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J Biol Chem, Vol. 274, Issue 9, 5550-5556, February 26, 1999

Protection against Lymphocytic Choriomeningitis Virus Infection Induced by a Reduced Peptide Bond Analogue of the H-2D^b-restricted CD8⁺ T Cell Epitope GP33

From the Institute for Medical Microbiology and Hygiene, Department of Immunology, University of Freiburg, 79104 Freiburg, Germany and the ^§ Institut de Biologie Moléculaire et Cellulaire, UPR 9021 CNRS, 67000 Strasbourg, France

Recent investigations have suggested that pseudopeptides containing modified peptide bonds might advantageously replace natural peptides in therapeutic strategies. We have generated eight reduced peptide bond (CH₂-NH) analogues corresponding to the H-2D^b-restricted CD8⁺ T cell epitope (called GP33) of the glycoprotein of the lymphocytic choriomeningitis virus. One of these pseudopeptides, containing a reduced peptide bond between residues 6 and 7 ((6-7)), displayed very similar properties of binding to major histocompatibility complex (MHC) and recognition by T cell receptor transgenic T cells specific for GP33 when compared with the parent peptide. We assessed in vitro and in vivo the proteolytic resistance of GP33 and (6-7) and analyzed its contribution to the priming properties of these peptides. The (6-7) analogue exhibited a dramatically increased proteolytic resistance when compared with GP33, and we show for the first time that MHC-peptide complexes formed in vivo with a pseudopeptide display a sustained half-life compared with the complexes formed with the natural peptide. Furthermore, in contrast to immunizations with GP33, three injections of (6-7) in saline induced significant antiviral protection in mice. The enhanced ability of (6-7) to induce antiviral protection may result from the higher stability of the analogue and/or of the MHC-analogue complexes.

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