利用硅蛋白模型预测SARS-CoV-2 XBB.1.5中和抗体活性的变化

IF 2 Q4 VIROLOGY
Colby T. Ford, Shirish Yasa, Denis Jacob Machado, Richard Allen White, Daniel A. Janies
{"title":"利用硅蛋白模型预测SARS-CoV-2 XBB.1.5中和抗体活性的变化","authors":"Colby T. Ford, Shirish Yasa, Denis Jacob Machado, Richard Allen White, Daniel A. Janies","doi":"10.3389/fviro.2023.1172027","DOIUrl":null,"url":null,"abstract":"The SARS-CoV-2 variant XBB.1.5 is of concern as it has high transmissibility. XBB.1.5 currently accounts for upwards of 30% of new infections in the United States. One year after our group published the predicted structure of the Omicron (B.1.1.529) variant’s receptor binding domain (RBD) and antibody binding affinity, we return to investigate the new mutations seen in XBB.1.5 which is a descendant of Omicron. Using in silico modeling approaches against newer neutralizing antibodies that are shown effective against B.1.1.529, we predict the immune consequences of XBB.1.5’s mutations and show that there is no statistically significant difference in overall antibody evasion when comparing to the B.1.1.529 and other related variants (e.g., BJ.1 andBM.1.1.1). However, noticeable changes in antibody binding affinity were seen due to specific amino acid changes of interest in the newer variants.","PeriodicalId":73114,"journal":{"name":"Frontiers in virology","volume":"17 1","pages":"0"},"PeriodicalIF":2.0000,"publicationDate":"2023-04-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Predicting changes in neutralizing antibody activity for SARS-CoV-2 XBB.1.5 using in silico protein modeling\",\"authors\":\"Colby T. Ford, Shirish Yasa, Denis Jacob Machado, Richard Allen White, Daniel A. Janies\",\"doi\":\"10.3389/fviro.2023.1172027\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The SARS-CoV-2 variant XBB.1.5 is of concern as it has high transmissibility. XBB.1.5 currently accounts for upwards of 30% of new infections in the United States. One year after our group published the predicted structure of the Omicron (B.1.1.529) variant’s receptor binding domain (RBD) and antibody binding affinity, we return to investigate the new mutations seen in XBB.1.5 which is a descendant of Omicron. Using in silico modeling approaches against newer neutralizing antibodies that are shown effective against B.1.1.529, we predict the immune consequences of XBB.1.5’s mutations and show that there is no statistically significant difference in overall antibody evasion when comparing to the B.1.1.529 and other related variants (e.g., BJ.1 andBM.1.1.1). However, noticeable changes in antibody binding affinity were seen due to specific amino acid changes of interest in the newer variants.\",\"PeriodicalId\":73114,\"journal\":{\"name\":\"Frontiers in virology\",\"volume\":\"17 1\",\"pages\":\"0\"},\"PeriodicalIF\":2.0000,\"publicationDate\":\"2023-04-26\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Frontiers in virology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.3389/fviro.2023.1172027\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"VIROLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Frontiers in virology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3389/fviro.2023.1172027","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"VIROLOGY","Score":null,"Total":0}
引用次数: 0

摘要

SARS-CoV-2变体XBB.1.5具有高传播性,值得关注。XBB.1.5目前占美国新感染病例的30%以上。在我们小组发表了预测的Omicron (B.1.1.529)变体的受体结合域(RBD)结构和抗体结合亲和力一年后,我们回到研究在Omicron的后代XBB.1.5中发现的新突变。使用针对新的中和抗体的计算机建模方法,对B.1.1.529有效,我们预测了XBB.1.5突变的免疫后果,并表明与B.1.1.529和其他相关变体(例如,BJ.1和bm .1.1.1)相比,总体抗体逃避没有统计学上的显著差异。然而,抗体结合亲和力的显著变化是由于新变异中感兴趣的特定氨基酸的变化。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Predicting changes in neutralizing antibody activity for SARS-CoV-2 XBB.1.5 using in silico protein modeling
The SARS-CoV-2 variant XBB.1.5 is of concern as it has high transmissibility. XBB.1.5 currently accounts for upwards of 30% of new infections in the United States. One year after our group published the predicted structure of the Omicron (B.1.1.529) variant’s receptor binding domain (RBD) and antibody binding affinity, we return to investigate the new mutations seen in XBB.1.5 which is a descendant of Omicron. Using in silico modeling approaches against newer neutralizing antibodies that are shown effective against B.1.1.529, we predict the immune consequences of XBB.1.5’s mutations and show that there is no statistically significant difference in overall antibody evasion when comparing to the B.1.1.529 and other related variants (e.g., BJ.1 andBM.1.1.1). However, noticeable changes in antibody binding affinity were seen due to specific amino acid changes of interest in the newer variants.
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
自引率
0.00%
发文量
0
×
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