Chemoenzymatic Synthesis of Tri-antennary N-Glycans Terminating in Sialyl-Lewisx Reveals the Importance of Glycan Complexity for Influenza A Virus Receptor Binding
文献类型：期刊论文
| 作者 | Li, Tiehai4,5; Spruit, Cindy M.3; Wei, Na5; Liu, Lin5; Wolfert, Margreet A.3,5; de Vries, Robert P.3; Boons, Geert-Jan1,2,3,5 |
| 刊名 | CHEMISTRY-A EUROPEAN JOURNAL
 |
| 出版日期 | 2024-05-08 |
| 页码 | 15 |
| 关键词 | Glycan Glycosyltransferases Chemoenzymatic Receptor specificity Lectin |
| ISSN号 | 0947-6539 |
| DOI | 10.1002/chem.202401108 |
| 通讯作者 | de Vries, Robert P.(r.vries@uu.nl) ; Boons, Geert-Jan(gjboons@ccrc.uga.edu) |
| 英文摘要 | Sialyl-Lewis(x) (SLe(x)) is involved in immune regulation, human fertilization, cancer, and bacterial and viral diseases. The influence of the complex glycan structures, which can present SLex epitopes, on binding is largely unknown. We report here a chemoenzymatic strategy for the preparation of a panel of twenty-two isomeric asymmetrical tri-antennary N-glycans presenting SLex-Lex epitopes on either the MGAT4 or MGAT5 arm that include putative high-affinity ligands for E-selectin. The N-glycans were prepared starting from a sialoglycopeptide isolated from egg yolk powder and took advantage of inherent substrate preferences of glycosyltransferases and the use of 5 '-diphospho-N-trifluoracetylglucosamine (UDP-GlcNHTFA) that can be transferred by branching N-acetylglucosaminyltransferases to give, after base treatment, GlcNH(2)-containing glycans that temporarily disable an antenna from enzymatic modification. Glycan microarray binding studies showed that E-selectin bound equally well to linear glycans and tri-antennary N-glycans presenting SLe(x)-Le(x). On the other hand, it was found that hemagglutinins (HA) of H5 influenza A viruses (IAV) preferentially bound the tri-antennary N-glycans. Furthermore, several H5 HAs preferentially bound to N-glycan presenting SLe(x) on the MGAT4 arm. SLe(x) is displayed in the respiratory tract of several avian species, demonstrating the relevance of investigating the binding of, among others IAVs, to complex N-glycans presenting SLe(x). |
| WOS关键词 | LIGAND-SPECIFICITY ; GLYCOSYLATION ; LECTIN ; ACID ; HEMAGGLUTININ ; RECOGNIZES |
| 资助项目 | National Institute of Allergy and Infectious Diseases of the National Institutes of Health[R01 AI165692] ; ERC Starting Grant from the European Commission[802780] ; Beijerinck Premium of the Royal Dutch Academy of Sciences |
| WOS研究方向 | Chemistry |
| 语种 | 英语 |
| WOS记录号 | WOS:001215667600001 |
| 出版者 | WILEY-V C H VERLAG GMBH |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/310858]  |
| 专题 | 中国科学院上海药物研究所 |
| 通讯作者 | de Vries, Robert P.; Boons, Geert-Jan |
| 作者单位 | 1.Univ Georgia, Chem Dept, Athens, GA 30602 USA 2.Univ Utrecht, Bijvoet Ctr Biomol Res, Utrecht, Netherlands 3.Univ Utrecht, Utrecht Inst Pharmaceut Sci, Dept Chem Biol & Drug Discovery, NL-3584 CG Utrecht, Netherlands 4.Chinese Acad Sci, Shanghai Inst Mat Med, Shanghai, Peoples R China 5.Univ Georgia, Complex Carbohydrate Res Ctr, Athens, GA 30602 USA |
| 推荐引用方式 GB/T 7714 | Li, Tiehai,Spruit, Cindy M.,Wei, Na,et al. Chemoenzymatic Synthesis of Tri-antennary N-Glycans Terminating in Sialyl-Lewisx Reveals the Importance of Glycan Complexity for Influenza A Virus Receptor Binding[J]. CHEMISTRY-A EUROPEAN JOURNAL,2024:15. |
| APA | Li, Tiehai.,Spruit, Cindy M..,Wei, Na.,Liu, Lin.,Wolfert, Margreet A..,...&Boons, Geert-Jan.(2024).Chemoenzymatic Synthesis of Tri-antennary N-Glycans Terminating in Sialyl-Lewisx Reveals the Importance of Glycan Complexity for Influenza A Virus Receptor Binding.CHEMISTRY-A EUROPEAN JOURNAL,15. |
| MLA | Li, Tiehai,et al."Chemoenzymatic Synthesis of Tri-antennary N-Glycans Terminating in Sialyl-Lewisx Reveals the Importance of Glycan Complexity for Influenza A Virus Receptor Binding".CHEMISTRY-A EUROPEAN JOURNAL (2024):15. |
入库方式： OAI收割
来源：上海药物研究所
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