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Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin

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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.

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Gao, Bin, Adhikari, Raju, Howarth, Mark, Nakamura, Kimitoshi, Gold, Marielle C., Hill, Ann B., Knee, Rai, Michalak, Marek and Elliott, Tim (2002) Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin Immunity, 16, (1), pp. 99-109. (doi:10.1016/S1074-7613(01)00260-6).

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Published date: January 2002


Local EPrints ID: 26319
ISSN: 1097-4180
PURE UUID: 3f5e7c58-d9f7-4999-816c-882dff447163
ORCID for Tim Elliott: ORCID iD

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Date deposited: 20 Apr 2006
Last modified: 17 Jul 2017 16:07

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Author: Bin Gao
Author: Raju Adhikari
Author: Mark Howarth
Author: Kimitoshi Nakamura
Author: Marielle C. Gold
Author: Ann B. Hill
Author: Rai Knee
Author: Marek Michalak
Author: Tim Elliott ORCID iD

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