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Recognition of open conformers of classical MHC by chaperones and monoclonal antibodies
Author(s) -
Hansen Ted H.,
Lybarger Lonnie,
Yu Lawrence,
Mitaksov Vesselin,
Fremont Daved H.
Publication year - 2005
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.0105-2896.2005.00315.x
Subject(s) - major histocompatibility complex , monoclonal antibody , mhc class i , biology , mhc restriction , peptide , epitope , antigen , microbiology and biotechnology , antibody , immunology , biochemistry
Summary: There is considerable evidence that the conformation and stability of class I and class II major histocompatibility complex (MHC) proteins is dependent upon high‐affinity peptide ligation, but structural data for an empty MHC protein unfortunately is lacking. However, several monoclonal antibodies (mAbs) that specifically detect open MHC conformers have been characterized, and they provide insights into the changes associated with peptide loading and unloading. Here, the structural changes make the argument that certain of these open conformer‐specific mAbs recognize analogous MHC segments as the molecular chaperones tapasin and DM. MHC residues located in regions flanking the peptide‐terminal anchoring pockets have been implicated in both chaperone and monoclonal antibody binding. Indeed, we propose these regions serve as peptide‐binding hinges that are uniquely accessible in open MHC.