A Mutant Cell in Which Association of Class I Heavy and Light Chains Is Induced by Viral Peptides
This extract was created in the absence of an abstract.
Excerpt
The majority of cytotoxic T lymphocytes (CTLs) recognize epitopes of viral proteins in association of class I molecules of the major histocompatibility complex (MHC) (Zinkemagel and Doherty 1979). Epitopes can be generated from protein antigens synthesized in the cytoplasm and are presented at the cell surface in a form that can be replaced in vitro with short synthetic peptides (for review, see Townsend and Bodmer 1989). These results imply that distinct mechanisms may control degradation of antigen, transport of peptides across a membrane, and association of peptides with the binding site of a class I molecule.
We have identified a mutant cell, RMA-S (see Ljunggren and Kärre 1985), that is not able to present an epitope of influenza nucleoprotein (NP) synthesized in the cytoplasm but can present the same epitope when exposed to it as a peptide in the extracellular fluid. This phenotype is consistent with a mutation disrupting transport...
