Ia-transfected L-cell fibroblasts present a lysozyme peptide but not the native protein to lysozyme-specific T cells
| Autor: | Nilabh Shastri, Bernard Malissen, Leroy Hood |
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| Rok vydání: | 1985 |
| Předmět: |
Macromolecular Substances
T-Lymphocytes Lymphocyte Cooperation Antigen-Presenting Cells Lymphocyte Activation Transfection Major histocompatibility complex L Cells (Cell Line) Major Histocompatibility Complex Mice chemistry.chemical_compound L Cells Antigen Animals Antigen-presenting cell Cells Cultured Multidisciplinary biology Histocompatibility Antigens Class II Molecular biology Peptide Fragments chemistry biology.protein Muramidase Lysozyme Neuraminidase Caltech Library Services Keyhole limpet hemocyanin Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 82:5885-5889 |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | We studied the antigen-presenting capacity of mouse L fibroblasts transfected with genes encoding Ia polypeptides of the major histocompatibility complex (MHC). These cells function as efficient antigen-presenting cells (APC) in stimulating peptide antigen-specific MHC-restricted proliferation of long-term T-cell lines, thus establishing the capacity of Ia-expressing L-cell transfectants to present antigens to apparently normal T cells. However, in contrast to splenic APC, L-cell transfectants fail to present native hen egg-white lysozyme to the same T cells. Since this result is similar to that obtained with physiologic APC pretreated to prevent antigen degradation, it suggests that L-cell transfectants, without such pretreatments, may be compromised in their ability to process native lysozyme. However, since such transfectant cells have been shown to present other complex polypeptides such as keyhole limpet hemocyanin, a random copolymer of glutamic acid, alanine, and tyrosine, and influenza virus neuraminidase, this observation suggests that protein antigens differ in the stringency of processing requirements. |
| Databáze: | OpenAIRE |
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