Cell surface expression and function of an HLA class II molecule with class I domain configuration.
Recombinant major histocompatibility complex (MHC) class II molecules were expressed with extracellular polypeptide domains reorganized to form heavy (H) and light (L) chains (alpha 1-beta 1-beta 2 and alpha 2) analogous to class I. Accurate protein folding and dimerization is demonstrated by the ability of this 3+1-DR1 construct to bind class II-restricted peptides and stimulate CD4+ T cells. Cell surface expression of a functional class II molecule consisting of H and L chains supports the validity of current class II models and affirms the evolutionary relatedness of class I/II. MHC functions that differ between class I/II may be influenced by domain configuration, and the use of domain-shifted constructs will allow examination of this possibility.
Olson
R R
RR
Veterans Affairs Medical Center, Iowa City, Iowa.
Reuter
J J
JJ
Scalf
K
K
D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA; D006684:HLA-DR Antigens / Q000096:biosynthesis* / Q000737:chemistry / Q000276:immunology; D015395:Histocompatibility Antigens Class I / Q000737:chemistry*; D006801:Humans; D007739:L Cells; D051379:Mice; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding
D006684:HLA-DR Antigens; D015395:Histocompatibility Antigens Class I; D004247:DNA