{"title":"Screening and identification of linear B-cell epitopes on structural proteins of African Swine Fever Virus","authors":"Haiyan Lu, Junjun Shao, Wei Liu, Shandian Gao, Guangqing Zhou, Xiaoyu Ning, Haiyan Huang, Yijia Liu, Huiyun Chang","doi":"10.1016/j.virusres.2024.199465","DOIUrl":null,"url":null,"abstract":"<div><div>This study aims to screen and identify linear B-cell epitopes on the structural proteins of African Swine Fever Virus (ASFV) to assist in the development of peptide-based vaccines. In experiments, 66 peptides of 12 structural proteins of ASFV were predicted as potential linear B-cell epitopes using bioinformatics tools and were designed; the potential epitope proteins carried the GST tag were expressed, purified, and subjected to antigenicity analysis with porcine antiserum against ASFV, and further identified based on their immunogenicity in mice. A total of 22 potential linear B-cell epitopes showed immunoreactivity and immunogenicity. Of these epitopes, 13 epitopes were firstly identified including 4 epitopes located in p72 (352–363, 416–434, 424–439, 496–530 aa), 3 epitopes located in pE248R (121–136, 138–169, 158–185 aa), and only one epitope of each protein of pH108R (33–46 aa), p17 (63–86 aa), pE120R (65–117 aa), pE199L (175–189 aa), p12 (36–56 aa) as well as pB438L (211–230 aa). Notably, the immunoreactivity of the epitopes from the 63-86 aa of p17 and the 65–117 aa of pE120R were the highest amongst identified epitopes, while the immunogenicity of epitopes from the 36–56 aa of p12, the 211–230 aa of pB438L, the 352–363 aa of p72 and the 63–86 aa of p17 were the best strong. The other 9 epitopes are partly overlapped with previous researches. These epitopes identified here will further enrich the database of ASFV epitope, as well as help to develop safe, effective epitope-based ASF vaccines and ASF diagnostic reagents.</div></div>","PeriodicalId":23483,"journal":{"name":"Virus research","volume":null,"pages":null},"PeriodicalIF":2.5000,"publicationDate":"2024-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Virus research","FirstCategoryId":"3","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0168170224001588","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: 0
Abstract
This study aims to screen and identify linear B-cell epitopes on the structural proteins of African Swine Fever Virus (ASFV) to assist in the development of peptide-based vaccines. In experiments, 66 peptides of 12 structural proteins of ASFV were predicted as potential linear B-cell epitopes using bioinformatics tools and were designed; the potential epitope proteins carried the GST tag were expressed, purified, and subjected to antigenicity analysis with porcine antiserum against ASFV, and further identified based on their immunogenicity in mice. A total of 22 potential linear B-cell epitopes showed immunoreactivity and immunogenicity. Of these epitopes, 13 epitopes were firstly identified including 4 epitopes located in p72 (352–363, 416–434, 424–439, 496–530 aa), 3 epitopes located in pE248R (121–136, 138–169, 158–185 aa), and only one epitope of each protein of pH108R (33–46 aa), p17 (63–86 aa), pE120R (65–117 aa), pE199L (175–189 aa), p12 (36–56 aa) as well as pB438L (211–230 aa). Notably, the immunoreactivity of the epitopes from the 63-86 aa of p17 and the 65–117 aa of pE120R were the highest amongst identified epitopes, while the immunogenicity of epitopes from the 36–56 aa of p12, the 211–230 aa of pB438L, the 352–363 aa of p72 and the 63–86 aa of p17 were the best strong. The other 9 epitopes are partly overlapped with previous researches. These epitopes identified here will further enrich the database of ASFV epitope, as well as help to develop safe, effective epitope-based ASF vaccines and ASF diagnostic reagents.
期刊介绍:
Virus Research provides a means of fast publication for original papers on fundamental research in virology. Contributions on new developments concerning virus structure, replication, pathogenesis and evolution are encouraged. These include reports describing virus morphology, the function and antigenic analysis of virus structural components, virus genome structure and expression, analysis on virus replication processes, virus evolution in connection with antiviral interventions, effects of viruses on their host cells, particularly on the immune system, and the pathogenesis of virus infections, including oncogene activation and transduction.