Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

We have identified two epitopes for Epstein-Barr virus specific cytotoxic T lymphocytes (CTL) restricted by the common allele HLA-B7. They are EBNA 3C 881-9 (QPRAPIRPI) and EBNA 3A 379-387 (RPPIFIRRL). The epitopes conform well to the recently described motif for HLA-B7-binding peptides (Huckzo et al., J. Immunol. 1993. 151:2572). Titration of the peptides in CTL assays and detergent lysate binding assays revealed that extending the peptides at either the N or C terminus did not reduce their affinity for HLA-B7. This behavior contrasted with HLA-B51, which binds peptides with a similar motif to B7, and has identical amino acid residues at sites expected to form the "F" pocket of the peptide-binding groove. HLA-B51 also bound the peptide EBNA 3C 881-9, but was unable to bind peptides extended at the C terminus.

Original publication

DOI

10.1002/eji.1830250105

Type

Journal article

Journal

Eur J Immunol

Publication Date

01/1995

Volume

25

Pages

18 - 24

Keywords

Amino Acid Sequence, Antigens, Viral, Cell Line, Clone Cells, Cytotoxicity Tests, Immunologic, DNA-Binding Proteins, Epitopes, Epstein-Barr Virus Nuclear Antigens, HLA-B7 Antigen, Herpesvirus 4, Human, Humans, Molecular Sequence Data, Peptide Fragments, Protein Binding, T-Lymphocytes, Cytotoxic, Transfection