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Peptide loading in the endoplasmic reticulum accelerates trafficking of peptide: MHC class II complexes in B cells

  • Original Paper
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Journal of Biomedical Science

Abstract

In a combination of biochemical and immunoelectron-microscopical approaches we studied intracellular trafficking and localization of the endoplasmic-reticulum (ER)-formed complexes of murine MHC class II molecule I-Ab and an antigenic peptide Eα52–68 covalently linked to its β-chain. The association with the peptide in the ER leads to sharp acceleration of the intracellular trafficking of the complexes to the plasma membrane. Within the cells, Eα52–68:I-Ab complexes accumulate in the multivesicular MHC class II compartment (MIIC), but not in denser multilaminar or intermediate type MIICs. The changes in the trafficking of ER-formed complexes result solely from the presence of the tethered peptide, since wild-type class II molecules traffic similarly in bare lymphocyte syndrome cells and in wild-type antigen-presenting cells.

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Morkowski, S., Raposo, G., Geuze, H.J. et al. Peptide loading in the endoplasmic reticulum accelerates trafficking of peptide: MHC class II complexes in B cells. J Biomed Sci 6, 53–63 (1999). https://doi.org/10.1007/BF02256424

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  • DOI: https://doi.org/10.1007/BF02256424

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