Characterization of two human IgM monoclonal antibodies reactive with HLA-B27
| Autor: | Antoine Toubert, K. Siemoneit, Thomas Eiermann, A. Wölpl, H. Neumayer, Shraga F. Goldmann |
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| Rok vydání: | 1995 |
| Předmět: |
medicine.drug_class
Immunology Molecular Sequence Data Monoclonal antibody Biochemistry Peripheral blood mononuclear cell Epitope Cell Line Mice Structure-Activity Relationship Pregnancy MHC class I Genetics medicine Tumor Cells Cultured Immunology and Allergy Cytotoxic T cell Animals Humans Amino Acid Sequence HLA-B27 Antigen Cell Line Transformed chemistry.chemical_classification biology Base Sequence Chemistry Antibodies Monoclonal General Medicine Molecular biology Amino acid Epitope mapping Immunoglobulin M biology.protein Leukocytes Mononuclear Female Antibody Epitope Mapping |
| Zdroj: | Tissue antigens. 46(4) |
| ISSN: | 0001-2815 |
| Popis: | We describe here the generation and characterization of two human monoclonal IgM antibodies (UL-4F11 and UL-F6) reactive with HLA-B27. The monoclonal antibody (mAb) UL-4F11 is cytotoxic for peripheral mononuclear cells and, therefore, useful as typing reagent for HLA-B27 and HLA-B38. Protein chemistry showed that the mAb UL-4F11 precipitates HLA-B27 molecules. Epitope mapping analysis suggests that the amino acids 45, 67, 82 and 83 (alpha-1 domain) of the HLA-B27 sequence are necessary for mAb UL-4F11 reactivity. The mAb UL-F6 is suitable for complement dependent lysis of lymphoblastoid cell lines and stimulated peripheral blood mononuclear cells with HLA-B27 (B*2701, B*2702, B*2703, B*2705, B*2707), B13, B40 (60, 61), B47 and B48 specificities. Its reactivity indicates that the amino acid valine in position 152 and glutamic acid in position 163 of the alpha-2 domain are crucial for the binding epitope. |
| Databáze: | OpenAIRE |
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