Reassociation with beta 2-microglobulin is necessary for Db class I major histocompatibility complex binding of an exogenous influenza peptide.
Reassociation with beta 2-microglobulin is necessary for Db class I major histocompatibility complex binding of an exogenous influenza peptide.
复制标题
与 β2-微球蛋白的重新结合对于外源流感肽的 Db I 类主要组织相容性复合物结合是必要的。
DOI：
10.1073/pnas.88.1.301
复制
发表时间：
1991
影响因子：
11.1
通讯作者：
Benacerraf,B
中科院分区：
文献类型：
--
作者：
Rock,KL;Gamble,S;Rothstein,L;Benacerraf,B
先前已显示对应于流感核蛋白（NP 365 -380）的残基365-380的合成肽与I类主要组织相容性复合物编码的分子缔合并刺激细胞毒性T淋巴细胞[汤森，A. R. M.，Rothbard，J.，Gotch，F. M.，Bahadur，G.，Wraith，D. & McMichael，A. J.（1986）Cell 44，959-968]。我们发现，在细胞表面上的完整的Db I类异二聚体是不接受结合这种抗原。然而，在外源性β 2-微球蛋白存在下，NP 365 -380容易与质膜上的Db分子缔合。此外，还存在第二种途径，通过该途径该肽与需要能量和从头蛋白质合成的I类分子缔合。这些发现对于维持细胞的免疫特性和使用肽作为引发溶细胞T细胞免疫的疫苗具有意义。
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.