Self-assembly of Human Galectin-1 via dual supramolecular interactions and its inhibition of T-cell agglutination and apoptosis
Self-assembly of Human Galectin-1 via dual supramolecular interactions and its inhibition of T-cell agglutination and apoptosis
复制标题
人半乳糖凝集素-1通过双重超分子相互作用的自组装及其对T细胞凝集和凋亡的抑制
DOI：
10.1007/s12274-018-2169-7
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发表时间：
2018-08
期刊：
影响因子：
9.9
通讯作者：
Jiang Ming
中科院分区：
文献类型：
--
作者：
Qi Wenjing;Zhang Yufei;Kochovski Zdravko;Wang Jue;Lu Yan;Chen Guosong;Jiang Ming
最近，我们提出了一种新的策略，构建人工植物蛋白组装体，这是通过添加一个小分子诱导，基于双超分子相互作用。在本文中，我们进一步探索了这种方法，用人半乳糖凝集素-1（Gal-1）作为构建块，形成自组装微带。两个非共价相互作用，包括乳糖-凝集素结合和罗丹明B（Rh B）的二聚化，由小分子配体的添加诱导，参与了动物蛋白的交联，导致组装体的形成。通过使用透射电子显微镜（TEM），冷冻电子显微镜（cryo-EM），和三维（3D）断层分析，我们到达了一个可能的机制模型的microorientations形成。此外，蛋白质组装体的形态可以通过改变孵育时间、蛋白质/配体比率和配体的化学结构来微调。有趣的是，蛋白质微带的形成成功地抑制了Gal-1诱导的T细胞凝集和凋亡。这是因为蛋白质组装体中的多价和动态相互作用与Gal-1和细胞表面上的聚糖之间的结合竞争，这抑制了Gal-1在促进肿瘤进展和转移中的功能。
Recently, we proposed a new strategy to construct artificial plant protein assemblies, which were induced by adding a small molecule, based on dual supramolecular interactions. In this paper, we further explored this method by employing Human Galectin-1 (Gal-1) as a building block to form self-assembled microribbons. Two non-covalent interactions, including lactose–lectin binding and dimerization of Rhodamine B (RhB), induced by the small molecule ligand addition, were involved in the crosslinking of the animal protein, resulting in the formation of assemblies. By using transmission electron microscopy (TEM), cryo-electron microscopy (cryo-EM), and three-dimensional (3D) tomographic analysis, we arrived at a possible mechanistic model for the microribbon formation. Furthermore, the morphology of protein assemblies could be fine-tuned by varying the incubation time, the protein/ligand ratio, and the chemical structures of ligands. Interestingly, the formation of protein microribbons successfully inhibited Gal-1 induced T-cell agglutination and apoptosis. This is because the multivalent and dynamic interactions in protein assemblies compete with the binding between Gal-1 and the glycans on cell surfaces, which suppresses the function of Gal-1 in promotion of tumor progression and metastasis.
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