- EMDB-39395: Cryo-EM structure of Hepatitis B virus surface antigen subviral p... -
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基本情報
登録情報
データベース: EMDB / ID: EMD-39395
タイトル
Cryo-EM structure of Hepatitis B virus surface antigen subviral particle with D2 symmetry
マップデータ
試料
ウイルス: Hepatitis B virus ayw/China/Tibet127/2002 (ウイルス)
タンパク質・ペプチド: Isoform S of Large envelope protein
キーワード
Surface antigen / Subviral particle / VIRUS LIKE PARTICLE
機能・相同性
Large envelope protein S / Major surface antigen from hepadnavirus / caveolin-mediated endocytosis of virus by host cell / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / virion membrane / membrane / Large envelope protein
National Natural Science Foundation of China (NSFC)
81520108019
中国
National Natural Science Foundation of China (NSFC)
813300237
中国
National Natural Science Foundation of China (NSFC)
31971118
中国
Ministry of Science and Technology (MoST, China)
2017YFC0840300
中国
Ministry of Science and Technology (MoST, China)
2020YFA0707500
中国
Chinese Academy of Sciences
XDB08020200
中国
Chinese Academy of Sciences
XDB37020203
中国
引用
ジャーナル: Science / 年: 2024 タイトル: Inherent symmetry and flexibility in hepatitis B virus subviral particles. 著者: Quan Wang / Tao Wang / Lin Cao / An Mu / Sheng Fu / Peipei Wang / Yan Gao / Wenxin Ji / Zhenyu Liu / Zhanqiang Du / Luke W Guddat / Wenchi Zhang / Shuang Li / Xuemei Li / Zhiyong Lou / ...著者: Quan Wang / Tao Wang / Lin Cao / An Mu / Sheng Fu / Peipei Wang / Yan Gao / Wenxin Ji / Zhenyu Liu / Zhanqiang Du / Luke W Guddat / Wenchi Zhang / Shuang Li / Xuemei Li / Zhiyong Lou / Xiangxi Wang / Zhongyu Hu / Zihe Rao / 要旨: 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, ...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.