An HLA-A2-restricted T-cell epitope mapped to the BNLF2a immune evasion protein of Epstein-Barr virus that inhibits TAP.
The early lytic cycle protein of Epstein-Barr virus (EBV), BNLF2a, has recently been shown to play a critical role in immune evasion by inhibiting the peptide transporter associated with antigen processing (TAP), thereby blocking antigen-specific CD8(+) T-cell recognition of many lytic cycle antigens. Surprisingly, we now show that a peptide ((50)VLFGLLCLL(58)) from the hydrophobic C-terminal region of this small (60-amino-acid) EBV protein is efficiently presented by the common class I allele HLA-A2 for recognition by cytotoxic T lymphocytes. The mechanism for this unexpected finding was revealed by experiments showing that this epitope is processed and presented independently of TAP.
Bell
Melissa J
MJ
Queensland Institute of Medical Research, 300 Herston Rd., Brisbane 4029, Australia.
Abbott
Rachel J M
RJ
Croft
Nathan P
NP
Hislop
Andrew D
AD
Burrows
Scott R
SR
D017951:Antigen Presentation; D018984:Epitopes, T-Lymphocyte / Q000276:immunology*; D015789:HLA-A2 Antigen / Q000276:immunology; D004854:Herpesvirus 4, Human / Q000276:immunology*; D017434:Protein Structure, Tertiary; D013602:T-Lymphocytes, Cytotoxic / Q000276:immunology; D014763:Viral Matrix Proteins / Q000276:immunology*
C539239:BNLF21 protein, human herpesvirus 4; D018984:Epitopes, T-Lymphocyte; D015789:HLA-A2 Antigen; D014763:Viral Matrix Proteins