Gao, Bin, Adhikari, Raju, Howarth, Mark, Nakamura, Kimitoshi, Gold, Marielle C., Hill, Ann B., Knee, Rai, Michalak, Marek and Elliott, Tim
Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin
Immunity, 16, (1), . (doi:10.1016/S1074-7613(01)00260-6).
Full text not available from this repository.
MHC class I molecules expressed in a calreticulin-deficient cell line (K42) assembled with ? 2-microglobulin (?2-m) normally, but their subsequent loading with optimal peptides was defective. Suboptimally loaded class I molecules were released into the secretory pathway. This occurred despite the ability of newly synthesized class I to interact with the transporter associated with antigen processing (TAP) loading complex. The efficiency of peptide loading was reduced by 50%–80%, and impaired T cell recognition was observed for three out of four antigens tested. The peptide-loading function was specific to calreticulin, since the defect in K42 could be rectified by transfection with calreticulin but not a soluble form of calnexin, which shares its lectin-like activity.
Actions (login required)