Abstract：
The impact of human IgE glycosylation on structure, function and disease mechanisms is not fully elucidated, and heterogeneity in different studies renders drawing conclusions challenging. Previous reviews discussed IgE glycosylation focusing on specific topics such as health versus disease, FcεR binding or impact on function. We present the first systematic review of human IgE glycosylation conducted utilizing the PRISMA guidelines. We sought to define the current consensus concerning the roles of glycosylation on structure, biology and disease. Despite diverse analytical methodologies, source, expression systems and the sparsity of data on IgE antibodies from non-allergic individuals, collectively evidence suggests differential glycosylation profiles, particularly in allergic diseases compared with healthy states, and indicates functional impact, and contributions to IgE-mediated hypersensitivities and atopic diseases. Beyond allergic diseases, dysregulated terminal glycan structures, including sialic acid, may regulate IgE metabolism. Glycan sites such as N394 may contribute to stabilizing IgE structure, with alterations in these glycans likely influencing both structure and IgE-FcεR interactions. This systematic review therefore highlights critical IgE glycosylation attributes in health and disease that may be exploitable for therapeutic intervention, and the need for novel analytics to explore pertinent research avenues.
摘要：
人IgE糖基化对结构的影响,功能和疾病机制尚未完全阐明，不同研究中的异质性使得得出结论具有挑战性。以前的评论讨论了IgE糖基化关注特定主题，如健康与疾病，FcεR结合或对功能的影响。我们提出了利用PRISMA指南进行的人类IgE糖基化的第一个系统综述。我们试图定义目前关于糖基化在结构上的作用的共识，生物学和疾病。尽管分析方法多种多样，来源,表达系统和来自非过敏个体的IgE抗体数据的稀疏性，集体证据表明差异糖基化谱，特别是在与健康状态相比的过敏性疾病中，并表明功能影响，以及对IgE介导的超敏反应和特应性疾病的贡献。除了过敏性疾病，末端聚糖结构失调，包括唾液酸,可调节IgE代谢。聚糖位点如N394可能有助于稳定IgE结构，这些聚糖的改变可能影响结构和IgE-FcεR相互作用。因此，本系统综述强调了健康和疾病中关键的IgE糖基化属性，这些属性可能可用于治疗干预。以及需要新颖的分析来探索相关的研究途径。
