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MHC class I molecules expressed in a calreticulin-deficient cell line (K42) assembled with beta 2-microglobulin (beta2-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.


Journal article



Publication Date





99 - 109


Animals, Antigen Presentation, Antiporters, Biological Transport, Calcium-Binding Proteins, Calreticulin, Cells, Cultured, Endoplasmic Reticulum, Heat-Shock Proteins, Histocompatibility Antigens Class I, Immunoglobulins, Isomerases, Membrane Transport Proteins, Mice, Protein Disulfide-Isomerases, Ribonucleoproteins