A Method to Detect the Binding of Hyper-Glycosylated Fragment Crystallizable (Fc) Region of Human IgG1 to Glycan Receptors.

A Method to Detect the Binding of Hyper-Glycosylated Fragment Crystallizable (Fc) Region of Human IgG1 to Glycan Receptors.
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一种检测人 IgG1 高糖基化片段可结晶 (Fc) 区域与聚糖受体结合的方法。

DOI:
10.1007/978-1-4939-8958-4_20
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发表时间:
2019
期刊:
Methods in molecular biology (Clifton, N.J.)
影响因子:
--
通讯作者:
Blundell P
Blundell P
中科院分区:
--
文献类型:
--
作者:
Blundell P

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工程化人IgG的可结晶片段(Fc)可以为单克隆抗体和基于Fc融合的药物和疫苗带来改善的效应器功能。此类Fc效应子功能主要由Fc内的翻译后修饰(PTM)控制,包括添加聚糖,其向这类治疗剂引入结构和功能异质性。在这里,我们描述了一个详细的方法,允许检测超唾液酸化的Fc聚糖受体,这将有助于未来开发新的单克隆抗体和Fc片段的治疗和疫苗。
Engineering the fragment crystallizable (Fc) of human IgG can bring improved effector functions to monoclonal antibodies and Fc-fusion-based medicines and vaccines. Such Fc-effector functions are largely controlled by posttranslational modifications (PTMs) within the Fc, including the addition of glycans that introduce structural and functional heterogeneity to this class of therapeutic. Here, we describe a detailed method to allow the detection of hyper-sialylated Fcs to glycan receptors that will facilitate the future development of new mAbs and Fc-fragment therapies and vaccines.
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发表时间: 2015-05-05
影响因子: 11.1
作者:
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通讯作者: Ravetch, Jeffrey V.
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影响因子: 11.1
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