MHC class I presentation of an exogenous polypeptide antigen encoded by the murine AIDS defective virus

Microbiology and Immunology

Volumn 41, Issue 7, 1997, Pages 563-570

  Yee, Sung Tae ^a,g   Okada, Yoshiaki ^a   Ogasawara, Kazumasa ^b   Omura, Satoshi ^c   Takatsuki, Akira ^d   Kakiuchi, Terutaka ^e   Muno, Daisaku ^f   Kominami, Eiki ^f   Mizuochi, Toshiaki ^a  

^a NATIONAL INSTITUTE OF INFECTIOUS DISEASES   (Japan)

^b HOKKAIDO UNIVERSITY   (Japan)

^c KITASATO INSTITUTE   (Japan)

^d INST OF PHYS AND CHEMICAL RESEARCH   (Japan)

^e TOHO UNIVERSITY   (Japan)

^f JUNTENDO UNIVERSITY   (Japan)

^g Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

Author keywords

Ag processing presentation; MHC class I; Murine AIDS

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2;

ACQUIRED IMMUNE DEFICIENCY SYNDROME; ANIMAL CELL; ANTIGEN PRESENTATION; ARTICLE; CONTROLLED STUDY; FEMALE; LYMPHOCYTE PROLIFERATION; MAJOR HISTOCOMPATIBILITY COMPLEX; MOUSE; NONHUMAN; RETROVIRUS; RODENT DISEASE; T LYMPHOCYTE;

ANIMALIA; MURINAE; RODENTIA; UNIDENTIFIED RETROVIRUS;

EID: 0030752345     PISSN: 03855600     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1348-0421.1997.tb01892.x     Document Type: Article

References (24)

1. Diment, S. 1990. Different roles for thiol and aspartyl proteases in antigen presentation of ovalbumin. J. Immunol. 145: 417-422.
2. Fenteany, G., Standaert, R.F., Lane, W.S., Choi, S., Corey, E.J., and Schreiber, S.L. 1995. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268: 726-731.
3. Harding, C.V. 1995. Phagocytic processing of antigens for presentation by MHC molecules. Trends Cell Biol. 5: 105-109.
4. Jondal, M., Schirmbeck, R., and Reimann, J. 1996. MHC class I-restricted CTL responses to exogenous antigens. Immunity 5: 295-302.
5. Kominami, E., Ueno, T., Muno, D., and Katunuma, N. 1991. The selective role of cathepsin B and D in the lysosomal degradation of endogenous and exogenous proteins. FEBS Lett. 287: 189-192.
6. Maric, M.A., Taylor, M.D., and Blum, J.S. 1994. Endosomal aspartic proteinases are required for invariant chain processing. Proc. Natl. Acad. Sci. U.S.A. 91: 2171-2175.
7. Matsunaga, Y., Shibata, T., Kido, H., and Katunuma, N. 1993. Participation of cathepsin B in processing of antigen presentation to MHC class II. FEBS Lett. 324: 325-330.
8. + T cells initiate cytotoxic T lymphocyte responses against allogenic major histocompatibility antigens but not against trinitrophenyl-modified cells. J. Exp. Med. 162: 427-443.
9. Mizuochi, T., Yee, S.-T., Kasai, M., Kakiuchi, T., Muno, D., and Kominami, E. 1994. Both cathepsin B and cathepsin D are necessary for processing of ovalbumin as well as for degradation of class II MHC invariant chain. Immunol. Lett. 43: 189-193.
10. Murata, M., Miyashita, S., Yokoo, C., Tamai, M., Hanada, K., Hatayama, K., Towatari, T., Nikawa, T., and Katunuma, N. 1991. Novel epoxysuccinyl peptides. Selective inhibitors of cathepsin B in vitro. FEBS Lett. 280: 307-310.
11. Ogasawara, K., Maloy, W.L., Beverly, B., and Schwartz, R.H. 1989. Functional analysis of the antigenic structure of a minor T cell determinant from pigeon cytochrome C. Evidence against an alpha-helical conformation. J. Immunol. 142: 1448-1456.
12. Omura, S., Fujimoto, T., Otoguro, K., Matsuzaki, K., Moriguchi, R., Tanaka, H., and Sasaki, Y. 1991. Lactacystin, a novel microbial metabolite, induces neutrogenesis of neuroblastoma cells. J. Antibiot. 44: 113-116.
13. Puri, J., and Factorovich, Y. 1988. Selective inhibition of antigen presentation to cloned T cells by protease inhibitors. J. Immunol. 141: 3313-3317.
14. Rammensee, H.G., Falk, K., and Rotzschke, O. 1993. Peptides naturally presented by MHC class I molecules. Annu. Rev. Immunol. 11: 213-244.
15. Reyes, V.E., Lu, S., and Humphreys, R.E. 1991. Cathepsin B cleavage of Ii from class II MHC a- and b-chains. J. Immunol. 146: 3877-3880.
16. Rock, K.L. 1996. A new foreign policy: MHC class I molecules monitor the outside world. Immunol. Today 17: 131-137.
17. Rodriguez, G.M., and Diment, D. 1992. Role of cathepsin D in antigen presentation of ovalbumin. J. Immunol. 149: 2894-2898.
18. Stripe, F., Olsnes, S., and Pihl, A. 1980. Gelonin, a new inhibitor of protein synthesis, nontoxic to intact cells. J. Biol. Chem. 255: 6947-6953.
19. Takahashi, H., Cease, K.G., and Berzofsky, J.A. 1989. Identification of proteases that process distinct epitopes on the same protein. J. Immunol. 142: 2221-2229.
20. Takatsuki, A., and Tamura, G. 1985. Brefeldin A, a specific inhibitor of intracellular translocation of vesicular stomatitis virus G protein: intracellular accumulation of high-man-nose type G protein and inhibition of its cell surface expression. Agric. Biol. Chem. 49: 899-902.
21. Towatari, T., Kawabata, Y, and Katunuma, N. 1979. Crystallization and properties of cathepsin B from rat liver. Eur. J. Biochem. 102: 279-289.
22. Townsend, A., Ohlen, C., Bastin, J., Ljunggren, H.G., Foster, L., and Karre, K. 1989. Association of class I major histocompatibility heavy and light chains induced by viral peptides. Nature 340: 443-448.
23. Ward, C.L., Omura, S., and Kopito, R.R. 1995. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83: 121-127.
24. + T cells. Immunol. Lett. 55: 93-98