8YMJ

Cryo-EM structure of Hepatitis B virus surface antigen subviral particle with D2 symmetry

This is a non-PDB format compatible entry.

Summary for 8YMJ

• Entry DOI: 10.2210/pdb8ymj/pdb
• EMDB information: 39395
• Descriptor: Isoform S of Large envelope protein (1 entity in total)
• Functional Keywords: surface antigen, subviral particle, virus like particle
• Biological source: Hepatitis B virus ayw/China/Tibet127/2002
• Total number of polymer chains: 80
• Total formula weight: 2032644.72

Authors

Wang, T.,Cao, L.,Mu, A.,Wang, Q.,Rao, Z.H. (deposition date: 2024-03-09, release date: 2024-09-18, Last modification date: 2024-10-09)

Primary citation

Wang, Q.,Wang, T.,Cao, L.,Mu, A.,Fu, S.,Wang, P.,Gao, Y.,Ji, W.,Liu, Z.,Du, Z.,Guddat, L.W.,Zhang, W.,Li, S.,Li, X.,Lou, Z.,Wang, X.,Hu, Z.,Rao, Z.
Inherent symmetry and flexibility in hepatitis B virus subviral particles.
Science, 385:1217-1224, 2024

PubMed 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.

PubMed: 39264996
DOI: 10.1126/science.adp1453

Experimental method

ELECTRON MICROSCOPY (6.6 Å)