Immunological characterization of an immunomodulatory epitope in S-antigen/arrestin with a sequence motif common to tumor necrosis factor α
| Autor: | Massoud Mirshahi, R. Stiemer, Jean-Pierre Faure, Margot Kraft, Heinrich Gausepohl, Yvonne de Kozak, Rainer Frank |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
medicine.drug_class
Molecular Sequence Data Immunology Peptide Monoclonal antibody Epitope Autoimmune Diseases Conserved sequence Epitopes medicine Animals Immunology and Allergy Amino Acid Sequence Antigens Eye Proteins chemistry.chemical_classification Arrestin Linear epitope biology Tumor Necrosis Factor-alpha Retinitis Antibodies Monoclonal Molecular biology Pepscan chemistry biology.protein Cattle Binding Sites Antibody Antibody Peptides Sequence motif |
| Zdroj: | Immunology Letters. 32:233-240 |
| ISSN: | 0165-2478 |
| DOI: | 10.1016/0165-2478(92)90055-s |
| Popis: | Some monoclonal antibodies (mAbs) to retinal S-antigen recognize a phylogenetically conserved epitope (S2) in the N-terminal part of the protein. These antibodies have been shown to inhibit the induction of experimental autoimmune uveoretinitis by S-antigen in rats. Using Pepscan method, we localized this epitope on the amino acid (aa) residues 40-50, i.e., PVDGVVLVDPE (peptide S2). MAb binding was confirmed by ELISA, competition-ELISA and dot blot. Other S-antigen peptides with homologies to epitope S2 and peptides exhibiting the pathogenic and T-cell proliferation inducing sites did not bind these mAbs. Epitope S2 displays an immunological crossreactivity with human tumor necrosis factor (TNF) alpha. Recent results indicate that both peptide S2 and a peptide from human TNF alpha (aa residues 31-53) containing the common sequence motif GVxLxD induce TNF alpha production in monocytes. We analyzed the fine structure of the common epitope by studying mAb binding in an amino acid residue exchange experiment. |
| Databáze: | OpenAIRE |
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