Immunoglobulin Research Laboratory, Department of Experimental Immunohematology, Sanquin Research, Amsterdam, The Netherlands; Department of Biomolecular Mass Spectrometry and Proteomics, Utrecht Institute for Pharmaceutical Sciences and Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, The Netherlands.
Immunoglobulin Research Laboratory, Department of Experimental Immunohematology, Sanquin Research, Amsterdam, The Netherlands; Landsteiner Laboratory, Amsterdam University Medical Center (UMC), University of Amsterdam, Amsterdam, The Netherlands.
Trends Immunol. 2022 Oct;43(10):800-814. doi: 10.1016/j.it.2022.08.001. Epub 2022 Aug 22.
Healthy immune responses require efficient protection without excessive inflammation. Recent discoveries on the degree of fucosylation of a human N-linked glycan at a conserved site in the immunoglobulin IgG-Fc domain might add an additional regulatory layer to adaptive humoral immunity. Specifically, afucosylation of IgG-Fc enhances the interaction of IgG with FcγRIII and thereby its activity. Although plasma IgG is generally fucosylated, afucosylated IgG is raised in responses to enveloped viruses and Plasmodium falciparum proteins expressed on infected erythrocytes, as well as during alloimmune responses. Moreover, while afucosylation can exacerbate some infectious diseases (e.g., COVID-19), it also correlates with traits of protective immunity against malaria and HIV-1. Herein we discuss the implications of IgG afucosylation for health and disease, as well as for vaccination.
健康的免疫反应需要在不过度引发炎症的情况下进行有效保护。最近在人类免疫球蛋白 IgG-Fc 结构域中保守位点的 N-连接糖基化程度方面的发现，可能为适应性体液免疫增加了一个额外的调节层。具体来说，IgG-Fc 的去岩藻糖化增强了 IgG 与 FcγRIII 的相互作用，从而提高了其活性。尽管血浆 IgG 通常是岩藻糖化的，但在针对包膜病毒和感染红细胞上表达的疟原虫蛋白的反应中以及在同种免疫反应中会产生去岩藻糖化的 IgG。此外，虽然去岩藻糖化会加重某些传染病（例如 COVID-19），但它也与针对疟疾和 HIV-1 的保护性免疫特征相关。本文讨论了 IgG 去岩藻糖化对健康和疾病以及疫苗接种的影响。
