Computational identification of monkeypox virus epitopes to generate a novel vaccine antigen against Mpox

IF 16.4 1区化学 Q1 CHEMISTRY, MULTIDISCIPLINARY

Accounts of Chemical Research Pub Date : 2024-11-01 DOI:10.1016/j.biologicals.2024.101798

Özge Dülek , Gizem Mutlu , Ecem Su Koçkaya , Hüseyin Can , Muhammet Karakavuk , Aysu Değirmenci Döşkaya , Adnan Yüksel Gürüz , Mert Döşkaya , Cemal Ün

{"title":"Computational identification of monkeypox virus epitopes to generate a novel vaccine antigen against Mpox","authors":"Özge Dülek , Gizem Mutlu , Ecem Su Koçkaya , Hüseyin Can , Muhammet Karakavuk , Aysu Değirmenci Döşkaya , Adnan Yüksel Gürüz , Mert Döşkaya , Cemal Ün","doi":"10.1016/j.biologicals.2024.101798","DOIUrl":null,"url":null,"abstract":"<div><div>Monkeypox virus (MPXV) belonging to poxviridae family causes chronic viral disease in various mammals including human and monkeys. Conventional vaccines developed against smallpox of poxviridae, are not specific against Mpox. Also, they can cause various side effects after vaccination. In this study, we aimed to analyze the A17L, A28L, A37R, A43R, E8L, H3L, B6R, and M1R structural proteins of MPXV and identify epitopes in them which can be used to generate vaccine antigens. Among the proteins analyzed, the M1R protein was predicted to be more appropriate for use in vaccine research due to its high antigenicity value and other physicochemical features. Also, A17L, B6R and E8L had high antigenicity values. E8L protein was more conserved while the A37R, A43R, and B6R proteins had signal peptides. Although a total of eight B cell epitopes were predicted in all proteins analyzed, CNGETK epitope belonging to B6R protein had the highest antigenicity value (1.7083), as well as was non-allergenic, non-toxic, and soluble. Based on T cell epitope analyses performed on all proteins, fourteen MHC-I/II epitopes were predicted that are antigenic, non-allergenic and non-toxic, as well as soluble. Among them, MHC-I related-HEIYDRNVGF epitope in A28L protein had the highest antigenicity value (1.6650) and MHC-II related-IGNIKIVQIDIRDIK epitope in A37R protein had the highest antigenicity value (2.0280). In conclusion, eight structural proteins of MPXV were successfully analyzed and 22 important epitopes were identified that could serve as vaccine antigens or in serological studies to develop diagnostic tools.</div></div>","PeriodicalId":1,"journal":{"name":"Accounts of Chemical Research","volume":null,"pages":null},"PeriodicalIF":16.4000,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Accounts of Chemical Research","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1045105624000551","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}

引用次数: 0

Abstract

Monkeypox virus (MPXV) belonging to poxviridae family causes chronic viral disease in various mammals including human and monkeys. Conventional vaccines developed against smallpox of poxviridae, are not specific against Mpox. Also, they can cause various side effects after vaccination. In this study, we aimed to analyze the A17L, A28L, A37R, A43R, E8L, H3L, B6R, and M1R structural proteins of MPXV and identify epitopes in them which can be used to generate vaccine antigens. Among the proteins analyzed, the M1R protein was predicted to be more appropriate for use in vaccine research due to its high antigenicity value and other physicochemical features. Also, A17L, B6R and E8L had high antigenicity values. E8L protein was more conserved while the A37R, A43R, and B6R proteins had signal peptides. Although a total of eight B cell epitopes were predicted in all proteins analyzed, CNGETK epitope belonging to B6R protein had the highest antigenicity value (1.7083), as well as was non-allergenic, non-toxic, and soluble. Based on T cell epitope analyses performed on all proteins, fourteen MHC-I/II epitopes were predicted that are antigenic, non-allergenic and non-toxic, as well as soluble. Among them, MHC-I related-HEIYDRNVGF epitope in A28L protein had the highest antigenicity value (1.6650) and MHC-II related-IGNIKIVQIDIRDIK epitope in A37R protein had the highest antigenicity value (2.0280). In conclusion, eight structural proteins of MPXV were successfully analyzed and 22 important epitopes were identified that could serve as vaccine antigens or in serological studies to develop diagnostic tools.

查看原文本刊更多论文

通过计算识别猴痘病毒表位，生成新型猴痘疫苗抗原。

猴痘病毒（MPXV）属于痘病毒科，会导致包括人类和猴子在内的多种哺乳动物患上慢性病毒性疾病。针对痘病毒科天花研制的传统疫苗对猴痘病毒没有特异性。此外，疫苗接种后还会产生各种副作用。在这项研究中，我们旨在分析 MPXV 的 A17L、A28L、A37R、A43R、E8L、H3L、B6R 和 M1R 结构蛋白，并确定其中可用于生成疫苗抗原的表位。在分析的蛋白质中，由于 M1R 蛋白具有较高的抗原性值和其他理化特征，因此被认为更适合用于疫苗研究。此外，A17L、B6R 和 E8L 的抗原性值也很高。E8L 蛋白的保守性较高，而 A37R、A43R 和 B6R 蛋白则具有信号肽。虽然在所有分析的蛋白质中总共预测出了 8 个 B 细胞表位，但属于 B6R 蛋白的 CNGETK 表位的抗原性值（1.7083）最高，而且无过敏性、无毒性和可溶性。根据对所有蛋白质进行的 T 细胞表位分析，预测出 14 个具有抗原性、非致敏性、无毒性和可溶性的 MHC-I/II 表位。其中，A28L 蛋白中与 MHC-I 相关的-HEIYDRNVGF 表位的抗原性值最高（1.6650），A37R 蛋白中与 MHC-II 相关的-IGNIKIVQIDIRDIK 表位的抗原性值最高（2.0280）。总之，我们成功地分析了 MPXV 的 8 种结构蛋白，并确定了 22 个重要表位，这些表位可作为疫苗抗原或用于血清学研究以开发诊断工具。

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

Accounts of Chemical Research 化学-化学综合

CiteScore

31.40

自引率

1.10%

发文量

312

审稿时长

2 months

期刊介绍： Accounts of Chemical Research presents short, concise and critical articles offering easy-to-read overviews of basic research and applications in all areas of chemistry and biochemistry. These short reviews focus on research from the author’s own laboratory and are designed to teach the reader about a research project. In addition, Accounts of Chemical Research publishes commentaries that give an informed opinion on a current research problem. Special Issues online are devoted to a single topic of unusual activity and significance. Accounts of Chemical Research replaces the traditional article abstract with an article "Conspectus." These entries synopsize the research affording the reader a closer look at the content and significance of an article. Through this provision of a more detailed description of the article contents, the Conspectus enhances the article's discoverability by search engines and the exposure for the research.