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Enzyme-Sialylation-Controlled Chemical Sulfation of Glycan Epitopes for Decoding the Binding of Siglec Ligands

文献类型：期刊论文

作者Ma, Shengzhou6,7; Zhang, Pengfei6,7; Ye, Jinfeng4; Tian, Yinping6,7; Tian, Xiao3; Jung, Jaesoo2; Macauley, Matthew S.1,2; Zhang, Jiabin3,5,7; Wu, Peng4; Wen, Liuqing5,6,7
刊名JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
出版日期2024-10-17
卷号146期号:43页码:29469-29480
ISSN号0002-7863
DOI10.1021/jacs.4c08817
通讯作者Zhang, Jiabin(jiabinzhang@simm.ac.cn) ; Wu, Peng(pengwu@scripps.edu) ; Wen, Liuqing(lwen@simm.ac.cn)
英文摘要Widely distributed in nature, sulfated glycan epitopes play important roles in diverse pathophysiological processes. However, due to their structural complexity, the preparation of glycan epitopes with structurally defined sulfation patterns is challenging, which significantly hampers the detailed elucidation of their biological functions at the molecular level. Here, we introduce a strategy for site-specific chemical sulfation of glycan epitopes, leveraging enzymatic sialylation and desialylation processes to precisely control the regio-specificity of sulfation of disaccharide or trisaccharide glycan backbones. Using this method, a sulfated glycan library covering the most common sialylated glycan epitopes was prepared in high yield and efficiency. By screening a microarray prepared with this glycan library, we systematically probed their binding specificity with human Siglecs (sialic acid-binding immunoglobulin-type lectins), many of which function as glyco-immune checkpoints to suppress immune system activation. Our investigation revealed that sulfation and sialylation patterns serve as important determinants of Siglec binding affinity and specificity. Thus, these findings offer new insights for the development of research tools and potential therapeutic agents targeting glyco-immune checkpoints by modulating the Siglec signaling pathway.
WOS关键词EFFICIENT CHEMOENZYMATIC SYNTHESIS ; MAACKIA-AMURENSIS ; HIGH-AFFINITY ; SPECIFICITY ; IDENTIFICATION ; SIALOADHESIN ; CHONDROITIN ; MICROARRAYS ; EXPRESSION ; RECEPTOR
资助项目Talent Plan of Shanghai Branch, Chinese Academy of Sciences[CASSHB-QNPD-2023-018] ; National Natural Science Foundation of China[92478106] ; National Natural Science Foundation of China[22207113] ; Natural Science Foundation of Shanghai Municipality[22ZR1474000] ; Shanghai Municipal Science and Technology Major Project ; NIH[R01AI154138]
WOS研究方向Chemistry
语种英语
WOS记录号WOS:001337767300001
出版者AMER CHEMICAL SOC
源URL[http://119.78.100.183/handle/2S10ELR8/313999]  
专题中国科学院上海药物研究所
通讯作者Zhang, Jiabin; Wu, Peng; Wen, Liuqing
作者单位1.Univ Alberta, Dept Med Microbiol & Immunol, Edmonton, AB T6G 2E1, Canada
2.Univ Alberta, Dept Chem, Edmonton, AB T6G 2E1, Canada
3.Chinese Acad Sci, Zhongshan Inst Drug Discovery, Shanghai Inst Mat Med, Zhongshan 528400, Guangdong, Peoples R China
4.Scripps Res Inst, Dept Mol Med, La Jolla, CA 92037 USA
5.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
6.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Chem Biol, Shanghai 201203, Peoples R China
7.Chinese Acad Sci, Shanghai Inst Mat Med, Carbohydrate Based Drug Res Ctr, Shanghai 201203, Peoples R China
推荐引用方式
GB/T 7714		 Ma, Shengzhou,Zhang, Pengfei,Ye, Jinfeng,et al. Enzyme-Sialylation-Controlled Chemical Sulfation of Glycan Epitopes for Decoding the Binding of Siglec Ligands[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,2024,146(43):29469-29480.
APA Ma, Shengzhou.,Zhang, Pengfei.,Ye, Jinfeng.,Tian, Yinping.,Tian, Xiao.,...&Wen, Liuqing.(2024).Enzyme-Sialylation-Controlled Chemical Sulfation of Glycan Epitopes for Decoding the Binding of Siglec Ligands.JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,146(43),29469-29480.
MLA Ma, Shengzhou,et al."Enzyme-Sialylation-Controlled Chemical Sulfation of Glycan Epitopes for Decoding the Binding of Siglec Ligands".JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 146.43(2024):29469-29480.

入库方式： OAI收割

来源：上海药物研究所

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