Department of Oral Biology, SUNY Buffalo, Buffalo, NY, USA.
Cell Immunol. 2010;263(1):41-8. doi: 10.1016/j.cellimm.2010.02.014. Epub 2010 Feb 24.
In this paper, we aim to characterize fibrinogen-IgG interactions, and explore how fibrinogen alters IgG-mediated phagocytosis. Using enzyme-linked binding assays, we found that fibrinogen binding to IgG is optimized for surfaces coated with high levels of IgG. Using a similar method, we have shown that for an antigen unable to specifically bind fibrinogen, fibrinogen enhances binding of antibodies towards that antigen. For binding of IgG antibodies to cells expressing Fc receptors, we found a bimodal binding response, where low levels of fibrinogen enhance binding of antibody to Fc receptors and high levels reduce it. This corresponds to a bimodal effect on phagocytosis of IgG-coated particles, which is inhibited in the presence of excess IgG during coating of the particles with antibodies and fibrinogen. We conclude that fibrinogen can modulate phagocytosis of IgG-coated particles in vitro by changing IgG binding behavior, and that high fibrinogen levels could negatively affect phagocytosis.
在本文中,我们旨在描述纤维蛋白原与 IgG 的相互作用,并探讨纤维蛋白原如何改变 IgG 介导的吞噬作用。我们使用酶联结合测定法发现,纤维蛋白原与 IgG 的结合在高浓度 IgG 包被的表面上达到最佳状态。使用类似的方法,我们已经表明,对于不能特异性结合纤维蛋白原的抗原,纤维蛋白原增强了针对该抗原的抗体的结合。对于表达 Fc 受体的细胞上 IgG 抗体的结合,我们发现了一种双模态结合反应,其中低浓度的纤维蛋白原增强了抗体与 Fc 受体的结合,而高浓度则降低了结合。这对应于 IgG 包被颗粒的吞噬作用的双模态效应,在抗体和纤维蛋白原包被颗粒的过程中,过量 IgG 的存在会抑制吞噬作用。我们得出结论,纤维蛋白原可以通过改变 IgG 的结合行为来调节体外 IgG 包被颗粒的吞噬作用,并且高纤维蛋白原水平可能会对吞噬作用产生负面影响。