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

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

Research output: Contribution to journalArticle

182 Scopus citations

Abstract

MHC class I molecules expressed in a calreticulin-deficient cell line (K42) assembled with β 2-microglobulin (β2-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.

Original languageEnglish (US)
Pages (from-to)99-109
Number of pages11
JournalImmunity
Volume16
Issue number1
DOIs
StatePublished - Jan 1 2002

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Infectious Diseases

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    Gao, B., Adhikari, R., Howarth, M., Nakamura, K., Gold, M. C., Hill, A. B., Knee, R., Michalak, M., & Elliott, T. (2002). Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin. Immunity, 16(1), 99-109. https://doi.org/10.1016/S1074-7613(01)00260-6