SARS-CoV-2变异体受体结合域突变集对RBD-ACE2复合物稳定性的影响

IF 2.1 4区 医学 Q3 VIROLOGY Future Virology Pub Date : 2023-03-01 DOI:10.2217/fvl-2022-0152
Mykyta Peka, Viktor Balatsky
{"title":"SARS-CoV-2变异体受体结合域突变集对RBD-ACE2复合物稳定性的影响","authors":"Mykyta Peka,&nbsp;Viktor Balatsky","doi":"10.2217/fvl-2022-0152","DOIUrl":null,"url":null,"abstract":"<p><p><b>Aim:</b> Bioinformatic analysis of mutation sets in receptor-binding domain (RBD) of currently and previously circulating SARS-CoV-2 variants of concern (VOCs) and interest (VOIs) to assess their ability to bind the ACE2 receptor. <b>Methods:</b> <i>In silico</i> sequence and structure-oriented approaches were used to evaluate the impact of single and multiple mutations. <b>Results:</b> Mutations detected in VOCs and VOIs led to the reduction of binding free energy of the RBD-ACE2 complex, forming additional chemical bonds with ACE2, and to an increase of RBD-ACE2 complex stability. <b>Conclusion:</b> Mutation sets characteristic of SARS-CoV-2 variants have complex effects on the ACE2 receptor-binding affinity associated with amino acid interactions at mutation sites, as well as on the acquisition of other viral adaptive advantages.</p>","PeriodicalId":12505,"journal":{"name":"Future Virology","volume":" ","pages":""},"PeriodicalIF":2.1000,"publicationDate":"2023-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/97/65/fvl-2022-0152.PMC10089296.pdf","citationCount":"2","resultStr":"{\"title\":\"The impact of mutation sets in receptor-binding domain of SARS-CoV-2 variants on the stability of RBD-ACE2 complex.\",\"authors\":\"Mykyta Peka,&nbsp;Viktor Balatsky\",\"doi\":\"10.2217/fvl-2022-0152\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p><b>Aim:</b> Bioinformatic analysis of mutation sets in receptor-binding domain (RBD) of currently and previously circulating SARS-CoV-2 variants of concern (VOCs) and interest (VOIs) to assess their ability to bind the ACE2 receptor. <b>Methods:</b> <i>In silico</i> sequence and structure-oriented approaches were used to evaluate the impact of single and multiple mutations. <b>Results:</b> Mutations detected in VOCs and VOIs led to the reduction of binding free energy of the RBD-ACE2 complex, forming additional chemical bonds with ACE2, and to an increase of RBD-ACE2 complex stability. <b>Conclusion:</b> Mutation sets characteristic of SARS-CoV-2 variants have complex effects on the ACE2 receptor-binding affinity associated with amino acid interactions at mutation sites, as well as on the acquisition of other viral adaptive advantages.</p>\",\"PeriodicalId\":12505,\"journal\":{\"name\":\"Future Virology\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":2.1000,\"publicationDate\":\"2023-03-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/97/65/fvl-2022-0152.PMC10089296.pdf\",\"citationCount\":\"2\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Future Virology\",\"FirstCategoryId\":\"3\",\"ListUrlMain\":\"https://doi.org/10.2217/fvl-2022-0152\",\"RegionNum\":4,\"RegionCategory\":\"医学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"VIROLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Future Virology","FirstCategoryId":"3","ListUrlMain":"https://doi.org/10.2217/fvl-2022-0152","RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"VIROLOGY","Score":null,"Total":0}
引用次数: 2

摘要

目的:通过生物信息学分析当前和以前流行的SARS-CoV-2关注变异体(VOCs)和感兴趣变异体(VOIs)的受体结合域(RBD)突变集,评估其结合ACE2受体的能力。方法:采用计算机序列法和结构定向法评价单突变和多突变的影响。结果:在VOCs和VOIs中检测到的突变导致RBD-ACE2复合物的结合自由能降低,与ACE2形成额外的化学键,RBD-ACE2复合物的稳定性增加。结论:SARS-CoV-2变异的突变集特征对突变位点氨基酸相互作用相关的ACE2受体结合亲和力以及其他病毒适应性优势的获得具有复杂的影响。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

摘要图片

摘要图片

摘要图片

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
The impact of mutation sets in receptor-binding domain of SARS-CoV-2 variants on the stability of RBD-ACE2 complex.

Aim: Bioinformatic analysis of mutation sets in receptor-binding domain (RBD) of currently and previously circulating SARS-CoV-2 variants of concern (VOCs) and interest (VOIs) to assess their ability to bind the ACE2 receptor. Methods: In silico sequence and structure-oriented approaches were used to evaluate the impact of single and multiple mutations. Results: Mutations detected in VOCs and VOIs led to the reduction of binding free energy of the RBD-ACE2 complex, forming additional chemical bonds with ACE2, and to an increase of RBD-ACE2 complex stability. Conclusion: Mutation sets characteristic of SARS-CoV-2 variants have complex effects on the ACE2 receptor-binding affinity associated with amino acid interactions at mutation sites, as well as on the acquisition of other viral adaptive advantages.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Future Virology
Future Virology 医学-病毒学
CiteScore
4.00
自引率
3.20%
发文量
84
审稿时长
6-12 weeks
期刊介绍: Future Virology is a peer-reviewed journal that delivers essential information in concise, at-a-glance article formats. Key advances in the field are reported and analyzed by international experts, providing an authoritative but accessible forum for this ever-expanding area of research. It is an interdisciplinary forum for all scientists working in the field today.
期刊最新文献
Trends and perspectives in tuberculosis and HIV co-infection studies over the past three decades Human RSVA-ON1, the only genotype present during 2019–2020 winter season in Riyadh, Saudi Arabia: a retrospective study Rosmarinic acid inhibits Rift Valley fever virus: in vitro, computational and analytical studies Plain language summary of the efficacy and safety of bepirovirsen in patients with chronic hepatitis B infection Expression and significance of IL-17A and IL-22 in children with infectious mononucleosis complicated with liver damage
×
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
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 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 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1