12
    • 84857065362 scopus 로고    scopus 로고
    • Proteasome subtypes and the processing of tumor antigens: increasing antigenic diversity
    • Vigneron, N. and Van den Eynde, B. J., Proteasome subtypes and the processing of tumor antigens: increasing antigenic diversity. Curr. Opin. Immunol. 2012. 24: 84-91.
    • (2012) Curr. Opin. Immunol. , vol.24 , pp. 84-91
    • Vigneron, N.1    Van den Eynde, B.J.2
  • 14
    • 0034614889 scopus 로고    scopus 로고
    • Efficient generation of a hepatitis B virus cytotoxic T lymphocyte epitope requires the structural features of immunoproteasomes
    • Sijts, A. J. A. M., Ruppert, T., Rehermann, B., Schmidt, M., Koszinowski, U. and Kloetzel, P. M., Efficient generation of a hepatitis B virus cytotoxic T lymphocyte epitope requires the structural features of immunoproteasomes. J. Exp. Med. 2000. 191: 503-513.
    • (2000) J. Exp. Med. , vol.191 , pp. 503-513
    • Sijts, A.J.A.M.1    Ruppert, T.2    Rehermann, B.3    Schmidt, M.4    Koszinowski, U.5    Kloetzel, P.M.6
  • 16
    • 84924308777 scopus 로고    scopus 로고
    • Standard and immunoproteasomes show similar peptide degradation specificities
    • Zanker, D. and Chen, W., Standard and immunoproteasomes show similar peptide degradation specificities. Eur. J. Immunol. 2014. 44: 3500-3503.
    • (2014) Eur. J. Immunol. , vol.44 , pp. 3500-3503
    • Zanker, D.1    Chen, W.2
  • 17
    • 77949524663 scopus 로고    scopus 로고
    • Immunoproteasome LMP2 60HH variant alters MBP epitope generation and reduces the risk to develop multiple sclerosis in italian female population
    • Mishto, M., Bellavista, E., Ligorio, C., Textoris-Taube, K., Santoro, A., Giordano, M., D'Alfonso, S. et al., Immunoproteasome LMP2 60HH variant alters MBP epitope generation and reduces the risk to develop multiple sclerosis in italian female population. PLoS One 2010. 5: e9287.
    • (2010) PLoS One , vol.5 , pp. e9287
    • Mishto, M.1    Bellavista, E.2    Ligorio, C.3    Textoris-Taube, K.4    Santoro, A.5    Giordano, M.6    D'Alfonso, S.7
  • 18
    • 84944788684 scopus 로고    scopus 로고
    • Quantitative time-resolved analysis reveals intricate, differential regulation of standard- and immuno-proteasomes
    • Liepe, J., Holzhütter, H. G., Bellavista, E., Kloetzel, P. M., Stumpf, M. P. H. and Mishto, M., Quantitative time-resolved analysis reveals intricate, differential regulation of standard- and immuno-proteasomes. eLife 2015. 4: e07545 2015.
    • (2015) eLife , vol.4 , pp. e07545
    • Liepe, J.1    Holzhütter, H.G.2    Bellavista, E.3    Kloetzel, P.M.4    Stumpf, M.P.H.5    Mishto, M.6
  • 19
    • 1642512398 scopus 로고    scopus 로고
    • Protein surgery
    • Rammensee, H., Protein surgery. Nature 2004. 427: 203-204.
    • (2004) Nature , vol.427 , pp. 203-204
    • Rammensee, H.1
  • 20
    • 55949117477 scopus 로고    scopus 로고
    • Transpeptidation and reverse proteolysis and their consequences for immunity
    • Berkers, C. R., de Jong, A., Ovaa, H. and Rodenko, B., Transpeptidation and reverse proteolysis and their consequences for immunity. Int. J. Biochem. Cell Biol. 2009. 41: 66-71.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 66-71
    • Berkers, C.R.1    de Jong, A.2    Ovaa, H.3    Rodenko, B.4
  • 22
    • 84950341717 scopus 로고    scopus 로고
    • The T210M substitution in the HLA-A*02:01 gp100 epitope strongly affects overall proteasomal cleavage site usage and antigen processing
    • Textoris-Taube, K., Keller, C., Liepe, J., Henklein, P., Sidney, J., Sette, A., Kloetzel, P. et al., The T210M substitution in the HLA-A*02:01 gp100 epitope strongly affects overall proteasomal cleavage site usage and antigen processing. J. Biol. Chem. 2015. 290: 30417-30428.
    • (2015) J. Biol. Chem. , vol.290 , pp. 30417-30428
    • Textoris-Taube, K.1    Keller, C.2    Liepe, J.3    Henklein, P.4    Sidney, J.5    Sette, A.6    Kloetzel, P.7
  • 23
    • 0035253353 scopus 로고    scopus 로고
    • A novel approach of direct ex vivo epitope mapping identifies dominant and subdominant CD4 and CD8 T cell epitopes from Listeria monocytogenes
    • Geginat, G., Schenk, S., Skoberne, M., Goebel, W. and Hof, H., A novel approach of direct ex vivo epitope mapping identifies dominant and subdominant CD4 and CD8 T cell epitopes from Listeria monocytogenes. J. Immunol. 2001. 166: 1877-1884.
    • (2001) J. Immunol. , vol.166 , pp. 1877-1884
    • Geginat, G.1    Schenk, S.2    Skoberne, M.3    Goebel, W.4    Hof, H.5
  • 24
    • 33750385670 scopus 로고    scopus 로고
    • Immunoproteasomes are essential for clearance of Listeria monocytogenes in nonlymphoid tissues but not for induction of bacteria-specific CD8+ T cells
    • Strehl, B., Joeris, T., Rieger, M., Visekruna, A., Textoris-Taube, K., Kaufmann, S. H. E., Kloetzel, P. M. et al., Immunoproteasomes are essential for clearance of Listeria monocytogenes in nonlymphoid tissues but not for induction of bacteria-specific CD8+ T cells. J. Immunol. 2006. 177: 6238-6244.
    • (2006) J. Immunol. , vol.177 , pp. 6238-6244
    • Strehl, B.1    Joeris, T.2    Rieger, M.3    Visekruna, A.4    Textoris-Taube, K.5    Kaufmann, S.H.E.6    Kloetzel, P.M.7
  • 25
    • 34250167524 scopus 로고    scopus 로고
    • Rates of processing determine the immunogenicity of immunoproteasome- generated epitopes
    • Deol, P., Zaiss, D. M. W., Monaco, J. J. and Sijts, A. J. A. M., Rates of processing determine the immunogenicity of immunoproteasome- generated epitopes. J. Immunol. 2007. 178: 7557-7562.
    • (2007) J. Immunol. , vol.178 , pp. 7557-7562
    • Deol, P.1    Zaiss, D.M.W.2    Monaco, J.J.3    Sijts, A.J.A.M.4
  • 26
    • 80052679971 scopus 로고    scopus 로고
    • Proteasome immunosubunits protect against the development of CD8 T cell-mediated autoimmune diseases
    • Zaiss, D. M. W., Bekker, C. P. J., Gröne, A., Lie, B. A. and Sijts, A. J. A. M., Proteasome immunosubunits protect against the development of CD8 T cell-mediated autoimmune diseases. J. Immunol. 2011. 187: 2302-2309.
    • (2011) J. Immunol. , vol.187 , pp. 2302-2309
    • Zaiss, D.M.W.1    Bekker, C.P.J.2    Gröne, A.3    Lie, B.A.4    Sijts, A.J.A.M.5
  • 27
    • 77956533051 scopus 로고    scopus 로고
    • Deletion of immunoproteasome subunits imprints on the transcriptome and has a broad impact on peptides presented by major histocompatibility complex I molecules
    • De Verteuil, D., Muratore-Schroeder, T. L., Granados, D. P., Fortier, M., Hardy, M., Bramoullé, A., Caron, É. et al., Deletion of immunoproteasome subunits imprints on the transcriptome and has a broad impact on peptides presented by major histocompatibility complex I molecules. Mol. Cell. Proteomics 2010. 9: 2034-2047.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 2034-2047
    • De Verteuil, D.1    Muratore-Schroeder, T.L.2    Granados, D.P.3    Fortier, M.4    Hardy, M.5    Bramoullé, A.6    Caron, E.7
  • 28
    • 0035806246 scopus 로고    scopus 로고
    • Immunoproteasomes shape immunodominance hierarchies of antiviral CD8+ T cells at the levels of T cell repertoire and presentation of viral antigens
    • Chen, W., Norbury, C. C., Cho, Y., Yewdell, J. W. and Bennink, J. R., Immunoproteasomes shape immunodominance hierarchies of antiviral CD8+ T cells at the levels of T cell repertoire and presentation of viral antigens. J. Exp. Med. 2001. 193: 1319-1326.
    • (2001) J. Exp. Med. , vol.193 , pp. 1319-1326
    • Chen, W.1    Norbury, C.C.2    Cho, Y.3    Yewdell, J.W.4    Bennink, J.R.5
  • 30
    • 30744465074 scopus 로고    scopus 로고
    • Destructive cleavage of antigenic peptides either by the immunoproteasome or by the standard proteasome results in differential antigen presentation
    • Chapiro, J., Claverol, S., Piette, F., Ma, W., Stroobant, V., Guillaume, B., Gairin, J. E. et al., Destructive cleavage of antigenic peptides either by the immunoproteasome or by the standard proteasome results in differential antigen presentation. J. Immunol. 2006. 176: 1053-1061.
    • (2006) J. Immunol. , vol.176 , pp. 1053-1061
    • Chapiro, J.1    Claverol, S.2    Piette, F.3    Ma, W.4    Stroobant, V.5    Guillaume, B.6    Gairin, J.E.7
  • 31
    • 0032033695 scopus 로고    scopus 로고
    • Coordinate regulation of complex T cell populations responding to bacterial infection
    • Busch, D. H., Pilip, I. M., Vijh, S. and Pamer, E. G., Coordinate regulation of complex T cell populations responding to bacterial infection. Immunity 1998. 8: 353-362.
    • (1998) Immunity , vol.8 , pp. 353-362
    • Busch, D.H.1    Pilip, I.M.2    Vijh, S.3    Pamer, E.G.4
  • 32
    • 33749528390 scopus 로고    scopus 로고
    • Confronting complexity: real-world immunodominance in antiviral CD8+ T cell responses
    • Yewdell, J. W., Confronting complexity: real-world immunodominance in antiviral CD8+ T cell responses. Immunity 2006. 25: 533-543.
    • (2006) Immunity , vol.25 , pp. 533-543
    • Yewdell, J.W.1
  • 33
    • 84945125570 scopus 로고    scopus 로고
    • Definition of proteasomal peptide splicing rules for high-efficiency spliced peptide presentation by MHC class I molecules
    • Berkers, C. R., De Jong, A., Schuurman, K. G., Linnemann, C., Meiring, H. D., Janssen, L., Neefjes, J. J. et al., Definition of proteasomal peptide splicing rules for high-efficiency spliced peptide presentation by MHC class I molecules. J. Immunol. 2015. 195: 4085-4095.
    • (2015) J. Immunol. , vol.195 , pp. 4085-4095
    • Berkers, C.R.1    De Jong, A.2    Schuurman, K.G.3    Linnemann, C.4    Meiring, H.D.5    Janssen, L.6    Neefjes, J.J.7
  • 34
    • 0028501143 scopus 로고
    • Efficiency of MHC class I antigen processing: a quantitative analysis
    • Villanueva, M. S., Fischer, P., Feen, K. and Pamer, E. G., Efficiency of MHC class I antigen processing: a quantitative analysis. Immunity 1994. 1: 479-489.
    • (1994) Immunity , vol.1 , pp. 479-489
    • Villanueva, M.S.1    Fischer, P.2    Feen, K.3    Pamer, E.G.4
  • 35
    • 0028853674 scopus 로고
    • Listeriolysin is processed efficiently into an MHC class I-associated epitope in Listeria monocytogenes-infected cells
    • Villanueva, M. S., Sijts, A. J. A. M. and Pamer, E. G., Listeriolysin is processed efficiently into an MHC class I-associated epitope in Listeria monocytogenes-infected cells. J. Immunol. 1995. 155: 5227-5233.
    • (1995) J. Immunol. , vol.155 , pp. 5227-5233
    • Villanueva, M.S.1    Sijts, A.J.A.M.2    Pamer, E.G.3
  • 36
    • 0030749118 scopus 로고    scopus 로고
    • MHC class I antigen processing of Listeria monocytogenes proteins: implications for dominant and subdominant CTL responses
    • Pamer, E. G., Sijts, A. J. A. M., Villanueva, M. S., Busch, D. H. and Vijh, S., MHC class I antigen processing of Listeria monocytogenes proteins: implications for dominant and subdominant CTL responses. Immunol. Rev. 1997. 158: 129-136.
    • (1997) Immunol. Rev. , vol.158 , pp. 129-136
    • Pamer, E.G.1    Sijts, A.J.A.M.2    Villanueva, M.S.3    Busch, D.H.4    Vijh, S.5
  • 37
    • 0032171644 scopus 로고    scopus 로고
    • A very high level of crossreactivity is an essential feature of the T- cell receptor
    • Mason, D., A very high level of crossreactivity is an essential feature of the T- cell receptor. Immunol. Today 1998. 19: 395-404.
    • (1998) Immunol. Today , vol.19 , pp. 395-404
    • Mason, D.1
  • 38
    • 16044372545 scopus 로고    scopus 로고
    • A single residue exchange within a viral CTL epitope alters proteasome-mediated degradation resulting in lack of antigen presentation
    • Ossendorp, F., Eggers, M., Neisig, A., Ruppert, T., Groettrup, M., Sijts, A., Mengedé, E. et al., A single residue exchange within a viral CTL epitope alters proteasome-mediated degradation resulting in lack of antigen presentation. Immunity 1996. 5: 115-124.
    • (1996) Immunity , vol.5 , pp. 115-124
    • Ossendorp, F.1    Eggers, M.2    Neisig, A.3    Ruppert, T.4    Groettrup, M.5    Sijts, A.6    Mengedé, E.7
  • 40
    • 18344412660 scopus 로고    scopus 로고
    • Abrogation of CTL epitope processing by single amino acid substitution flanking the C-terminal proteasome cleavage site
    • Beekman, N. J., Van Veelen, P. A., Van Hall, T., Neisig, A., Sijts, A., Camps, M., Kloetzel, P. M. et al., Abrogation of CTL epitope processing by single amino acid substitution flanking the C-terminal proteasome cleavage site. J. Immunol. 2000. 164: 1898-1905.
    • (2000) J. Immunol. , vol.164 , pp. 1898-1905
    • Beekman, N.J.1    Van Veelen, P.A.2    Van Hall, T.3    Neisig, A.4    Sijts, A.5    Camps, M.6    Kloetzel, P.M.7
  • 41
    • 34250327986 scopus 로고    scopus 로고
    • The N-terminal flanking region of the TRP2360-368 melanoma antigen determines proteasome activator PA28 requirement for epitope liberation
    • Textoris-Taube, K., Henklein, P., Pollmann, S., Bergann, T., Weisshoff, H., Seifert, U., Drung, I. et al., The N-terminal flanking region of the TRP2360-368 melanoma antigen determines proteasome activator PA28 requirement for epitope liberation. J. Biol. Chem. 2007. 282: 12749-12754.
    • (2007) J. Biol. Chem. , vol.282 , pp. 12749-12754
    • Textoris-Taube, K.1    Henklein, P.2    Pollmann, S.3    Bergann, T.4    Weisshoff, H.5    Seifert, U.6    Drung, I.7
  • 44
    • 84898817294 scopus 로고    scopus 로고
    • Molecular alterations in proteasomes of rat liver during aging result in altered proteolytic activities
    • Gohlke, S., Mishto, M., Textoris-Taube, K., Keller, C., Giannin, C., Vasuri, F., Capizzi, E. et al., Molecular alterations in proteasomes of rat liver during aging result in altered proteolytic activities. Age 2014. 36: 57-72.
    • (2014) Age , vol.36 , pp. 57-72
    • Gohlke, S.1    Mishto, M.2    Textoris-Taube, K.3    Keller, C.4    Giannin, C.5    Vasuri, F.6    Capizzi, E.7
  • 45
    • 84940606835 scopus 로고    scopus 로고
    • The immunoproteasome ß5i subunit is a key contributor to ictogenesis in a rat model of chronic epilepsy
    • Mishto, M., Raza, M. L., de Biase, D., Ravizza, T., Vasuri, F., Martucci, M., Keller, C. et al., The immunoproteasome ß5i subunit is a key contributor to ictogenesis in a rat model of chronic epilepsy. Brain Behav. Immun. 2015. 49: 188-196.
    • (2015) Brain Behav. Immun. , vol.49 , pp. 188-196
    • Mishto, M.1    Raza, M.L.2    de Biase, D.3    Ravizza, T.4    Vasuri, F.5    Martucci, M.6    Keller, C.7
  • 46
    • 0036902105 scopus 로고    scopus 로고
    • An IFN-γ-induced aminopeptidase in the ER, ERAP I, trims precursors to MHC class I-presented peptides
    • Saric, T., Chang, S., Hattori, A., York, I. A., Markant, S., Rock, K. L., Tsujimoto, M. et al., An IFN-γ-induced aminopeptidase in the ER, ERAP I, trims precursors to MHC class I-presented peptides. Nat. Immunol. 2002. 3: 1169-1176.
    • (2002) Nat. Immunol. , vol.3 , pp. 1169-1176
    • Saric, T.1    Chang, S.2    Hattori, A.3    York, I.A.4    Markant, S.5    Rock, K.L.6    Tsujimoto, M.7
  • 47
    • 33645788632 scopus 로고    scopus 로고
    • A structural model of 20S immunoproteasomes: effect of LMP2 codon 60 polymorphism on expression, activity, intracellular localisation and insight into the regulatory mechanisms
    • Mishto, M., Santoro, A., Bellavista, E., Sessions, R., Textoris-Taube, K., Dal Piaz, F., Carrard, G. et al., A structural model of 20S immunoproteasomes: effect of LMP2 codon 60 polymorphism on expression, activity, intracellular localisation and insight into the regulatory mechanisms. Biol. Chem. 2006. 387: 417-429.
    • (2006) Biol. Chem. , vol.387 , pp. 417-429
    • Mishto, M.1    Santoro, A.2    Bellavista, E.3    Sessions, R.4    Textoris-Taube, K.5    Dal Piaz, F.6    Carrard, G.7
  • 48
    • 34249663299 scopus 로고    scopus 로고
    • Integrating epitope data into the emerging web of biomedical knowledge resources
    • Peters, B. and Sette, A., Integrating epitope data into the emerging web of biomedical knowledge resources. Nat. Rev. Immunol. 2007. 7: 485-490.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 485-490
    • Peters, B.1    Sette, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.