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MHC Class I
all nucleated cells, peptide load in the ER
MHC Class I Intracellular Pathogens
cleared when CD8 recognizes the structural domain of the alpha-subunit of MHC class I on an infected cell
MHC Class I Intracellular Proteins
in the ER, loaded with peptides that move to the plasma membrane and present peptide to CD8 T cells
MHC Class I Load in the ER Steps
formation of peptide-loading complex, digestion of proteins by proteasome, peptide transport into ER, peptide trimming, transport of plasma membrane
TAP
transporter associated with peptide processing
ERAP
endoplasmic reticulum aminopeptidase
MHC Class II
cannot bind peptides in the ER, professional APC; begin in the secretory pathway but are not loaded until they are part of a vesicle capable of fusing with a phagolysosome
MHC Class II Extracellular Pathogens
cleared by the activation of phagocytes and B cells, antibody production when the CD4 coreceptor recognized the structural domains on both subunits of MHC class II when peptide is presented
MHC Class II Extracellular Proteins
MHC molecules are loaded with peptides from these which then move to plasma membrane and present peptide to CD4 T cells, present peptides from these on surface of APCs; macrophages, dendritic cells, B cells
MHC Class II Loading in the Late Endosomes Steps
MHC II molecules are assembled in ER, peptide-binding groove is blocked with a peptide chain (invariant chain), phagocytosis and fusion with the MHC compartment, peptide loading via HLA DM regulates exchange of CLIP for phagolysosomal peptides
MHC Class II Loading in the Late Endosomes Steps Simple
MHC Class II binds invariant chain, production of CLIP, phagolysosome fusion with MHC class II vesicle, peptide loading