Anderson M S, Swier K, Arneson L, Miller J
Department of Molecular Genetics and Cell Biology, University of Chicago, Illinois 60637.
J Exp Med. 1993 Dec 1;178(6):1959-69. doi: 10.1084/jem.178.6.1959.
The cytosolic tail of the major histocompatibility complex class II-associated invariant chain (Ii) molecule is thought to contain the endosomal localization signal that directs and/or retains newly synthesized class II within the endosomal antigen processing compartment. To determine the role of this signal in class II transport and antigen presentation we have generated class II-positive L cell transfectants that coexpress wild type or truncated forms of Ii. Deletion of the endosomal localization signal from Ii results in rapid transport of class II-Ii complexes to the cell surface. Once at the cell surface, the complex is efficiently internalized, Ii is degraded, and class II free of Ii is recycled back to the plasma membrane. Interestingly, the truncated form of Ii is still able to increase the efficiency of antigen presentation to T cells. These data suggest that the ability of Ii to enhance antigen presentation is not limited to Golgi apparatus-endosomal sorting and raise the possibility that endocytosed class II can form immunogenic complexes with newly processed antigen.
主要组织相容性复合体II类相关恒定链(Ii)分子的胞质尾部被认为含有内体定位信号,该信号在内体抗原加工区室中指导和/或保留新合成的II类分子。为了确定该信号在II类转运和抗原呈递中的作用,我们构建了共表达野生型或截短形式Ii的II类阳性L细胞转染体。从Ii中删除内体定位信号会导致II-Ii复合物快速转运到细胞表面。一旦到达细胞表面,该复合物就会被有效地内化,Ii被降解,不含Ii的II类分子循环回到质膜。有趣的是,截短形式的Ii仍然能够提高向T细胞呈递抗原的效率。这些数据表明,Ii增强抗原呈递的能力不限于高尔基体-内体分选,并增加了内吞的II类分子可以与新加工的抗原形成免疫原性复合物的可能性。