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Elucidation of N-/O-glycosylation and site-specific mapping of sialic acid linkage isomers of SARS-CoV-2 human receptor angiotensin-converting enzyme 2

文献类型：期刊论文

作者Wei, Liming3,4; Chen, Yuning1,2; Feng, Xiaoxiao3,4; Yao, Jun3,4; Zhang, Lei3,4; Zhou, Xinwen3,4; Yan, Guoquan3,4; Qiu, Hong1,2; Wang, Chunhe1,2; Lu, Haojie3,4
刊名ANALYST
出版日期2023-10-05
卷号148期号:20页码:5002-5011
ISSN号0003-2654
DOI10.1039/d3an01079a
通讯作者Wang, Chunhe(wangc@simm.ac.cn) ; Lu, Haojie(luhaojie@fudan.edu.cn)
英文摘要Human angiotensin-converting enzyme 2 (hACE2) is the primary receptor for cellular entry of SARS-CoV-2 into human host cells. hACE2 is heavily glycosylated and glycans on the receptor may play a role in viral binding. Thus, comprehensive characterization of hACE2 glycosylation could aid our understanding of interactions between the receptor and SARS-CoV-2 spike (S) protein, as well as provide a basis for the development of therapeutic drugs targeting this crucial interaction. Herein, 138 N-glycan compositions were identified, most of which are complex-type N-glycans, from seven N-glycosites of hACE2. Among them, 67% contain at least one sialic acid residue. At the level of glycopeptides, the overall quantification of sialylated glycan isomers observed on the sites N322 and N546 have a higher degree of NeuAc (a2-3)Gal (over 80.3%) than that of other N-glycosites (35.6-71.0%). In terms of O-glycans, 69 glycan compositions from 12 O-glycosites were identified, and especially, the C-terminus of hACE2 is heavily O-glycosylated. The terminal sialic acid linkage type of H1N1S1 and H1N1S2 are covered highly with a2,3-sialic acid. These findings could aid the investigation of the interaction between SARS-CoV-2 and human host cells.
WOS关键词O-GLYCOSYLATION ; SPIKE ; GLYCAN ; VIRUS ; RBD ; COV
资助项目Shanghai Science and Technology Program[2016YFA0501303] ; Shanghai Science and Technology Program[2020YFE0202200] ; National Key Research and Development Program of China[21974025] ; NSF of China[18PJD002] ; Shanghai Pujiang Program[2017SHZDZX01] ; Shanghai Municipal Science and Technology Major Project ; NHC Key Laboratory of Glycoconjugates Research (Fudan University)
WOS研究方向Chemistry
语种英语
出版者ROYAL SOC CHEMISTRY
WOS记录号WOS:001068858000001
源URL[http://119.78.100.183/handle/2S10ELR8/307257]  
专题中国科学院上海药物研究所
通讯作者Wang, Chunhe; Lu, Haojie
作者单位1.Univ Chinese Acad Sci, Sch Pharm, 19A Yuquan Rd, Beijing 100049, Peoples R China
2.Chinese Acad Sci Dept, Shanghai Inst Mat Med, 555 Zuchongzhi Rd, Shanghai 201203, Peoples R China
3.Fudan Univ, Dept Chem, 131 Dongan Rd, Shanghai, Peoples R China
4.Fudan Univ, Inst Biomed Sci, 131 Dongan Rd, Shanghai, Peoples R China
推荐引用方式
GB/T 7714		 Wei, Liming,Chen, Yuning,Feng, Xiaoxiao,et al. Elucidation of N-/O-glycosylation and site-specific mapping of sialic acid linkage isomers of SARS-CoV-2 human receptor angiotensin-converting enzyme 2[J]. ANALYST,2023,148(20):5002-5011.
APA Wei, Liming.,Chen, Yuning.,Feng, Xiaoxiao.,Yao, Jun.,Zhang, Lei.,...&Lu, Haojie.(2023).Elucidation of N-/O-glycosylation and site-specific mapping of sialic acid linkage isomers of SARS-CoV-2 human receptor angiotensin-converting enzyme 2.ANALYST,148(20),5002-5011.
MLA Wei, Liming,et al."Elucidation of N-/O-glycosylation and site-specific mapping of sialic acid linkage isomers of SARS-CoV-2 human receptor angiotensin-converting enzyme 2".ANALYST 148.20(2023):5002-5011.

入库方式： OAI收割

来源：上海药物研究所

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