Affiliation:
1. Department of Immunology, Rappaport Faculty of Medicine, Technion, Haifa, Israel
Abstract
Abstract
Treatment with IVIg can, on rare occasions, lead to detrimental effects such as enhanced erythrocyte sequestration and an increase in serum immune complexes with inflammatory sequellae such as exacerbation of glomerular nephritis. In this study, IVIg (Sandoglobin) was examined for complement binding moieties which resemble immune complexes and can mediate the binding of IgG and C′3b to human erythrocytes via CR1 and enhance erythrocyte susceptibility to sequestration. Sephacryl S-200 HR separated IVIg into two fractions: monomeric IgG (74%) and larger complexes of the molecular weight of an IgG dimer or greater (≥ 300 kD) (26%). In the presence of complement, the ‘dimers’ bound to human erythrocytes, rendering them susceptible to phagocytosis in vitro. Removal of erythrocyte-specific isoantibodies from the IVIg had no effect on ‘dimer’ binding to the erythrocytes. Monomeric IgG contained virtually no complement-activating, erythrocyte-binding activity. Erythrocyte binding of complement-bearing IgG ‘dimers’ and subsequent phagocytosis resembles the binding of complement-bearing immune complexes to erythrocyte CR1. Exposure to Factor I leads to the release of complement-bearing IgG ‘dimers’ from erythrocyte CR1 and to the abrogation of erythrophagocytosis. Binding of complement-bearing IgG ‘dimers’ to the erythrocyte is blocked by To5, a CR1-specific monoclonal antibody.
Publisher
Oxford University Press (OUP)
Subject
Immunology,Immunology and Allergy
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