Zhiyuan Gong , Hailun Li , Meichen Qian , Yujie Bai , Hongli Jin , Jingxuan Sun , Mengyao Zhang , Cuicui Jiao , Pei Huang , Yuanyuan Li , Haili Zhang , Hualei Wang
{"title":"Incorporation of Escherichia coli heat-labile enterotoxin B subunit into rabies virus particles enhances its immunogenicity in mice and dogs","authors":"Zhiyuan Gong , Hailun Li , Meichen Qian , Yujie Bai , Hongli Jin , Jingxuan Sun , Mengyao Zhang , Cuicui Jiao , Pei Huang , Yuanyuan Li , Haili Zhang , Hualei Wang","doi":"10.1016/j.bsheal.2023.05.005","DOIUrl":null,"url":null,"abstract":"<div><p>Although inactivated vaccines against rabies have the advantage of high safety, effective protection against rabies virus (RABV) infection often requires multiple, high-dose immunization. Incorporating a molecular adjuvant into the viral particles has been found to be a useful strategy to promote the immune effectiveness of inactivated vaccines. In this study, we constructed a recombinant virus, rCVS11-LTB, which chimerically expresses a molecular adjuvant heat-labile enterotoxin B subunit (LTB) protein on the surface of the RABV particles. Immunogenicity <em>in vivo</em> was found to be promoted by rCVS11-LTB through the activation of dendritic cells (DCs). Our results demonstrated that inactivated rCVS11-LTB was able to induce higher levels of virus-neutralizing antibodies (VNAs) in both mice and dogs than the parent virus rCVS11, to enhance the cellular immune response and T cell immune memory in mice, and was also able to provide 100% protection in mice from lethal doses of rabies virus, indicating its potential as a safe and effective inactivated rabies vaccine candidate.</p></div>","PeriodicalId":36178,"journal":{"name":"Biosafety and Health","volume":"5 5","pages":"Pages 308-319"},"PeriodicalIF":3.5000,"publicationDate":"2023-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biosafety and Health","FirstCategoryId":"3","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2590053623000551","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"PUBLIC, ENVIRONMENTAL & OCCUPATIONAL HEALTH","Score":null,"Total":0}
引用次数: 0
Abstract
Although inactivated vaccines against rabies have the advantage of high safety, effective protection against rabies virus (RABV) infection often requires multiple, high-dose immunization. Incorporating a molecular adjuvant into the viral particles has been found to be a useful strategy to promote the immune effectiveness of inactivated vaccines. In this study, we constructed a recombinant virus, rCVS11-LTB, which chimerically expresses a molecular adjuvant heat-labile enterotoxin B subunit (LTB) protein on the surface of the RABV particles. Immunogenicity in vivo was found to be promoted by rCVS11-LTB through the activation of dendritic cells (DCs). Our results demonstrated that inactivated rCVS11-LTB was able to induce higher levels of virus-neutralizing antibodies (VNAs) in both mice and dogs than the parent virus rCVS11, to enhance the cellular immune response and T cell immune memory in mice, and was also able to provide 100% protection in mice from lethal doses of rabies virus, indicating its potential as a safe and effective inactivated rabies vaccine candidate.