Inherent symmetry and flexibility in hepatitis B virus subviral particles-Reference-Cited by-同舟云学术

Inherent symmetry and flexibility in hepatitis B virus subviral particles

Published:2024-09-13 Issue:6714 Volume:385 Page:1217-1224
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Wang Quan¹²³^ORCID,Wang Tao⁴^ORCID,Cao Lin⁵^ORCID,Mu An⁶⁷^ORCID,Fu Sheng⁶^ORCID,Wang Peipei¹^ORCID,Gao Yan¹^ORCID,Ji Wenxin³^ORCID,Liu Zhenyu⁴,Du Zhanqiang⁵,Guddat Luke W.⁸^ORCID,Zhang Wenchi⁶,Li Shuang⁶,Li Xuemei⁶,Lou Zhiyong⁴^ORCID,Wang Xiangxi⁶^ORCID,Hu Zhongyu⁹^ORCID,Rao Zihe¹⁴⁵⁶^ORCID

Affiliation:

1. Shanghai Institute for Advanced Immunochemical Studies and School of Life Science and Technology, ShanghaiTech University, Shanghai, China.

2. Shanghai Clinical Research and Trial Center, Shanghai, China.

3. National Facility for Protein Science, Shanghai Advanced Research Institute, Chinese Academy of Sciences (CAS), Shanghai, China.

4. Laboratory of Structural Biology, Tsinghua University, Beijing, China.

5. State Key Laboratory of Medicinal Chemical Biology, Frontiers Science Center for Cell Response, College of Life Sciences, and State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin, China.

6. National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, CAS, Beijing, China.

7. University of Chinese Academy of Sciences, Beijing, China.

8. School of Chemistry and Molecular Biosciences, the University of Queensland, Brisbane, Australia.

9. National Institutes for Food and Drug Control, Beijing, China.

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 D 2 - and D 4 -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.

Publisher

American Association for the Advancement of Science (AAAS)

Link

https://www.science.org/doi/pdf/10.1126/science.adp1453

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