Wed, 20 Aug 2008 22:09:03 BST CiteULike: davidlott Anthony http://www.citeulike.org/user/davidlott/author/Anthony CiteULike.org en-gb Copyright © 2004-2008 citeulike.org http://www.citeulike.org/user/davidlott/article/2739090 <i>Science, Vol. 320, No. 5874. (18 April 2008), pp. 373-376.</i><br /><br />It is well established that high doses of monomeric immunoglobulin G (IgG) purified from pooled human plasma [intravenous immunoglobulin (IVIG)] confer anti-inflammatory activity in a variety of autoimmune settings. However, exactly how those effects are mediated is not clear because of the heterogeneity of IVIG. Recent studies have demonstrated that the anti-inflammatory activity of IgG is completely dependent on sialylation of the N-linked glycan of the IgG Fc fragment. Here we determine the precise glycan requirements for this anti-inflammatory activity, allowing us to engineer an appropriate IgG1 Fc fragment, and thus generate a fully recombinant, sialylated IgG1 Fc with greatly enhanced potency. This therapeutic molecule precisely defines the biologically active component of IVIG and helps guide development of an IVIG replacement with improved activity and availability. 10.1126/science.1154315 Recapitulation of IVIG Anti-Inflammatory Activity with a Recombinant IgG Fc Robert Anthony Falk Nimmerjahn David Ashline Vernon Reinhold James Paulson Jeffrey Ravetch doi:10.1126/science.1154315 Science, Vol. 320, No. 5874. (18 April 2008), pp. 373-376. 2008-04-30T16:15:50-00:00 2008 Science 320 5874 373 376 antibody autoimmune heterogeneity igg immunoglobin inflammation monomeric