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. 2000 Jul 3;192(1):87–98. doi: 10.1084/jem.192.1.87

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© 2000 The Rockefeller University Press

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/).

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Recombinant forms of SpA display a broad range of Fab-binding avidities. The relative Fab-binding activities of five different forms of SpA were compared in inhibition immunoassays of the binding of an S107-encoded IgG in solution to wells coated with an SpA variant. In these studies, the activity of native SpA is compared with a form of SpA created by chemical modification (MSpA), an SpA monomer, domain D (DD′), and dimeric (dimtetDD′) and tetrameric (tetmDD′) forms of domain D′, which include two site-specific mutations that remove Fc-binding activity.