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J. Biol. Chem., Vol. 276, Issue 27, 24525-24530, July 6, 2001

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-Amino Acid Scan of a Class I Major Histocompatibility Complex-restricted Alloreactive T-cell Epitope^*

Stefan Reinelt, Merce Marti^§, Séverine Dédier, Thomas Reitinger^¶, Gerd Folkers, José A. López de Castro^§, and Didier Rognan^**

From the  Department of Applied Biosciences, Swiss Federal Institute of Technology, Wintherthurerstrasse 190, CH-8057 Zürich, Switzerland, ^§ Centro de Biologia Molecular "Severo Ochoa", Universidad Autonoma de Madrid, Facultad de Ciencias, Cantoblanco, E-28049 Madrid, Spain, and  Laboratoire de Pharmacochimie de la Communication Cellulaire, Unité Mixte de Recherches CNRS 7081, 74 route du Rhin, B.P.24, F-67401 Illkirch, France

An HLA-B27-restricted self-octapeptide known to react with an alloreactive T-cell receptor has been modified by systematic substitution of a -amino acid for the natural -amino acid residue, over the whole length of the parent epitope. All modified peptides were shown to bind to recombinant HLA-B*2705 and induce stable major histocompatibility complex-peptide complexes, but with some variation depending on the position of the -amino acid on the peptide sequence. Alteration of the natural peptide sequence at the two N-terminal positions (positions 1 and 2) decreases binding affinity and thermodynamic stability of the refolded complex, but all other positions (from position 3 to the C-terminal residue) were insensitive to the -amino acid substitution. All modified peptides were recognized by an alloreactive T-cell clone specific for the parent epitope with decreased efficiency, to an extent dependent of the position that was modified. Furthermore, the introduction of a single -amino acid at the first two positions of the modified peptide was shown to be sufficient to protect them against enzymatic cleavage. Thus, -amino acids represent new interesting templates for alteration of T-cell epitopes to design either synthetic vaccines of T-cell receptor antagonists.

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