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Peptide exchange in MHC molecules
Author(s) -
Jensen Peter E.,
Weber Dominique A.,
Thayer Wesley R,
Westerman Larry E.,
Dao Chinh T
Publication year - 1999
Publication title -
immunological reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.839
H-Index - 223
eISSN - 1600-065X
pISSN - 0105-2896
DOI - 10.1111/j.1600-065x.1999.tb01368.x
Subject(s) - antigen processing , antigen presentation , major histocompatibility complex , mhc restriction , mhc class i , biology , cd74 , antigen , microbiology and biotechnology , peptide , mhc class ii , chaperone (clinical) , transporter associated with antigen processing , cross presentation , endosome , biochemistry , immune system , immunology , t cell , medicine , pathology , intracellular
Summary: Major histocompatibihty complex (MHC)‐encoded glycoproteins bind peptide antigens through non‐covalent interactions to generate complexes that are displayed on tbe surface of antigen‐presenting cells (APC) for recognition by T ceils, Peptide‐binding site occupancy is necessary for stable assembly of newly synthesized MHC proteins and export from the endoplasmic reticulum (ER), The MHC class II antigen‐processing pathway provides a mechanism for presentation of peptides generated in the endosomal pathway of APC, The chaperone protein, invariant chain, includes a surrogate peptide that stahilizes newly synthesized class II molecules during transport to endosomal compartments. The invariant chain‐derived peptide must be replaced through a peptide exchange reaction that is promoted by acidic pH and the MHC‐encoded co‐factor HLA‐DM, Peptide exchange reactions are not required for presentation of antigens by MHC class I molecules because they bind antigens during initial assembly in the ER, However, exchange reactions may play an important role in editing the repertoire of peptides presented by both class II and class I molecules, thus influencing the specificity of immunity and tolerance.