Quan Wang, Tao Wang, Lin Cao, An Mu, Sheng Fu, Peipei Wang, Yan Gao, Wenxin Ji, Zhenyu Liu, Zhanqiang Du, Luke W. Guddat, Wenchi Zhang, Shuang Li, Xuemei Li, Zhiyong Lou, Xiangxi Wang, Zhongyu Hu, Zihe Rao
{"title":"乙型肝炎病毒亚病毒粒子固有的对称性和灵活性","authors":"Quan Wang, Tao Wang, Lin Cao, An Mu, Sheng Fu, Peipei Wang, Yan Gao, Wenxin Ji, Zhenyu Liu, Zhanqiang Du, Luke W. Guddat, Wenchi Zhang, Shuang Li, Xuemei Li, Zhiyong Lou, Xiangxi Wang, Zhongyu Hu, Zihe Rao","doi":"10.1126/science.adp1453","DOIUrl":null,"url":null,"abstract":"<div >Chronic hepatitis B virus (HBV) infection poses a major global health challenge with massive morbidity and mortality. Despite a preventive vaccine, current treatments provide limited virus clearance, necessitating lifelong commitment. The HBV surface antigen (HBsAg) is crucial for diagnosis and prognosis, yet its high-resolution structure and assembly on the virus envelope remain elusive. Utilizing extensive datasets and advanced cryo–electron microscopy analysis, we present structural insights into HBsAg at a near-atomic resolution of 3.7 angstroms. HBsAg homodimers assemble into subviral particles with <b><i>D</i></b><sub>2</sub>- and <b><i>D</i></b><sub>4</sub>-like quasisymmetry, elucidating the dense-packing rules and structural adaptability of HBsAg. These findings provide insights into how HBsAg assembles into higher-order filaments and interacts with the capsid to form virions.</div>","PeriodicalId":21678,"journal":{"name":"Science","volume":null,"pages":null},"PeriodicalIF":44.7000,"publicationDate":"2024-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Inherent symmetry and flexibility in hepatitis B virus subviral particles\",\"authors\":\"Quan Wang, Tao Wang, Lin Cao, An Mu, Sheng Fu, Peipei Wang, Yan Gao, Wenxin Ji, Zhenyu Liu, Zhanqiang Du, Luke W. Guddat, Wenchi Zhang, Shuang Li, Xuemei Li, Zhiyong Lou, Xiangxi Wang, Zhongyu Hu, Zihe Rao\",\"doi\":\"10.1126/science.adp1453\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div >Chronic hepatitis B virus (HBV) infection poses a major global health challenge with massive morbidity and mortality. Despite a preventive vaccine, current treatments provide limited virus clearance, necessitating lifelong commitment. The HBV surface antigen (HBsAg) is crucial for diagnosis and prognosis, yet its high-resolution structure and assembly on the virus envelope remain elusive. Utilizing extensive datasets and advanced cryo–electron microscopy analysis, we present structural insights into HBsAg at a near-atomic resolution of 3.7 angstroms. HBsAg homodimers assemble into subviral particles with <b><i>D</i></b><sub>2</sub>- and <b><i>D</i></b><sub>4</sub>-like quasisymmetry, elucidating the dense-packing rules and structural adaptability of HBsAg. These findings provide insights into how HBsAg assembles into higher-order filaments and interacts with the capsid to form virions.</div>\",\"PeriodicalId\":21678,\"journal\":{\"name\":\"Science\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":44.7000,\"publicationDate\":\"2024-09-12\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Science\",\"FirstCategoryId\":\"103\",\"ListUrlMain\":\"https://www.science.org/doi/10.1126/science.adp1453\",\"RegionNum\":1,\"RegionCategory\":\"综合性期刊\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"MULTIDISCIPLINARY SCIENCES\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Science","FirstCategoryId":"103","ListUrlMain":"https://www.science.org/doi/10.1126/science.adp1453","RegionNum":1,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"MULTIDISCIPLINARY SCIENCES","Score":null,"Total":0}
Inherent symmetry and flexibility in hepatitis B virus subviral particles
Chronic hepatitis B virus (HBV) infection poses a major global health challenge with massive morbidity and mortality. Despite a preventive vaccine, current treatments provide limited virus clearance, necessitating lifelong commitment. The HBV surface antigen (HBsAg) is crucial for diagnosis and prognosis, yet its high-resolution structure and assembly on the virus envelope remain elusive. Utilizing extensive datasets and advanced cryo–electron microscopy analysis, we present structural insights into HBsAg at a near-atomic resolution of 3.7 angstroms. HBsAg homodimers assemble into subviral particles with D2- and D4-like quasisymmetry, elucidating the dense-packing rules and structural adaptability of HBsAg. These findings provide insights into how HBsAg assembles into higher-order filaments and interacts with the capsid to form virions.
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Science is a leading outlet for scientific news, commentary, and cutting-edge research. Through its print and online incarnations, Science reaches an estimated worldwide readership of more than one million. Science’s authorship is global too, and its articles consistently rank among the world's most cited research.
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Science seeks to publish those papers that are most influential in their fields or across fields and that will significantly advance scientific understanding. Selected papers should present novel and broadly important data, syntheses, or concepts. They should merit recognition by the wider scientific community and general public provided by publication in Science, beyond that provided by specialty journals. Science welcomes submissions from all fields of science and from any source. The editors are committed to the prompt evaluation and publication of submitted papers while upholding high standards that support reproducibility of published research. Science is published weekly; selected papers are published online ahead of print.
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