中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Chemical Synthesis Creates Single Glycoforms of the Ectodomain of Herpes Simplex Virus-1 Glycoprotein D

文献类型:期刊论文

作者Zhao, Jie1; Liu, Xinliang1; Liu, Jialin4; Ye, Farong1; Wei, Bingcheng1; Deng, Minggang3; Li, Tiehai4; Huang, Ping1; Wang, Ping1,2
刊名JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
出版日期2023-12-20
卷号146期号:4页码:2615-2623
ISSN号0002-7863
DOI10.1021/jacs.3c11543
通讯作者Li, Tiehai(tiehaili@simm.ac.cn) ; Huang, Ping(hp158@sjtu.edu.cn) ; Wang, Ping(wangp1@sjtu.edu.cn)
英文摘要Herpes simplex virus-1 (HSV-1) utilizes multiple viral surface glycoproteins to trigger virus entry and fusion. Among these glycoproteins, glycoprotein D (gD) functions as a receptor-binding protein, which makes it an attractive target for the development of vaccines against HSV-1 infection. Several recombinant gD subunit vaccines have been investigated in both preclinical and clinical phases with varying degrees of success. It is fundamentally critical to explore the functions of gD glycans. In light of this, we report an efficient synthetic platform to construct glycosylated gDs bearing homogeneous glycans at N94 and N121. The oligosaccharides were prepared by enzymatic synthesis and conjugated to peptidyl sectors. The glycoproteins were constructed via a combination of 7-(piperazin-1-yl)-2-(methyl)-quinolinyl (PPZQ)-assisted expressed protein ligation and beta-mercapto amino acid-assisted-desulfurization strategies. Biological studies showed that synthetic gDs exhibited potent in vivo activity in mice.
WOS关键词LINKED OLIGOSACCHARIDES ; LIGATION ; PROTEIN ; TYPE-1 ; DESULFURIZATION ; CYSTEINE ; GLYCOPEPTIDES ; EXPRESSION ; INFECTION ; PEPTIDES
资助项目China Postdoctoral Science Foundation[22225701] ; National Science Fund for Distinguished Young Scholars[22077080] ; National Science Fund for Distinguished Young Scholars[92253302] ; National Science Fund for Distinguished Young Scholars[22077130] ; National Science Fund for Distinguished Young Scholars[22275122] ; National Natural Science Foundation of China[21TQ1400210] ; Shanghai Pilot Program for Basic Research-Shanghai Jiao Tong University[2023M732214] ; China Postdoctoral Science Foundation[20230102] ; Interdisciplinary Program of Shanghai Jiao Tong University[2021Szvup077] ; Special Projects of the Central Government in Guidance of Local Science and Technology Development
WOS研究方向Chemistry
语种英语
出版者AMER CHEMICAL SOC
WOS记录号WOS:001155532300001
源URL[http://119.78.100.183/handle/2S10ELR8/309063]  
专题中国科学院上海药物研究所
通讯作者Li, Tiehai; Huang, Ping; Wang, Ping
作者单位1.Zhangjiang Inst Adv Study, Ctr Chem Glycobiol, Frontiers Sci Ctr Transformat Mol, Sch Chem & Chem Engn,Shanghai Key Lab Mol Engn Ch, Shanghai 200240, Peoples R China
2.Shanghai Jiao Tong Univ, Shenzhen Res Inst, Shenzhen 518057, Peoples R China
3.Huazhong Agr Univ, Coll Life Sci & Technol, State Key Lab Agr Microbiol, Wuhan 430070, Peoples R China
4.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Chem Biol, Shanghai 201203, Peoples R China
推荐引用方式
GB/T 7714
Zhao, Jie,Liu, Xinliang,Liu, Jialin,et al. Chemical Synthesis Creates Single Glycoforms of the Ectodomain of Herpes Simplex Virus-1 Glycoprotein D[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,2023,146(4):2615-2623.
APA Zhao, Jie.,Liu, Xinliang.,Liu, Jialin.,Ye, Farong.,Wei, Bingcheng.,...&Wang, Ping.(2023).Chemical Synthesis Creates Single Glycoforms of the Ectodomain of Herpes Simplex Virus-1 Glycoprotein D.JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,146(4),2615-2623.
MLA Zhao, Jie,et al."Chemical Synthesis Creates Single Glycoforms of the Ectodomain of Herpes Simplex Virus-1 Glycoprotein D".JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 146.4(2023):2615-2623.

入库方式: OAI收割

来源:上海药物研究所

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