Molecular chaperones and the immune response
| Autor: | Willi K. Born, Douglas B. Young, E. Roman, M.-J. Gething, I. G. Haas, A. R. Coates, Rebecca L. O'Brien, P. Viitanen, W. J. Welch, P. Lund, C Moreno |
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| Rok vydání: | 1993 |
| Předmět: |
Binding Sites
Chaperonins Antigen processing T-Lymphocytes Immunogenicity Histocompatibility Antigens Class I Antigen presentation Histocompatibility Antigens Class II Proteins T lymphocyte Biology General Biochemistry Genetics and Molecular Biology Cell biology Epitopes Immune system Antigen Heat shock protein Chaperone (protein) biology.protein Animals Humans Antigens General Agricultural and Biological Sciences Heat-Shock Proteins |
| Zdroj: | Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences. 339:363-368 |
| ISSN: | 1471-2970 0962-8436 |
| Popis: | Molecular chaperones belonging to heat shock protein families have been identified as prominent antigens in the immune response to a wide variety of infections. Recognition of such highly conserved antigens may contribute to protective immunity but, in some circumstances, may also have pathological autoimmune consequences. Recognition of chaperones may be an inherent feature of the immune system. Peptide mapping experiments revealed an overlap between hsp 70-binding sites and immunodominant regions of three protein antigens, consistent with a possible functional activity for molecular chaperones in the processing and presentation of peptides during class II-restricted T lymphocyte responses. A functional role for molecular chaperones in antigen processing may be a factor which contributes to their immunogenicity. |
| Databáze: | OpenAIRE |
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