Andersen M H, Bonfill J E, Neisig A, Arsequell G, Sondergaard I, Valencia G, Neefjes J, Zeuthen J, Elliott T, Haurum J S
Institute of Cancer Biology, Danish Cancer Society, Copenhagen.
J Immunol. 1999 Oct 1;163(7):3812-8.
CTL recognize short peptide fragments presented by class I MHC molecules. In this study, we examined the effect of phosphorylation on TAP transport, binding to class I MHC molecules, and recognition by CTL of peptide fragments from known phosphorylated oncogene proteins or virus phosphoproteins. We show that phosphopeptides can be efficiently transported from the cytosol to the endoplasmic reticulum by the TAP. Furthermore, we show that phosphorylation can have a neutral, negative, or even a positive effect on peptide binding to class I MHC. Finally, we have generated phosphopeptide-specific CTL that discriminate between the phosphorylated and the nonphosphorylated versions of the peptide. We conclude that phosphopeptide-specific CTL responses are likely to constitute a subset of the class I MHC-restricted CTL repertoire in vivo.
细胞毒性T淋巴细胞（CTL）识别由I类主要组织相容性复合体（MHC）分子呈递的短肽片段。在本研究中，我们检测了磷酸化对抗原加工相关转运体（TAP）转运、与I类MHC分子结合以及CTL对来自已知磷酸化癌基因蛋白或病毒磷蛋白的肽片段识别的影响。我们发现磷酸化肽段可被TAP有效地从胞质溶胶转运至内质网。此外，我们表明磷酸化对肽段与I类MHC的结合可能具有中性、负面甚至正面影响。最后，我们产生了能区分磷酸化和非磷酸化肽段的磷酸化肽段特异性CTL。我们得出结论，磷酸化肽段特异性CTL反应很可能构成体内I类MHC限制性CTL库的一个子集。
