Recapitulation of IVIG Anti-Inflammatory Activity with a Recombinant IgG Fc Export

@article{citeulike:2739090, abstract = {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}, author = {Anthony, Robert M. and Nimmerjahn, Falk and Ashline, David J. and Reinhold, Vernon N. and Paulson, James C. and Ravetch, Jeffrey V.}, citeulike-article-id = {2739090}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.1154315}, citeulike-linkout-1 = {http://www.sciencemag.org/cgi/content/abstract/320/5874/373}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/18420934}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=18420934}, day = {18}, doi = {10.1126/science.1154315}, journal = {Science}, keywords = {antibody, autoimmune, heterogeneity, igg, immunoglobin, inflammation, monomeric}, month = {April}, number = {5874}, pages = {373--376}, posted-at = {2008-04-30 17:16:29}, priority = {2}, title = {Recapitulation of IVIG Anti-Inflammatory Activity with a Recombinant IgG Fc}, url = {http://dx.doi.org/10.1126/science.1154315}, volume = {320}, year = {2008} }

TY - JOUR ID - citeulike:2739090 L3 - citeulike-article-id:2739090 N2 - 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 IS - 5874 JF - Science EP - 376 TI - Recapitulation of IVIG Anti-Inflammatory Activity with a Recombinant IgG Fc VL - 320 SP - 373 KW - antibody KW - autoimmune KW - heterogeneity KW - igg KW - immunoglobin KW - inflammation KW - monomeric AU - Anthony, Robert AU - Nimmerjahn, Falk AU - Ashline, David AU - Reinhold, Vernon AU - Paulson, James AU - Ravetch, Jeffrey PY - 2008/04/18/ UR - http://dx.doi.org/10.1126/science.1154315 ER -