• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

探究 SARS-CoV-2 变异株奥密克戎和 XBB 与常见表面的纳米力学相互作用。

Probing nanomechanical interactions of SARS-CoV-2 variants Omicron and XBB with common surfaces.

机构信息

State Key Laboratory of Coordination Chemistry, School of Chemistry and Chemical Engineering, Chemistry and Biomedicine Innovation Centre (ChemBIC), Nanjing University, Nanjing, China.

出版信息

Chem Commun (Camb). 2023 Sep 19;59(75):11268-11271. doi: 10.1039/d3cc02721j.

DOI:10.1039/d3cc02721j
PMID:37664897
Abstract

The emergence of SARS-CoV-2 variants has further raised concerns about viral transmission. A fundamental understanding of the intermolecular interactions between the coronavirus and different surfaces is needed to address the transmission of SARS-CoV-2 through respiratory droplet-contaminated surfaces or fomites. The receptor-binding domain (RBD) of the spike protein is a key target for the adhesion of SARS-CoV-2 on the surface. To understand the effect of mutations on adhesion, atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS) was used to quantify the interactions between wild-type, Omicron, and XBB with several surfaces. The measurement revealed that RBD exhibits relatively higher forces on paper and gold surfaces, with the average force being 1.5 times greater compared to that on plastic surface. In addition, the force elevation on paper and gold surfaces for the variants can reach ∼28% relative to the wild type. These findings enhance our understanding of the nanomechanical interactions of the virus on common surfaces.

摘要

SARS-CoV-2 变体的出现进一步引发了人们对病毒传播的担忧。为了解决通过呼吸道飞沫污染表面或污染物传播 SARS-CoV-2 的问题,需要深入了解冠状病毒与不同表面之间的分子间相互作用。刺突蛋白的受体结合域(RBD)是 SARS-CoV-2 表面附着的关键靶点。为了了解突变对附着的影响,使用基于原子力显微镜的单分子力谱学(AFM-SMFS)来量化野生型、奥密克戎和 XBB 与几种表面的相互作用。测量结果表明,RBD 在纸张和金表面上表现出相对较高的力,平均力比在塑料表面上高 1.5 倍。此外,变体在纸张和金表面上的力升高幅度相对于野生型可达约 28%。这些发现提高了我们对病毒在常见表面上的纳米力学相互作用的理解。

相似文献

1
Probing nanomechanical interactions of SARS-CoV-2 variants Omicron and XBB with common surfaces.探究 SARS-CoV-2 变异株奥密克戎和 XBB 与常见表面的纳米力学相互作用。
Chem Commun (Camb). 2023 Sep 19;59(75):11268-11271. doi: 10.1039/d3cc02721j.
2
A Nanomechanical Study on Deciphering the Stickiness of SARS-CoV-2 on Inanimate Surfaces.一种用于破译 SARS-CoV-2 在无生命表面粘性的纳米力学研究。
ACS Appl Mater Interfaces. 2020 Dec 30;12(52):58360-58368. doi: 10.1021/acsami.0c16800. Epub 2020 Dec 18.
3
Distinctive Features of the XBB.1.5 and XBB.1.16 Spike Protein Receptor-Binding Domains and Their Roles in Conformational Changes and Angiotensin-Converting Enzyme 2 Binding.XBB.1.5 和 XBB.1.16 刺突蛋白受体结合域的特征及其在构象变化和血管紧张素转化酶 2 结合中的作用。
Int J Mol Sci. 2023 Aug 9;24(16):12586. doi: 10.3390/ijms241612586.
4
Atomic Force Microscopy and Infrared Nanospectroscopy of COVID-19 Spike Protein for the Quantification of Adhesion to Common Surfaces.用于定量分析常见表面黏附性的 COVID-19 刺突蛋白原子力显微镜和红外纳米光谱研究
Langmuir. 2021 Oct 19;37(41):12089-12097. doi: 10.1021/acs.langmuir.1c01910. Epub 2021 Oct 5.
5
Assessment of mutations on RBD in the Spike protein of SARS-CoV-2 Alpha, Delta and Omicron variants.评估 SARS-CoV-2 Alpha、Delta 和 Omicron 变异株 Spike 蛋白上 RBD 突变。
Sci Rep. 2022 May 20;12(1):8540. doi: 10.1038/s41598-022-12479-9.
6
Omicron (BA.1) and sub-variants (BA.1.1, BA.2, and BA.3) of SARS-CoV-2 spike infectivity and pathogenicity: A comparative sequence and structural-based computational assessment.Omicron (BA.1)及其子变体(BA.1.1、BA.2 和 BA.3)对 SARS-CoV-2 刺突的感染性和致病性:基于序列和结构的比较计算评估。
J Med Virol. 2022 Oct;94(10):4780-4791. doi: 10.1002/jmv.27927. Epub 2022 Jun 16.
7
Structural Study of SARS-CoV-2 Antibodies Identifies a Broad-Spectrum Antibody That Neutralizes the Omicron Variant by Disassembling the Spike Trimer.SARS-CoV-2 抗体的结构研究鉴定出一种广谱抗体,通过分解 Spike 三聚体来中和奥密克戎变体。
J Virol. 2022 Aug 24;96(16):e0048022. doi: 10.1128/jvi.00480-22. Epub 2022 Aug 4.
8
Omicron BA.1 and BA.2 variants increase the interactions of SARS-CoV-2 spike glycoprotein with ACE2.奥密克戎 BA.1 和 BA.2 变异体增加了 SARS-CoV-2 刺突糖蛋白与 ACE2 的相互作用。
J Mol Graph Model. 2022 Dec;117:108286. doi: 10.1016/j.jmgm.2022.108286. Epub 2022 Aug 4.
9
Understanding the Driving Forces That Trigger Mutations in SARS-CoV-2: Mutational Energetics and the Role of Arginine Blockers in COVID-19 Therapy.理解引发 SARS-CoV-2 突变的驱动因素:突变能学以及精氨酸阻滞剂在 COVID-19 治疗中的作用。
Viruses. 2022 May 11;14(5):1029. doi: 10.3390/v14051029.
10
Probing the binding nature and stability of highly transmissible mutated variant alpha to omicron of SARS-CoV-2 RBD with ACE2 via molecular dynamics simulation.通过分子动力学模拟探究高传染性突变 alpha 变体与 SARS-CoV-2 RBD 上的 ACE2 的结合性质和稳定性。
J Cell Biochem. 2023 Aug;124(8):1115-1134. doi: 10.1002/jcb.30432. Epub 2023 Jul 12.

引用本文的文献

1
AlphaFold2 Modeling and Molecular Dynamics Simulations of the Conformational Ensembles for the SARS-CoV-2 Spike Omicron JN.1, KP.2 and KP.3 Variants: Mutational Profiling of Binding Energetics Reveals Epistatic Drivers of the ACE2 Affinity and Escape Hotspots of Antibody Resistance.AlphaFold2 对 SARS-CoV-2 刺突奥密克戎 JN.1、KP.2 和 KP.3 变体构象集合的建模和分子动力学模拟:结合能突变分析揭示 ACE2 亲和力的上位驱动因素和抗体耐药性逃逸热点。
Viruses. 2024 Sep 13;16(9):1458. doi: 10.3390/v16091458.
2
Molecular Mechanism of Interaction between DNA Aptamer and Receptor-Binding Domain of Severe Acute Respiratory Syndrome Coronavirus 2 Variants Revealed by Steered Molecular Dynamics Simulations.基于定向分子动力学模拟揭示的 DNA 适体与严重急性呼吸综合征冠状病毒 2 变异株受体结合域相互作用的分子机制。
Molecules. 2024 May 9;29(10):2215. doi: 10.3390/molecules29102215.
3
Enzymatic Protein Immobilization for Nanobody Array.酶固定化蛋白质用于纳米抗体阵列。
Molecules. 2024 Jan 11;29(2):366. doi: 10.3390/molecules29020366.