AI Article Synopsis
- - Chronic hepatitis B virus (HBV) infection is a significant global health issue, leading to high rates of illness and death, even with an available vaccine.
- - Current treatments only partially clear the virus, requiring patients to manage the infection for life, making the study of HBV's structure and behavior crucial.
- - Researchers used advanced cryo-electron microscopy to analyze the HBV surface antigen (HBsAg) at near-atomic resolution, revealing how HBsAg forms complex structures that contribute to viral assembly and function.
Article 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 - and -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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| http://dx.doi.org/10.1126/science.adp1453 | DOI Listing |
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