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Abstract
Chimeric histocompatibility genes encoding the amino-terminal (beta 1) domain of the
class II Ak beta polypeptide and the carboxy-terminal (C2, transmembrane, and intracytoplasmic)
domains of either the class I H-2Ld or H-2Dd molecules were stably introduced into
mouse L cells. Although both were transcribed, only 5' Ak beta/3' H-2Dd transformants
had significant cell membrane expression of a 30-40 kd, heterogeneous glycoprotein
containing Ak beta 1 and H-2Dd (C2) serological epitopes. These transformants had
a unique pattern of reactivity with monoclonal antibodies previously identified as
requiring the Ak beta 1 domain for recognition of complete I-A molecules. These results
allow new insight into the structural requirements for cell surface expression of
proteins and provide unique cellular reagents for the dissection of humoral and cell-mediated
recognition of MHC molecules.