Rock K L, Gamble S, Rothstein L, Benacerraf B
Division of Lymphocyte Biology, Dana-Farber Cancer Institute, Boston, MA 02115.
Proc Natl Acad Sci U S A. 1991 Jan 1;88(1):301-4. doi: 10.1073/pnas.88.1.301.
A synthetic peptide corresponding to residues 365-380 of the influenza nucleoprotein (NP365-380) has been previously shown to associate with class I major histocompatibility complex-encoded molecules and to stimulate cytotoxic T lymphocytes [Townsend, A. R. M., Rothbard, J., Gotch, F. M., Bahadur, G., Wraith, D. & McMichael, A. J. (1986) Cell 44, 959-968]. We find that intact Db class I heterodimers on the cell surface are unreceptive to binding this antigen. However, NP365-380 readily associates with Db molecules on the plasma membrane in the presence of exogenous beta 2-microglobulin. In addition, there is a second pathway through which this peptide associates with class I molecules that requires energy and de novo protein synthesis. These findings have implications for maintaining the immunological identity of cells and for the use of peptides as vaccines for priming cytolytic T-cell immunity.
先前已表明，一种与流感核蛋白365 - 380位残基相对应的合成肽（NP365 - 380）可与I类主要组织相容性复合体编码分子结合，并刺激细胞毒性T淋巴细胞[汤森德，A.R.M.，罗斯巴德，J.，戈奇，F.M.，巴哈杜尔，G.，雷思，D. & 麦克迈克尔，A.J.（1986年）《细胞》44卷，959 - 968页]。我们发现，细胞表面完整的Db I类异二聚体对结合这种抗原不敏感。然而，在存在外源性β2 - 微球蛋白的情况下，NP365 - 380很容易与质膜上的Db分子结合。此外，该肽与I类分子结合还有第二条途径，这需要能量和从头蛋白质合成。这些发现对于维持细胞的免疫特性以及将肽用作引发溶细胞性T细胞免疫的疫苗具有重要意义。
