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The Ro/SSA autoantigen as an immunogen. Some anti-Ro/SSA antibody binds IgG
The rheumatic disease autoantigen, Ro/SSA, was immunogenic to a rabbit host. The heteroimmune rabbit serum bound the Ro/SSA particle in immunoblots and in an ELISA. Both the rabbit anti-Ro/SSA and a human prototype anti-Ro/SSA serum also bound IgG; and moreover, IgG inhibited both rabbit and human a...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1986
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188496/ https://www.ncbi.nlm.nih.gov/pubmed/3097237 |
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collection | PubMed |
description | The rheumatic disease autoantigen, Ro/SSA, was immunogenic to a rabbit host. The heteroimmune rabbit serum bound the Ro/SSA particle in immunoblots and in an ELISA. Both the rabbit anti-Ro/SSA and a human prototype anti-Ro/SSA serum also bound IgG; and moreover, IgG inhibited both rabbit and human anti-Ro/SSA activity. Anti-IgG activity of the rabbit and human anti-Ro/SSA sera bound Ro/SSA by Western blot and solid-phase assays. In addition, purified Ro/SSA inhibited the anti-IgG activity of the anti-Ro/SSA sera from rabbit and man. Affinity purification of the IgG- and Ro/SSA-binding fractions of the rabbit anti-Ro/SSA demonstrated that both the anti-Ro/SSA and anti-IgG activities were concentrated in these fractions. These data show that Ro/SSA and IgG share epitopes that are bound by anti-Ro/SSA antibody. Inhibition experiments suggest that this antibody is found in most human anti-Ro/SSA autoimmune sera and that the epitope(s) are found in the F(ab')2 fragment of IgG. |
format | Text |
id | pubmed-2188496 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1986 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21884962008-04-17 The Ro/SSA autoantigen as an immunogen. Some anti-Ro/SSA antibody binds IgG J Exp Med Articles The rheumatic disease autoantigen, Ro/SSA, was immunogenic to a rabbit host. The heteroimmune rabbit serum bound the Ro/SSA particle in immunoblots and in an ELISA. Both the rabbit anti-Ro/SSA and a human prototype anti-Ro/SSA serum also bound IgG; and moreover, IgG inhibited both rabbit and human anti-Ro/SSA activity. Anti-IgG activity of the rabbit and human anti-Ro/SSA sera bound Ro/SSA by Western blot and solid-phase assays. In addition, purified Ro/SSA inhibited the anti-IgG activity of the anti-Ro/SSA sera from rabbit and man. Affinity purification of the IgG- and Ro/SSA-binding fractions of the rabbit anti-Ro/SSA demonstrated that both the anti-Ro/SSA and anti-IgG activities were concentrated in these fractions. These data show that Ro/SSA and IgG share epitopes that are bound by anti-Ro/SSA antibody. Inhibition experiments suggest that this antibody is found in most human anti-Ro/SSA autoimmune sera and that the epitope(s) are found in the F(ab')2 fragment of IgG. The Rockefeller University Press 1986-12-01 /pmc/articles/PMC2188496/ /pubmed/3097237 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles The Ro/SSA autoantigen as an immunogen. Some anti-Ro/SSA antibody binds IgG |
title | The Ro/SSA autoantigen as an immunogen. Some anti-Ro/SSA antibody binds IgG |
title_full | The Ro/SSA autoantigen as an immunogen. Some anti-Ro/SSA antibody binds IgG |
title_fullStr | The Ro/SSA autoantigen as an immunogen. Some anti-Ro/SSA antibody binds IgG |
title_full_unstemmed | The Ro/SSA autoantigen as an immunogen. Some anti-Ro/SSA antibody binds IgG |
title_short | The Ro/SSA autoantigen as an immunogen. Some anti-Ro/SSA antibody binds IgG |
title_sort | ro/ssa autoantigen as an immunogen. some anti-ro/ssa antibody binds igg |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188496/ https://www.ncbi.nlm.nih.gov/pubmed/3097237 |