National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
米国
引用
ジャーナル: Sci Adv / 年: 2022 タイトル: Cryo-EM structures of human hepatitis B and woodchuck hepatitis virus small spherical subviral particles. 著者: Haitao Liu / Xupeng Hong / Ji Xi / Stephan Menne / Jianming Hu / Joseph Che-Yen Wang / 要旨: 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 ...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.
履歴
登録
2022年2月2日
登録サイト: RCSB / 処理サイト: RCSB
改定 1.0
2022年8月24日
Provider: repository / タイプ: Initial release
改定 1.1
2024年2月21日
Group: Data collection / カテゴリ: chem_comp_atom / chem_comp_bond
平均露光時間: 3 sec. / 電子線照射量: 30 e/Å2 / フィルム・検出器のモデル: GATAN K3 (6k x 4k) / 撮影したグリッド数: 1
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解析
CTF補正
タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION
3次元再構成
解像度: 6.3 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 36166 / 対称性のタイプ: POINT
原子モデル構築
詳細: The authors state that the model was built using 6.5 A cryo-EM map and Alphafold2, so the clashes cannot be totally resolved due to the lack of density from cryo-EM maps.