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J. Biol. Chem., Vol. 276, Issue 41, 38255-38260, October 12, 2001

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Pleiotropic Effects of Post-translational Modifications on the Fate of Viral Glycopeptides as Cytotoxic T Cell Epitopes^*

Denis Hudrisier^§¶, Joëlle Riond, Honoré Mazarguil, and Jean Edouard Gairin

From the  Institut de Pharmacologie et de Biologie Structurale, UMR5089 CNRS/Université Paul Sabatier, 205 route de Narbonne, 31400 Toulouse, France and the ^§ Institut National de la Santé et de la Recherche Médicale, U395, CHU Purpan, BP3028, 31024 Toulouse Cedex 03, France

The fate of viral glycopeptides as cytotoxic T lymphocyte (CTL) epitopes is unclear. We have dissected the mechanisms of antigen presentation and CTL recognition of the peptide GP392-400 (WLVTNGSYL) from the lymphocytic choriomeningitis virus (LCMV) and compared them with those of the previously reported GP92-101 antigen (CSANNSHHYI). Both GP392-400 and GP92-101 bear a glycosylation motif, are naturally N-glycosylated in the mature viral glycoproteins, bind to major histocompatibility complex H-2D^b molecules, and are immunogenic. However, post-translational modifications differentially affected GP92-101 and GP392-400. Upon N-glycosylation or de-N-glycosylation, a marked decrease in major histocompatibility complex binding was observed for GP392-400 but not for GP92-101. Further, under its N-glycosylated or de-N-glycosylated form, GP392-400 then lost its initial ability to generate a CTL response in mice, whereas GP92-101 was still immunogenic under the same conditions. The genetically encoded form of GP392-400, which on the basis of its immunogenicity could still be presented with H-2D^b during the course of LCMV infection, does not in fact appear at the surface of LCMV-infected cells. Our results show that post-translational modifications of viral glycopeptides can have pleiotropic effects on their presentation to and recognition by CTL that contribute to either creation of neo-epitopes or destruction of potential epitopes.

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