Inherent symmetry and flexibility in hepatitis B virus subviral particles

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

Inherent symmetry and flexibility in hepatitis B virus subviral particles

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

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English (US)
Pages (from-to)	1217-1224
Number of pages	8
Journal	Science (New York, N.Y.)
Volume	385
Issue number	6714
DOIs	https://doi.org/10.1126/science.adp1453
State	Published - Sep 13 2024
Externally published	Yes

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title = "Inherent symmetry and flexibility in hepatitis B virus subviral particles",

abstract = "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.",

author = "Quan Wang and Tao Wang and Lin Cao and An Mu and Sheng Fu and Peipei Wang and Yan Gao and Wenxin Ji and Zhenyu Liu and Zhanqiang Du and Guddat, {Luke W.} and Wenchi Zhang and Shuang Li and Xuemei Li and Zhiyong Lou and Xiangxi Wang and Zhongyu Hu and Zihe Rao",

year = "2024",

month = sep,

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doi = "10.1126/science.adp1453",

language = "English (US)",

volume = "385",

pages = "1217--1224",

journal = "Science (New York, N.Y.)",

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TY - JOUR

T1 - Inherent symmetry and flexibility in hepatitis B virus subviral particles

AU - Wang, Quan

AU - Wang, Tao

AU - Cao, Lin

AU - Mu, An

AU - Fu, Sheng

AU - Wang, Peipei

AU - Gao, Yan

AU - Ji, Wenxin

AU - Liu, Zhenyu

AU - Du, Zhanqiang

AU - Guddat, Luke W.

AU - Zhang, Wenchi

AU - Li, Shuang

AU - Li, Xuemei

AU - Lou, Zhiyong

AU - Wang, Xiangxi

AU - Hu, Zhongyu

AU - Rao, Zihe

PY - 2024/9/13

Y1 - 2024/9/13

N2 - 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.

AB - 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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DO - 10.1126/science.adp1453

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AN - SCOPUS:85204044503

SN - 0036-8075

VL - 385

SP - 1217

EP - 1224

JO - Science (New York, N.Y.)

JF - Science (New York, N.Y.)

IS - 6714

ER -

Inherent symmetry and flexibility in hepatitis B virus subviral particles

Abstract

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