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Advanced Immunology I (Feb. 6, 2004)
Yueh-hsiu Chien
The source of Antigenic Peptides Associated with Class I MHC
Molecules
(What is known then, what is new now)
N. Shastri, S. Schwab and T. Serwold, Producing nature's gene-chips: the
generation of peptides for display by MHC class I molecules. Annu. Rev.
Immunol. 20 (2002), pp. 463–493.
New vs. Old
1. U. Schubert, L.C. Anton, J. Gibbs, C.C. Norbury, J.W. Yewdell and J.R.
Bennink, Rapid degradation of a large fraction of newly synthesized
proteins by proteasomes. Nature 404 (2000), pp. 770–774.
2. E.A. Reits, J.C. Vos, M. Gromme and J. Neefjes, The major substrates for
TAP in vivo are derived from newly synthesized proteins. Nature 404
(2000), pp. 774–778.
3. E.A. Reits, A. Griekspoor, J. Neijssen, T. Groothuis, K. Jalink, P. van
Veelen, H. Janssen, J. Calafat, J.W. Drijfhout and J. Neefjes, Peptide
diffusion, protection and degradation in nuclear and cytoplasmic
compartments before antigen presentation by MHC class I. Immunity 18
(2003), pp. 97–108.
4. S. Khan, R. de Giuli, G. Schmidtke, M. Bruns, M. Buchmeier, M. van den
Broek and M. Groettrup, Cutting edge: neosynthesis is required for the
presentation of a T cell epitope from a long-lived viral protein. J. Immunol.
167 (2001), pp. 4801–4804.
5. J. Levitskaya, M. Coram, V. Levitsky, S. Imreh, P.M. Steigerwald-Mullen,
G. Klein, M.G. Kurilla and M.G. Masucci, Inhibition of antigen processing
by the internal repeat region of the Epstein-Barr virus nuclear antigen-1.
Nature 375 (1995), pp. 685–688.
6. Y. Yin, B. Manoury and R. Fahraeus, Self-inhibition of synthesis and
antigen presentation by Epstein-Barr virus-encoded EBNA1. Science 301
(2003), pp. 1371–1374.
7. M.F. Princiotta, D. Finzi, S.B. Qian, J. Gibbs, S. Schuchmann, F.
Buttgereit, J.R. Bennink and J.W. Yewdell, Quantitating protein synthesis,
degradation, and endogenous antigen processing. Immunity 18 (2003),
pp. 343–354. (A comprehensive study on the dynamics of protein turnover
and the efficiency of generating MHC class I assembled peptides)
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Coding vs. Noncoding
8 S.R. Schwab, K.C. Li, C. Kang and N. Shastri, Constitutive display of
cryptic translation products by MHC class I molecules. Science 301
(2003), pp. 1367–1371.
Inside vs. Outside
9. J. Garin, R. Diez, S. Kieffer, J.F. Dermine, S. Duclos, E. Gagnon, R.
Sadoul, C. Rondeau and M. Desjardins, The phagosome proteome:
insight into phagosome functions. J. Cell Biol. 152 (2001), pp. 165–180.
10. E. Gagnon, S. Duclos, C. Rondeau, E. Chevet, P.H. Cameron, O.
Steele-Mortimer, J. Paiement, J.J. Bergeron and M. Desjardins,
Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry
into macrophages. Cell 110 (2002), pp. 119–131.
11. B. Tsai, Y. Ye and T.A. Rapoport, Retro-translocation of proteins from
the endoplasmic reticulum into the cytosol. Nat. Rev. Mol. Cell. Biol. 3
(2002), pp. 246–255.
12.M. Houde, S. Bertholet, E. Gagnon, S. Brunet, G. Goyette, A. Laplante,
M.F. Princiotta, P. Thibault, D. Sacks and M. Desjardins, Phagosomes are
competent organelles for antigen cross-presentation. Nature 425 (2003),
pp. 402–406.
13. P. Guermonprez, L. Saveanu, M. Kleijmeer, J. Davoust, P. Van Endert
and S. Amigorena, ER-phagosome fusion defines an MHC class I crosspresentation compartment in dendritic cells. Nature 425 (2003), pp. 397–
402.
14. A.L. Ackerman, C. Kyritsis, R. Tampe and P. Cresswell, Early
phagosomes in dendritic cells form a cellular compartment sufficient for
cross presentation of exogenous antigens. Proc. Natl. Acad. Sci. USA 100
(2003), pp. 12889–12894.
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