메뉴 건너뛰기




Volumn 11, Issue 8-9, 2009, Pages 795-802

Role of tripeptidyl peptidase II in the processing of Listeria monocytogenes-derived MHC class I-presented antigenic peptides

Author keywords

Antigen presentation; Protease inhibitors, Listeria monocytogenes; Proteasome

Indexed keywords

BACTERIAL ANTIGEN; EPITOPE; ISOPROTEIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PROTEASOME; PROTEIN P60; PROTEINASE; TRIPEPTIDYL PEPTIDASE II; UNCLASSIFIED DRUG;

EID: 67650553100     PISSN: 12864579     EISSN: 1769714X     Source Type: Journal    
DOI: 10.1016/j.micinf.2009.04.019     Document Type: Article
Times cited : (4)

References (22)
  • 1
    • 0035142615 scopus 로고    scopus 로고
    • Cut and trim: generating MHC class I peptide ligands
    • Yewdell J.W., and Bennink J.R. Cut and trim: generating MHC class I peptide ligands. Curr. Opin. Immunol 13 (2001) 13-18
    • (2001) Curr. Opin. Immunol , vol.13 , pp. 13-18
    • Yewdell, J.W.1    Bennink, J.R.2
  • 2
    • 29244461714 scopus 로고    scopus 로고
    • The aminopeptidase ERAAP shapes the peptide repertoire displayed by major histocompatibility complex class I molecules
    • Hammer G.E., Gonzalez F., Champsaur M., Cado D., and Shastri N. The aminopeptidase ERAAP shapes the peptide repertoire displayed by major histocompatibility complex class I molecules. Nat. Immunol 7 (2006) 103-112
    • (2006) Nat. Immunol , vol.7 , pp. 103-112
    • Hammer, G.E.1    Gonzalez, F.2    Champsaur, M.3    Cado, D.4    Shastri, N.5
  • 4
    • 0032563221 scopus 로고    scopus 로고
    • Interferon-gamma can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase
    • Beninga J., Rock K.L., and Goldberg A.L. Interferon-gamma can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase. J. Biol. Chem. 273 (1998) 18734-18742
    • (1998) J. Biol. Chem. , vol.273 , pp. 18734-18742
    • Beninga, J.1    Rock, K.L.2    Goldberg, A.L.3
  • 5
    • 0035965357 scopus 로고    scopus 로고
    • Major histocompatibility complex class I-presented antigenic peptides are degraded in cytosolic extracts primarily by thimet oligopeptidase
    • Saric T., Beninga J., Graef C.I., Akopian T.N., Rock K.L., and Goldberg A.L. Major histocompatibility complex class I-presented antigenic peptides are degraded in cytosolic extracts primarily by thimet oligopeptidase. J. Biol. Chem. 276 (2001) 36474-36481
    • (2001) J. Biol. Chem. , vol.276 , pp. 36474-36481
    • Saric, T.1    Beninga, J.2    Graef, C.I.3    Akopian, T.N.4    Rock, K.L.5    Goldberg, A.L.6
  • 6
    • 0032499199 scopus 로고    scopus 로고
    • A proteolytic system that compensates for loss of proteasome function
    • Glas R., Bogyo M., McMaster J.S., Gaczynska M., and Ploegh H.L. A proteolytic system that compensates for loss of proteasome function. Nature 392 (1998) 618-622
    • (1998) Nature , vol.392 , pp. 618-622
    • Glas, R.1    Bogyo, M.2    McMaster, J.S.3    Gaczynska, M.4    Ploegh, H.L.5
  • 8
    • 0036776742 scopus 로고    scopus 로고
    • Beyond the proteasome: trimming, degradation and generation of MHC class I ligands by auxiliary proteases
    • Saveanu L., Fruci D., and van Endert P. Beyond the proteasome: trimming, degradation and generation of MHC class I ligands by auxiliary proteases. Mol. Immunol 39 (2002) 203-215
    • (2002) Mol. Immunol , vol.39 , pp. 203-215
    • Saveanu, L.1    Fruci, D.2    van Endert, P.3
  • 9
    • 43649106216 scopus 로고    scopus 로고
    • Role of tripeptidyl peptidase II in MHC class I antigen processing - the end of controversies?
    • Endert P. Role of tripeptidyl peptidase II in MHC class I antigen processing - the end of controversies?. Eur. J. Immunol 38 (2008) 609-613
    • (2008) Eur. J. Immunol , vol.38 , pp. 609-613
    • Endert, P.1
  • 10
    • 23944471148 scopus 로고    scopus 로고
    • Tripeptidyl-peptidase II: a multi-purpose peptidase
    • Tomkinson B., and Lindas A.C. Tripeptidyl-peptidase II: a multi-purpose peptidase. Int. J. Biochem. Cell Biol. 37 (2005) 1933-1937
    • (2005) Int. J. Biochem. Cell Biol. , vol.37 , pp. 1933-1937
    • Tomkinson, B.1    Lindas, A.C.2
  • 12
    • 0031110168 scopus 로고    scopus 로고
    • Immunodominant and subdominant CTL responses to Listeria monocytogenes infection
    • Vijh S., and Pamer E.G. Immunodominant and subdominant CTL responses to Listeria monocytogenes infection. J. Immunol 158 (1997) 3366-3371
    • (1997) J. Immunol , vol.158 , pp. 3366-3371
    • Vijh, S.1    Pamer, E.G.2
  • 13
    • 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 166 (2001) 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
  • 15
    • 6344225314 scopus 로고    scopus 로고
    • Cross-presentation of Listeria-derived CD8 T cell epitopes requires unstable bacterial translation products
    • Janda J., Schoneberger P., Skoberne M., Messerle M., Russmann H., and Geginat G. Cross-presentation of Listeria-derived CD8 T cell epitopes requires unstable bacterial translation products. J. Immunol 173 (2004) 5644-5651
    • (2004) J. Immunol , vol.173 , pp. 5644-5651
    • Janda, J.1    Schoneberger, P.2    Skoberne, M.3    Messerle, M.4    Russmann, H.5    Geginat, G.6
  • 16
    • 0032563205 scopus 로고    scopus 로고
    • Characterization and cloning of tripeptidyl peptidase II from the fruit fly, Drosophila melanogaster
    • Renn S.C., Tomkinson B., and Taghert P.H. Characterization and cloning of tripeptidyl peptidase II from the fruit fly, Drosophila melanogaster. J. Biol. Chem. 273 (1998) 19173-19182
    • (1998) J. Biol. Chem. , vol.273 , pp. 19173-19182
    • Renn, S.C.1    Tomkinson, B.2    Taghert, P.H.3
  • 18
    • 33746215297 scopus 로고    scopus 로고
    • Tripeptidyl peptidase II is the major peptidase needed to trim long antigenic precursors, but is not required for most MHC class I antigen presentation
    • York I.A., Bhutani N., Zendzian S., Goldberg A.L., and Rock K.L. Tripeptidyl peptidase II is the major peptidase needed to trim long antigenic precursors, but is not required for most MHC class I antigen presentation. J. Immunol 177 (2006) 1434-1443
    • (2006) J. Immunol , vol.177 , pp. 1434-1443
    • York, I.A.1    Bhutani, N.2    Zendzian, S.3    Goldberg, A.L.4    Rock, K.L.5
  • 19
    • 1842785206 scopus 로고    scopus 로고
    • A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation
    • Reits E., Neijssen J., Herberts C., Benckhuijsen W., Janssen L., Drijfhout J.W., and Neefjes J. A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation. Immunity 20 (2004) 495-506
    • (2004) Immunity , vol.20 , pp. 495-506
    • Reits, E.1    Neijssen, J.2    Herberts, C.3    Benckhuijsen, W.4    Janssen, L.5    Drijfhout, J.W.6    Neefjes, J.7
  • 20
    • 0035027705 scopus 로고    scopus 로고
    • Effects of an inhibitor of tripeptidyl peptidase II (Ala-Ala-Phe-chloromethylketone) and its combination with an inhibitor of the chymotrypsin-like activity of the proteasome (PSI) on apoptosis, cell cycle and proteasome activity in U937 cells
    • Bury M., Mlynarczuk I., Pleban E., Hoser G., Kawiak J., and Wojcik C. Effects of an inhibitor of tripeptidyl peptidase II (Ala-Ala-Phe-chloromethylketone) and its combination with an inhibitor of the chymotrypsin-like activity of the proteasome (PSI) on apoptosis, cell cycle and proteasome activity in U937 cells. Folia Histochem. Cytobiol 39 (2001) 131-132
    • (2001) Folia Histochem. Cytobiol , vol.39 , pp. 131-132
    • Bury, M.1    Mlynarczuk, I.2    Pleban, E.3    Hoser, G.4    Kawiak, J.5    Wojcik, C.6
  • 21
    • 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 1 (1994) 479-489
    • (1994) Immunity , vol.1 , pp. 479-489
    • Villanueva, M.S.1    Fischer, P.2    Feen, K.3    Pamer, E.G.4
  • 22
    • 38049034323 scopus 로고    scopus 로고
    • A deterministic model for the processing and presentation of bacteria-derived antigenic peptides
    • Janda J., and Geginat G. A deterministic model for the processing and presentation of bacteria-derived antigenic peptides. J. Theor. Biol. 250 (2008) 532-546
    • (2008) J. Theor. Biol. , vol.250 , pp. 532-546
    • Janda, J.1    Geginat, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.