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 Ealpha52-68 covalently linked to its beta-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, Ealpha52-68: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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Antibodies, Monoclonal
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Antigens, Differentiation, B-Lymphocyte / metabolism
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Antigens, Surface / genetics
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Antigens, Surface / metabolism*
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B-Lymphocytes / metabolism*
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Biological Transport
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Cell Compartmentation
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Cell Membrane / metabolism
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Endoplasmic Reticulum / metabolism*
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Histocompatibility Antigens Class II / chemistry
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Histocompatibility Antigens Class II / genetics
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Histocompatibility Antigens Class II / metabolism*
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Humans
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Kinetics
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Mice
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Mice, Inbred BALB C
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Microscopy, Immunoelectron
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Peptide Fragments*
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Peptides / metabolism*
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Receptors, Antigen, T-Cell*
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Severe Combined Immunodeficiency / metabolism
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Subcellular Fractions
Substances
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Antibodies, Monoclonal
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Antigens, Differentiation, B-Lymphocyte
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Antigens, Surface
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Histocompatibility Antigens Class II
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Peptide Fragments
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Peptides
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Receptors, Antigen, T-Cell
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Recombinant Proteins
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antigenic peptide Ealpha52-68
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invariant chain