Design of dimeric peptides obtained from a subdominant Epstein-Barr virus LMP2-derived epitope

Mauro Marastoni, Martina Bazzaro, Riccardo Gavioli, Fabiola Micheletti, Serena Traniello, Roberto Tomatis

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

The latent membrane protein 2 (LMP2) is expressed in EBV-associated tumours. LMP2 is a target of HLA-A2 restricted EBV-specific CTL responses and consequently it may represent a good target for specific CTL-based immunotherapies. However, the efficacy of such therapy is limited by the poor immunogenicity of the protein that induces weak cytotoxic T lymphocyte (CTL) responses directed against the CLGGLLTMV (CLG) epitope. Indeed, the CLG peptide presents low affinity for HLA-A2 and does not produce stable complexes. Therefore we synthesized and tested CLG-dimeric analogues with the purpose of characterizing new compounds with the capacity to bind HLA-A2 molecules. By these studies we have identified a few peptides which, compared to the natural epitope, showed higher affinity for HLA-A2 molecules and superior capacity to form a complex. These dimeric peptides may have the potential to induce efficient CTL responses directed to the natural epitope. (C) 2000 Editions scientifiques et medicales Elsevier SAS.

Original languageEnglish (US)
Pages (from-to)593-598
Number of pages6
JournalEuropean Journal of Medicinal Chemistry
Volume35
Issue number6
DOIs
StatePublished - Jun 2000

Bibliographical note

Funding Information:
Financial support of this work by Ministero dell’Università e della Ricerca Scientifica e Tecnologica (Cofinanziamento Progetto Chimica dei Composti Organici di Interesse Biologico), Istituto Superiore di Sanità (Progetto AIDS) is gratefully acknowledged.

Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.

Keywords

  • Dimeric analogues
  • Epstein-Barr virus
  • Immunogenic peptides
  • Segment condensation
  • Solid phase synthesis

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