Peptide loading in the endoplasmic reticulum accelerates trafficking of peptide: MHC class II complexes in B cells |
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| Authors: | Stanislaw Morkowski Graça Raposo Hans J Geuze Alexander Y Rudensky |
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| Institution: | (1) The Department of Immunology, University of Washington School of Medicine, Seattle, Wash., USA;(2) Department of Cell Biology and Institute of Biomembranes, University of Utrecht School of Medicine, Utrecht, The Netherlands;(3) Present address: Section de Recherche URM/44, rue d'Ulm, Institut Curie, 75005 Paris, France;(4) Howard Hughes Medical Institute, University of Washington, Box 357370, 98195 Seattle, WA, USA |
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| 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 E 52–68 covalently linked to its  -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, E52–68: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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| Keywords: | MHC class II Invariant chain Class II:peptide complexes Intracellular trafficking |
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