The stability of PCV2 virus-like particles from mammalian cells and challenges for biotechnological applications

IF 4.5 3区 医学 Q2 IMMUNOLOGY
Natalia Olivero-Deibe , Ezequiel N. Frigini , Natalia Ramos , Federico Carrión , Florencia Fadel , Lihuén Villarreal , Juan C. Benech , Juan Arbiza , Sergio Pantano , Claudia Ortega
{"title":"The stability of PCV2 virus-like particles from mammalian cells and challenges for biotechnological applications","authors":"Natalia Olivero-Deibe ,&nbsp;Ezequiel N. Frigini ,&nbsp;Natalia Ramos ,&nbsp;Federico Carrión ,&nbsp;Florencia Fadel ,&nbsp;Lihuén Villarreal ,&nbsp;Juan C. Benech ,&nbsp;Juan Arbiza ,&nbsp;Sergio Pantano ,&nbsp;Claudia Ortega","doi":"10.1016/j.vaccine.2024.126549","DOIUrl":null,"url":null,"abstract":"<div><div>Porcine circovirus type 2 (PCV2) is a highly damaging pathogen for pig farming, causing significant economic losses. Despite the availability of vaccines based on different technologies, the virus steadily infects the world's pig population. In this context, virus-like particles (VLPs) constitute appealing alternatives for vaccine development as they lack the viral genome but present intact external surfaces.</div><div>Using PCV2 VLPs expressed and purified from Expi293F cells, we demonstrate the potential to generate high-purity VLPs with excellent antigenic properties through biochemical, biophysical, and immunological characterization. Using different techniques, we also determined the melting temperature of these VLPs at nearly 55 °C.</div><div>Furthermore, we conducted multiscale simulations of whole VLPs combined with multiple sequence analyses to provide a new perspective into the stability determinants. Computational results support our findings and underscore the importance of protein-nucleic acid interactions in stabilizing the VLP structure. Moreover, we spotted an unforeseen correlation between amino acid conservation, solvent exposure, and flexibility, revealing a link to viral assembly and immune evasion. These novel insights are crucial to guide the development of stabilized VLP for new vaccine prototypes to respond to the emergence of new PCV2 genotypes.</div></div>","PeriodicalId":23491,"journal":{"name":"Vaccine","volume":"44 ","pages":"Article 126549"},"PeriodicalIF":4.5000,"publicationDate":"2024-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Vaccine","FirstCategoryId":"3","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0264410X24012313","RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"IMMUNOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

Porcine circovirus type 2 (PCV2) is a highly damaging pathogen for pig farming, causing significant economic losses. Despite the availability of vaccines based on different technologies, the virus steadily infects the world's pig population. In this context, virus-like particles (VLPs) constitute appealing alternatives for vaccine development as they lack the viral genome but present intact external surfaces.
Using PCV2 VLPs expressed and purified from Expi293F cells, we demonstrate the potential to generate high-purity VLPs with excellent antigenic properties through biochemical, biophysical, and immunological characterization. Using different techniques, we also determined the melting temperature of these VLPs at nearly 55 °C.
Furthermore, we conducted multiscale simulations of whole VLPs combined with multiple sequence analyses to provide a new perspective into the stability determinants. Computational results support our findings and underscore the importance of protein-nucleic acid interactions in stabilizing the VLP structure. Moreover, we spotted an unforeseen correlation between amino acid conservation, solvent exposure, and flexibility, revealing a link to viral assembly and immune evasion. These novel insights are crucial to guide the development of stabilized VLP for new vaccine prototypes to respond to the emergence of new PCV2 genotypes.
求助全文
约1分钟内获得全文 求助全文
来源期刊
Vaccine
Vaccine 医学-免疫学
CiteScore
8.70
自引率
5.50%
发文量
992
审稿时长
131 days
期刊介绍: Vaccine is unique in publishing the highest quality science across all disciplines relevant to the field of vaccinology - all original article submissions across basic and clinical research, vaccine manufacturing, history, public policy, behavioral science and ethics, social sciences, safety, and many other related areas are welcomed. The submission categories as given in the Guide for Authors indicate where we receive the most papers. Papers outside these major areas are also welcome and authors are encouraged to contact us with specific questions.
×
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