Bell Melissa J, Abbott Rachel J M, Croft Nathan P, Hislop Andrew D, Burrows Scott R
Queensland Institute of Medical Research, 300 Herston Rd., Brisbane 4029, Australia.
J Virol. 2009 Mar;83(6):2783-8. doi: 10.1128/JVI.01724-08. Epub 2009 Jan 7.
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.
爱泼斯坦-巴尔病毒（EBV）的早期裂解周期蛋白BNLF2a最近被证明在免疫逃逸中起关键作用，它通过抑制与抗原加工相关的肽转运体（TAP），从而阻断抗原特异性CD8(+) T细胞对许多裂解周期抗原的识别。令人惊讶的是，我们现在发现，这种小的（60个氨基酸）EBV蛋白疏水C末端区域的一个肽（(50)VLFGLLCLL(58)）能被常见的I类等位基因HLA-A2有效呈递，以供细胞毒性T淋巴细胞识别。通过实验揭示了这一意外发现的机制，表明该表位的加工和呈递不依赖于TAP。
