CTL epitope generation is tightly linked to cellular proteolysis of a Listeria monocytogenes antigen

Journal of Immunology

Volumn 156, Issue 4, 1996, Pages 1497-1503

  Sijts, Alice J A M ^a   Villanueva, Merceditas S ^a   Pamer, Eric G ^a  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ANTIGEN; EPITOPE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PROTEASOME; PROTEINASE INHIBITOR;

ANIMAL CELL; ANTIGEN PRESENTATION; ANTIGEN RECOGNITION; ARTICLE; CONTROLLED STUDY; CYTOTOXIC T LYMPHOCYTE; LISTERIA MONOCYTOGENES; MAJOR HISTOCOMPATIBILITY COMPLEX; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEINASE INHIBITION;

AMINO ACID SEQUENCE; ANIMALS; ANTIGENS, BACTERIAL; BACTERIAL PROTEINS; CELLS, CULTURED; EPITOPES; H-2 ANTIGENS; LISTERIA MONOCYTOGENES; MICE; MICE, INBRED BALB C; MICE, INBRED C57BL; MOLECULAR SEQUENCE DATA; T-LYMPHOCYTES, CYTOTOXIC;

EID: 0030040594     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (35)

1. Townsend, A , and H. Bodmer. 1989. Antigen recognition by class I-restricted T lymphocytes. Annu Rev. Immunol. 7:601.
2. Rammensee, H -G., K. Falk, and O Rotzske. 1993. Peptides naturally presented by MHC class I molecules. Annu. Rev. Immunol. 11:213.
3. Cresswell, P., M. Androlewicz, L Denzin, B. Ortmann, and B. Sadasivan 1994 Assembly and transport of class I MHC glycoproteins. In Antigen Processing and Presentation. R. Humphreys and S. Pierce, eds. Academic Press Inc., San Diego, CA, p. 33.
4. Schumacher, T. N. M., D. V. Kantesaria, M.-T. Heemels, P G Ashton-Rickardt, J. C Shepherd, K. Fruh, Y. Yang, P. A. Peterson, S. Tonegawa, and H L Ploegh 1994 Peptide length and sequence specificity of the mouse TAP1/TAP2 translocator. J. Exp. Med. 179:533
5. Goldberg, A. L , and K L. Rock. 1992. Proteolysis, proteasomes and antigen presentation. Nature 357:375.
6. Kechsteiner, M., L. Hoffman, and W. Daniel. 1993. The multicatalytic and 26S proteases. J. Biol Chem 268:6065.
7. Ciechanover, A 1994. The ubiquitin-proteasome proteolytic pathway. Cell 79: 13.
8. Orlowski, M., C. Cardozo, and C. Michaud. 1993. Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex: properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acids Biochemistry 32:1503.
9. Driscoll, J., M. G. Brown, D. Finley, and J. J. Monaco. 1993. MHC- linked LMP gene products specifically alter peptidase activities of the proteasome Nature 365:262.
10. Gaczynska, M., K. L. Rock, and A. L. Goldberg 1993 γ-Interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes Nature 365:264
11. Boes, B , H. Hengel, T. Ruppert, G. Multhaup, U. H. Koszinowski, and P -M. Kloetzel. 1994. Interferon-γ stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes. J Exp Med. 179:901
12. Ustrell, V., G. Pratt, and M. Rechsteiner. 1995 Effects of interferon γ and major histocompatibility complex-encoded subunits on peptidase activities of human multicatalytic proteases. Proc. Natl. Acad. Sci. USA 92:584.
13. Fehling, H. J , W. Swat, C. Laplace, R. Kuhn, K. Rajewski, U. Müller, and H. von Boehmer. 1994. MHC class I expression in mice lacking the proteasome subunit LMP-7. Science 265:1234.
14. Van Kaer, L., P. G. Ashton-Rickardt, M. Eichelberger, M. Gaczynska, K Nagashima, K. L. Rock, A L. Goldberg, P. C. Doherty, and S. Tonegawa. 1994. Altered peptidase and viral-specific T cell response in LMP2 mutant mice Immunity 1:533
15. Dick, L R., C. Aldrich, S. C Jameson, C. R. Moornaw, B. C Pramanik, C. K. Doyle, G. N. DeMartino, M. J Bevan, J. M. Forman, and C. A. Slaughter 1994. Proteolytic processing of ovalbumin and β-galactosidase by the proteasome to yield antigenic peptides. J. Immunol. 152:3884
16. Rock, K. L., C. Gramm, L. Rothstein, K. Clark, R. Stein, L. Dick, D. Hwang, and A. L Goldberg 1994. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78:761.
17. Pamer, E. G. 1993. Cellular immunity to intracellular bacteria. Curr. Opin. Immunol. 5:492.
18. Portnoy, D. A., and S. Jones. 1994. The cell biology of Listeria monocytogenes infection (escape from a vacuole). Ann NY Acad. Sci. 73:15.
19. Pamer, E. G. 1994. Direct sequence identification and kinetic analysis of an MHC class I-restricted Listeria monocytogenes CTL epitope. J. Immunol. 152:686.
20. Sijts, A. J. A. M., A. Neissig, J. Neefjes, and E G. Pamer. 1995 Two Listeria monocytogenes CTL epitopes are processed from the same antigen with different efficiencies. J. Immunol 156:685.
21. Villanueva, M. S., P. Fischer, K. Feen, and E. G. Pamer. 1994. Efficiency of MHC class 1 antigen processing: a quantitative analysis. Immunity 1:479.
22. Villanueva, M. S., C J. M. Beckers, and E. G. Pamer. 1994. Infection with Listeria manocytogenes impairs sialic acid addition to host cell glycoproteins. J Exp Med. 180:2137
23. Smith, M H., and B. H. Barber 1990. The conformational flexibility of class I H-2 molecules as revealed by anti-peptide antibodies specific for intracytoplasmic determinants: differential reactivity of beta-2 microglobulin "bound" and "free" heavy chains. Mol. Immunol. 27:169.
24. Vinitsky, A , C. Michaud, J. C. Powers, and M Orlowski. 1992. Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex. Biochemistry 31:9421.
25. Krangel, M. S , H. T. Orr, and J. L. Strominger. 1979. Assembly and maturation of HLA-A and HLA-B antigens in vivo. Cell 18:979.
26. Kohler, S., M. Leimeister-Wachter, T. Chakraborty, F. Lottspeich, and W. Goebel, 1990. The gene coding for protein p60 of Listeria monocytogenes and its use as a specific probe for Listeria monocytogenes. Infect. Immun. 58:1943.
27. Niedermann. G., S. Butz, H G. Ihlenfeldt, R Grimm, M. Lucchiari, H. Hoschutzky, G. Jung, B. Maier, and K. Eichmann. 1995 Contribution of proteasome-mediated proteolysis to the hierarchy of epitopes presented by major histocompatibility complex class I molecules. Immunity 2:289
28. Falk, K , O. Rotschke, and H.-G. Rammensee. 1990 Cellular peptide composition governed by major histocompatibility complex class I molecules. Nature 348:248.
29. Roelse, J., M. Grommé, F. Momburg, G. Hämmerling, and J Neefjes. 1994. Trimming of TAP-translocated peptides in the endoplasmic reticulum and in the cytosol during recycling. J. Exp. Med. 180:1591.
30. Snyder, H. L., J -W. Yewdell, and I. R. Bennink. 1994. Trimming of antigenic peptides in an early secretory compartment J. Exp. Med. 180:2389
31. Michalek, M T., E. P Grant, C. Gramm, A. L. Goldberg, and K. L Rock. 1993. A role for the ubiquitin-dependent proteolytic pathway in MHC class I-restricted antigen presentation. Nature 363:552.
32. Cox, J. H., P. Galardy, J. R. Bennink, and J. W Yewdell 1995. Presentation of endogenous and exogenous antigens is not affected by inactivation of El ubiquitin-activating enzyme in temperature sensitive cell lines. J. Immunol 154:511
33. Carbone, F. R., N. A. Hosken, M. W. Moore, and M. J Bevan. 1989. Class I MHC-restricted cytotoxic responses to soluble protein antigens. Cold Spring Harbor Symp. Quant. Biol. LIV:551
34. Murakami, Y., S. Matsufuji, T Kameji, S. Hayashi, K. Igarashi, T. Tamura, K. Tanaka, and A. Ichihara 1992. Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination. Nature 360:597
35. Vinitsky, A., C. Cardozo, L. Sepp-Lorenzino, C. Michaud, and M Orlowski. 1994. Inhibition of the proteolytic activity of the multicatalytic proteinase complex (proteasome) by substrate-related peptidyl aldehydes. J. Biochem. 269:29860.