Anti-β2 glycoprotein I (β2GPI) autoantibodies recognize an epitope on the first domain of β2GPI
| Autor: | D M Marquis, Edward J. Victoria, G M Iverson |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1998 |
| Předmět: |
Enzyme-Linked Immunosorbent Assay
Biology Epitope Chromatography Affinity law.invention Epitopes law medicine Beta 2-Glycoprotein I Humans Amino Acid Sequence Peptide sequence Autoantibodies Glycoproteins Sequence Deletion Autoimmune disease chemistry.chemical_classification Multidisciplinary Autoantibody Anticoagulants Thrombosis Biological Sciences medicine.disease musculoskeletal system Virology Molecular biology Thrombocytopenia Recombinant Proteins chemistry Mutagenesis beta 2-Glycoprotein I Recombinant DNA Phospholipid Binding Glycoprotein |
| Popis: | Anticardiolipin (aCL) autoantibodies are associated with thrombosis, recurrent fetal loss, and thrombocytopenia. Only aCL found in autoimmune disease require the participation of the phospholipid binding plasma protein beta2 glycoprotein I (beta2GPI) for antibody binding and now are called anti-beta2GPI. The antigenic specificity of aCL affinity purified from 11 patients with high titers was evaluated in an effort to better understand the pathophysiology associated with aCL. Seven different recombinant domain-deleted mutants of human beta2GPI, and full length human beta2GPI (wild-type), were used in competition assays to inhibit the autoantibodies from binding to immobilized wild-type beta2GPI. Only those domain-deleted mutants that contained domain 1 inhibited the binding to immobilized wild-type beta2GPI from all of the patients. The domain-deleted mutants that contained domain 1 inhibited all aCL in a similar but not identical pattern, suggesting that these aCL recognize a similar, but distinguishable, epitope(s) present on domain 1. |
| Databáze: | OpenAIRE |
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