Antibody glycosylation in inflammation, disease and vaccination.

Antibody glycosylation in inflammation, disease and vaccination.
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DOI:
10.1016/j.smim.2018.05.003
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发表时间:
2018-10
影响因子:
7.8
通讯作者:
Joosten SA
Joosten SA
中科院分区:
医学2区
文献类型:
--
作者:
Alter G;Ottenhoff THM;Joosten SA

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抗体是识别抗原的免疫球蛋白,在抗原特异性结构域中具有惊人的多样性。抗体应答的多样性通过修饰如体细胞重组和超突变进一步增加。此外,同种型的变化和翻译后修饰如Fc糖基化进一步增加效应子功能的多样性。特别地,聚糖结构的变化显著地有助于抗体的功能能力。考虑到这些修饰的动态性质受到炎症环境的强烈影响,这是特别感兴趣的。有趣的是,抗体的聚糖谱已经在炎性(自身)免疫疾病中被非常详细地揭示,但在感染性疾病和疫苗接种领域仅受到有限的关注。在这里,我们回顾了目前对免疫球蛋白糖基化的认识,特别关注传染病和传染病疫苗接种领域的研究,这是一个有很多有趣机会的领域。
Antibodies are antigen recognizing immunoglobulins with an amazingly diverse repertoire in the antigen specific domain. The diversity of the antibody response is further increased by modifications such as somatic recombination and hypermutation. Furthermore, variation in the isotype and post-translational modifications such as Fc glycosylation further increase diversity of the effector functions. In particular variations in the glycan structures contribute significantly to the functional capacities of the antibodies. This is of particular interest given the dynamic nature of these modifications that is strongly influenced by the inflammatory environment. Intriguingly, the glycan profile of antibodies has been unravelled in great detail in inflammatory (auto)immune diseases but received only limited attention in the area of infectious diseases and vaccination. Here, we reviewed the current knowledge on immunoglobulin glycosylation and specifically focussed on studies in the field of infectious diseases and vaccination against infectious diseases, an area with a lot of interesting opportunities.
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