{"title":"小型 HBV 表面抗原的结构揭示了二聚体的形成机制","authors":"Xiao He, Yunlu Kang, Weiyu Tao, Jiaxuan Xu, Xiaoyu Liu, Lei Chen","doi":"10.1101/2024.09.13.612767","DOIUrl":null,"url":null,"abstract":"Hepatitis B surface antigen (HBsAg), the only membrane protein on the HBV viral envelope, plays essential roles in HBV assembly, viral release, host cell attachment, and entry. It is also the target of neutralizing antibodies. Despite its functional and therapeutic importance, the detailed structure of HBsAg has remained enigmatic. Here, we present the core structure of HBsAg at 3.6 A resolution, determined using recombinant small spherical subviral particles (SVPs). The structure reveals how two HBsAg monomers interact to form a dimer, which is the basic building block of SVPs.","PeriodicalId":501048,"journal":{"name":"bioRxiv - Biophysics","volume":"117 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2024-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Structure of small HBV surface antigen reveals mechanism of dimer formation\",\"authors\":\"Xiao He, Yunlu Kang, Weiyu Tao, Jiaxuan Xu, Xiaoyu Liu, Lei Chen\",\"doi\":\"10.1101/2024.09.13.612767\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Hepatitis B surface antigen (HBsAg), the only membrane protein on the HBV viral envelope, plays essential roles in HBV assembly, viral release, host cell attachment, and entry. It is also the target of neutralizing antibodies. Despite its functional and therapeutic importance, the detailed structure of HBsAg has remained enigmatic. Here, we present the core structure of HBsAg at 3.6 A resolution, determined using recombinant small spherical subviral particles (SVPs). The structure reveals how two HBsAg monomers interact to form a dimer, which is the basic building block of SVPs.\",\"PeriodicalId\":501048,\"journal\":{\"name\":\"bioRxiv - Biophysics\",\"volume\":\"117 1\",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2024-09-15\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"bioRxiv - Biophysics\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1101/2024.09.13.612767\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"bioRxiv - Biophysics","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1101/2024.09.13.612767","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Structure of small HBV surface antigen reveals mechanism of dimer formation
Hepatitis B surface antigen (HBsAg), the only membrane protein on the HBV viral envelope, plays essential roles in HBV assembly, viral release, host cell attachment, and entry. It is also the target of neutralizing antibodies. Despite its functional and therapeutic importance, the detailed structure of HBsAg has remained enigmatic. Here, we present the core structure of HBsAg at 3.6 A resolution, determined using recombinant small spherical subviral particles (SVPs). The structure reveals how two HBsAg monomers interact to form a dimer, which is the basic building block of SVPs.
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