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Journal of Virology, March 2009, p. 2783-2788, Vol. 83, No. 6
0022-538X/09/$08.00+0 doi:10.1128/JVI.01724-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Rachel J. M. Abbott,2,
Nathan P. Croft,2
Andrew D. Hislop,2* and
Scott R. Burrows1*
Queensland Institute of Medical Research and Australian Centre for Vaccine Development, Brisbane, Australia,1 Institute for Cancer Studies, University of Birmingham, Birmingham, United Kingdom2
Received 13 August 2008/ Accepted 1 January 2009
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 (50VLFGLLCLL58) 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.
Published ahead of print on 7 January 2009.
M.J.B. and R.J.M.A. contributed equally to this work.
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