Gege Zhang , Qi Peng , Shiyu Liu , Baochao Fan , Chuanhong Wang , Xu Song , Qiuxia Cao , Chengcheng Li , Hong Xu , Hongting Lu , Meiying Bao , Shanshan Yang , Yunchuan Li , Jiaxiang Wang , Bin Li
{"title":"穗状病毒蛋白 RBD 中的糖基化位点可降低 PEDV AH2012/12 的免疫原性","authors":"Gege Zhang , Qi Peng , Shiyu Liu , Baochao Fan , Chuanhong Wang , Xu Song , Qiuxia Cao , Chengcheng Li , Hong Xu , Hongting Lu , Meiying Bao , Shanshan Yang , Yunchuan Li , Jiaxiang Wang , Bin Li","doi":"10.1016/j.virusres.2024.199381","DOIUrl":null,"url":null,"abstract":"<div><p>Porcine epidemic diarrhea (PED) is a highly contagious swine intestinal disease caused by PED virus (PEDV). Vaccination is a promising strategy to prevent and control PED. Previous studies have confirmed that glycosylation could regulate the immunogenicity of viral antigens. In this study, we constructed three recombinant PEDVs which removed the glycosylation sites in RBD. Viral infection assays revealed that similar replication characteristics between the recombinant viruses and parental PEDV. Although animal challenging study demonstrated that the glycosylation sites in RBD do not affect the pathogenicity of PEDV, we found that removing the glycosylation sites on the RBD regions could promote the IgG and neutralization titer <em>in vivo</em>, suggesting deglycosylation in RBD could enhance the immunogenicity of PEDV. These findings demonstrated that removal of the glycosylation sites in RBD is a promising method to develop PEDV vaccines.</p></div>","PeriodicalId":23483,"journal":{"name":"Virus research","volume":null,"pages":null},"PeriodicalIF":2.5000,"publicationDate":"2024-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S0168170224000741/pdfft?md5=3bd0414b966b07c43e55793e98da314a&pid=1-s2.0-S0168170224000741-main.pdf","citationCount":"0","resultStr":"{\"title\":\"The glycosylation sites in RBD of spike protein attenuate the immunogenicity of PEDV AH2012/12\",\"authors\":\"Gege Zhang , Qi Peng , Shiyu Liu , Baochao Fan , Chuanhong Wang , Xu Song , Qiuxia Cao , Chengcheng Li , Hong Xu , Hongting Lu , Meiying Bao , Shanshan Yang , Yunchuan Li , Jiaxiang Wang , Bin Li\",\"doi\":\"10.1016/j.virusres.2024.199381\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Porcine epidemic diarrhea (PED) is a highly contagious swine intestinal disease caused by PED virus (PEDV). Vaccination is a promising strategy to prevent and control PED. Previous studies have confirmed that glycosylation could regulate the immunogenicity of viral antigens. In this study, we constructed three recombinant PEDVs which removed the glycosylation sites in RBD. Viral infection assays revealed that similar replication characteristics between the recombinant viruses and parental PEDV. Although animal challenging study demonstrated that the glycosylation sites in RBD do not affect the pathogenicity of PEDV, we found that removing the glycosylation sites on the RBD regions could promote the IgG and neutralization titer <em>in vivo</em>, suggesting deglycosylation in RBD could enhance the immunogenicity of PEDV. These findings demonstrated that removal of the glycosylation sites in RBD is a promising method to develop PEDV vaccines.</p></div>\",\"PeriodicalId\":23483,\"journal\":{\"name\":\"Virus research\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":2.5000,\"publicationDate\":\"2024-05-02\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.sciencedirect.com/science/article/pii/S0168170224000741/pdfft?md5=3bd0414b966b07c43e55793e98da314a&pid=1-s2.0-S0168170224000741-main.pdf\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Virus research\",\"FirstCategoryId\":\"3\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0168170224000741\",\"RegionNum\":4,\"RegionCategory\":\"医学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"VIROLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Virus research","FirstCategoryId":"3","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0168170224000741","RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"VIROLOGY","Score":null,"Total":0}
The glycosylation sites in RBD of spike protein attenuate the immunogenicity of PEDV AH2012/12
Porcine epidemic diarrhea (PED) is a highly contagious swine intestinal disease caused by PED virus (PEDV). Vaccination is a promising strategy to prevent and control PED. Previous studies have confirmed that glycosylation could regulate the immunogenicity of viral antigens. In this study, we constructed three recombinant PEDVs which removed the glycosylation sites in RBD. Viral infection assays revealed that similar replication characteristics between the recombinant viruses and parental PEDV. Although animal challenging study demonstrated that the glycosylation sites in RBD do not affect the pathogenicity of PEDV, we found that removing the glycosylation sites on the RBD regions could promote the IgG and neutralization titer in vivo, suggesting deglycosylation in RBD could enhance the immunogenicity of PEDV. These findings demonstrated that removal of the glycosylation sites in RBD is a promising method to develop PEDV vaccines.
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.