Construction, expression and recognition of an H-2 molecule lacking its carboxyl terminus.
A mouse major histocompatibility antigen (H-2) gene, encoding a novel H-2Ld molecule lacking its intracytoplasmic domain, has been constructed and introduced into mouse L-cells. The novel H-2 molecule is found on the surface of the transfected cells at the same level as L-cells transfected with the native H-2Ld gene. Allo- and influenza-specific cytotoxic T lymphocytes can recognize the truncated H-2 gene product nearly as efficiently as the normal H-2Ld gene product. However, vesicular stomatitis virus-specific cytotoxic T lymphocytes recognize the truncated H-2Ld molecule less efficiently than the complete H-2Ld product. The rate of capping of the truncated H-2Ld molecule was investigated and found to be the same as that of the complete H-2Ld gene product.
D000595:Amino Acid Sequence; D003593:Cytoplasm / Q000502:physiology; D003602:Cytotoxicity, Immunologic; D005796:Genes; D006183:H-2 Antigens / Q000235:genetics* / Q000276:immunology; D007152:Immunologic Capping; D008565:Membrane Proteins / Q000502:physiology; D011485:Protein Binding; D012326:RNA Splicing; D013601:T-Lymphocytes / Q000276:immunology*; D014158:Transcription, Genetic; D001613:beta 2-Microglobulin / Q000378:metabolism
D006183:H-2 Antigens; D008565:Membrane Proteins; D001613:beta 2-Microglobulin