Biomimetic Recognition of SARS-CoV-2 Receptor-Binding Domain N-Glycans by an Antiviral Synthetic Receptor.

IF 2.6 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
ChemBioChem Pub Date : 2025-02-21 DOI:10.1002/cbic.202500106
Carlo Santambrogio, Mirco Toccafondi, Lorena Donnici, Elisa Pesce, Raffaele De Francesco, Renata Grifantini, Erika Ponzini, Francesco Milanesi, Marco Fragai, Cristina Nativi, Stefano Roelens, Rita Grandori, Oscar Francesconi
{"title":"Biomimetic Recognition of SARS-CoV-2 Receptor-Binding Domain N-Glycans by an Antiviral Synthetic Receptor.","authors":"Carlo Santambrogio, Mirco Toccafondi, Lorena Donnici, Elisa Pesce, Raffaele De Francesco, Renata Grifantini, Erika Ponzini, Francesco Milanesi, Marco Fragai, Cristina Nativi, Stefano Roelens, Rita Grandori, Oscar Francesconi","doi":"10.1002/cbic.202500106","DOIUrl":null,"url":null,"abstract":"<p><p>Recognition of glycans by simple synthetic receptors is a key issue in supramolecular chemistry, endowed with relevant implications in glycobiology and medicine. In this context, glycoproteins featuring N-glycans represent an important biological target, because they are often exploited by enveloped viruses in adhesion and infection processes. However, a direct evidence for their recognition by a synthetic receptor targeting N-glycans is still missing in the literature. Using a combination of glycoengineering and mass spectrometry techniques, we present here the direct evidence of biomimetic recognition of complex-type N-glycans exposed on the receptor-binding domain (RBD) of the wild-type spike protein of SARS-CoV-2 by a biologically active, synthetic receptor.</p>","PeriodicalId":140,"journal":{"name":"ChemBioChem","volume":" ","pages":"e202500106"},"PeriodicalIF":2.6000,"publicationDate":"2025-02-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"ChemBioChem","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1002/cbic.202500106","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

Recognition of glycans by simple synthetic receptors is a key issue in supramolecular chemistry, endowed with relevant implications in glycobiology and medicine. In this context, glycoproteins featuring N-glycans represent an important biological target, because they are often exploited by enveloped viruses in adhesion and infection processes. However, a direct evidence for their recognition by a synthetic receptor targeting N-glycans is still missing in the literature. Using a combination of glycoengineering and mass spectrometry techniques, we present here the direct evidence of biomimetic recognition of complex-type N-glycans exposed on the receptor-binding domain (RBD) of the wild-type spike protein of SARS-CoV-2 by a biologically active, synthetic receptor.

简单合成受体识别聚糖是超分子化学的一个关键问题,对糖生物学和医学具有重要意义。在这方面,以 N-聚糖为特征的糖蛋白是一个重要的生物靶标,因为包膜病毒在粘附和感染过程中经常利用它们。然而,文献中仍缺少针对 N-糖的合成受体识别它们的直接证据。利用糖工程和质谱技术的结合,我们在这里展示了一种具有生物活性的合成受体对暴露在 SARS-CoV-2 野生型尖峰蛋白受体结合域(RBD)上的复合型 N-糖进行仿生识别的直接证据。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
ChemBioChem
ChemBioChem 生物-生化与分子生物学
CiteScore
6.10
自引率
3.10%
发文量
407
审稿时长
1 months
期刊介绍: ChemBioChem (Impact Factor 2018: 2.641) publishes important breakthroughs across all areas at the interface of chemistry and biology, including the fields of chemical biology, bioorganic chemistry, bioinorganic chemistry, synthetic biology, biocatalysis, bionanotechnology, and biomaterials. It is published on behalf of Chemistry Europe, an association of 16 European chemical societies, and supported by the Asian Chemical Editorial Society (ACES).
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信