7TUL

Woodchuck hepatitis small surface protein without cytosolic and antigenic loops

Summary for 7TUL

• Entry DOI: 10.2210/pdb7tul/pdb
• EMDB information: 26118
• Descriptor: Large envelope protein (1 entity in total)
• Functional Keywords: whv, svp, whsag, envelope protein, viral protein
• Biological source: Woodchuck hepatitis virus (WHV)
• Total number of polymer chains: 2
• Total formula weight: 51301.27

Authors

Liu, H.,Wang, J.C.Y. (deposition date: 2022-02-02, release date: 2022-08-24, Last modification date: 2024-02-21)

Primary citation

Liu, H.,Hong, X.,Xi, J.,Menne, S.,Hu, J.,Wang, J.C.
Cryo-EM structures of human hepatitis B and woodchuck hepatitis virus small spherical subviral particles.
Sci Adv, 8:eabo4184-eabo4184, 2022

PubMed Abstract: The loss of detectable hepatitis B surface antigen (HBsAg) is considered a functional cure in chronic hepatitis B. Naturally, HBsAg can be incorporated into the virion envelope or assembled into subviral particles (SVPs) with lipid from host cells. Until now, there has been no detailed structure of HBsAg, and the published SVP structures are controversial. Here, we report the first subnanometer-resolution structures of spherical SVP from hepatitis B virus (HBV) and the related woodchuck hepatitis virus (WHV) determined by cryo-electron microscopy in combination with AlphaFold2 prediction. Both structures showed unique rhombicuboctahedral symmetry with 24 protruding spikes comprising dimer of small HBsAg with four helical domains. The lipid moiety in the SVP is organized in a noncanonical lipid patch instead of a lipid bilayer, which can accommodate the exposed hydrophobic surface and modulate particle stability. Together, these findings advance our knowledge of viral membrane organization and the structures of HBV and WHV spherical SVPs.

PubMed: 35930632
DOI: 10.1126/sciadv.abo4184

Experimental method

ELECTRON MICROSCOPY (6.5 Å)