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.

中文翻译：

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IgE 糖基化及其对结构和功能的影响：系统评价


人类 IgE 糖基化对结构、功能和疾病机制的影响尚未完全阐明，不同研究的异质性使得得出结论具有挑战性。以前的综述讨论了 IgE 糖基化，侧重于特定主题，例如健康与疾病、FcεR 结合或对功能的影响。我们提出了第一个使用 PRISMA 指南进行的人 IgE 糖基化的系统评价。我们试图定义当前关于糖基化对结构、生物学和疾病作用的共识。尽管分析方法、来源、表达系统以及来自非过敏个体的 IgE 抗体数据稀缺，但总体证据表明糖基化谱不同，尤其是在与健康状态相比的过敏性疾病中，并表明功能影响和对 IgE 介导的超敏反应和特应性疾病的贡献。除了过敏性疾病外，失调的末端聚糖结构（包括唾液酸）可能调节 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会影响结构和 IgE-FcεR 相互作用。因此，本系统综述强调了健康和疾病中可用于治疗干预的关键 IgE 糖基化属性，以及需要新的分析来探索相关的研究途径。