Suppr超能文献

设计并过量生产一种gp350/220串联表位,该表位显示出成为一种EB病毒疫苗的潜力。

Designing and overproducing a tandem epitope of gp350/220 that shows a potential to become an EBV vaccine.

作者信息

Veronica Margarecaesha Anyndita Nadya, Dluha Nurul, Rifa'i Muhaimin, Himmah Karimatul, Wahyuningsih Mulya Dwi

机构信息

Biology Department, Faculty of Mathematics and Natural Sciences, Brawijaya University, Indonesia.

Pusat Studi Biosistem, LPPM, Brawijaya University, Indonesia.

出版信息

Heliyon. 2018 Mar 7;4(3):e00564. doi: 10.1016/j.heliyon.2018.e00564. eCollection 2018 Mar.

Abstract

BACKGROUND

Epstein-Barr virus (EBV) can cause cancer in people from around the world. There is no EBV vaccine available for use on a global scale. However, emerging evidence suggests that the epitope on the gp350/220 capsid protein may be developed into an EBV vaccine. Nevertheless, the production of small, single epitope is challenging of stability issues and possible alteration of peptide structure. In this study, a tandem epitope was developed consisting of three single epitopes, aimed to improve stability, antigenicity and preserve epitope structure.

MATERIALS AND METHODS

A tandem epitope was designed using bioinformatics based on the epitope structure of the gp350/220 protein. The tandem epitope structure was analyzed using a protein folding method with Abalone software, which was further refined via YASARA force field and molecular repairing using a FoldX method. Immunogenicity was examined with Epitopia software, whereas allergen properties were tested using AlgPred. The pattern of the tandem epitope binding with anti-gp350/220 antibodies was performed using Z-dock and snugDock. The tandem epitope was then overproduced in strain BL21 as a host cell.

RESULT

Our model demonstrated a successfully designed and overproduced tandem epitope. The tandem epitope demonstrated a similar structure compared with the epitope of whole protein gp350/220. Our epitope also demonstrated non-allergen and antigenicity properties, and possessed antibody binding patterns consistent with whole protein gp350/220.

CONCLUSION AND RECOMMENDATION

These data suggest a novel tandem epitope composed of three similar epitopes demonstrates antigenicity, structure, and binding properties consistent with whole protein gp350/220. We also demonstrate successful production of the tandem epitope using strain BL21 as a host. Future experimental animal research is necessary to test the ability of this tandem epitope to stimulate antibody production.

摘要

背景

爱泼斯坦-巴尔病毒(EBV)可在世界各地的人群中引发癌症。目前尚无可在全球范围内使用的EBV疫苗。然而,新出现的证据表明,gp350/220衣壳蛋白上的表位可能被开发成一种EBV疫苗。尽管如此,生产小的单一表位面临着稳定性问题以及肽结构可能改变的挑战。在本研究中,开发了一种由三个单一表位组成的串联表位,旨在提高稳定性、抗原性并保留表位结构。

材料与方法

基于gp350/220蛋白的表位结构,利用生物信息学设计了一种串联表位。使用Abalone软件通过蛋白质折叠方法分析串联表位结构,通过YASARA力场进一步优化,并使用FoldX方法进行分子修复。使用Epitopia软件检测免疫原性,使用AlgPred测试过敏原特性。使用Z-dock和snugDock进行串联表位与抗gp350/220抗体结合模式的研究。然后在BL21菌株作为宿主细胞中过量表达该串联表位。

结果

我们的模型展示了成功设计并过量表达的串联表位。该串联表位与整个gp350/220蛋白的表位相比,结构相似。我们的表位还表现出非过敏原和抗原性特性,并且具有与整个gp350/220蛋白一致的抗体结合模式。

结论与建议

这些数据表明,由三个相似表位组成的新型串联表位具有与整个gp350/220蛋白一致的抗原性、结构和结合特性。我们还展示了以BL21菌株作为宿主成功生产串联表位。未来有必要进行实验动物研究,以测试这种串联表位刺激抗体产生的能力。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/93fc/5857718/50ea367a828f/gr1.jpg

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