EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Prefusion structure, evasion and neutralization of HSV-1 glycoprotein B.
ジャーナル・号・ページ	Nat Microbiol, Vol. 10, Issue 11, Page 2966-2980, Year 2025
掲載日	2025年10月31日
著者	Ryan S Roark / Andrew J Schaub / Wei Shi / Maple Wang / Fabiana A Bahna / Jordan E Becker / Andrea Biju / Sue Chong / Haijuan Du / Yicheng Guo / Hsiang Hong / Phinikoula S Katsamba / Seetha M Mannepalli / Adam S Olia / Li Ou / Sarah K Rubin / Yosef Sabo / Mehin Suleiman / Malcolm L Wells / Baoshan Zhang / Cheng Cheng / Anum Glasgow / David D Ho / Yaoxing Huang / Theodore C Pierson / Reda Rawi / Tongqing Zhou / Lawrence Shapiro / Peter D Kwong /
PubMed 要旨	Glycoprotein B (gB) refolds between prefusion and postfusion conformations to facilitate herpesvirus entry into host cells. However, the isolation of prefusion-specific neutralizing antibodies, ...Glycoprotein B (gB) refolds between prefusion and postfusion conformations to facilitate herpesvirus entry into host cells. However, the isolation of prefusion-specific neutralizing antibodies, effective against other viral entry machines, has been challenging. Here we describe stabilization of the prefusion gB ectodomain from herpes simplex virus 1 (HSV-1), determine ectodomain structures at 2.9- to 4.1-Å resolution using cryogenic electron microscopy (cryo-EM) and isolate a prefusion-specific gB-neutralizing antibody termed WS.HSV-1.24. Murine immunization with gB stabilized in the prefusion conformation induced high titres of antibodies binding to both prefusion and postfusion gB, but-most notably-without measurable serum neutralization. Accessibility analysis revealed iso-surface exposure, with accessible surfaces on prefusion HSV-1 gB also exposed on postfusion gB. Structural analysis suggested substantial plasticity, with regions that refolded between pre- and postfusion conformations relegated to domain interfaces with limited accessibility; indeed, WS.HSV-1.24 recognized a domain-interface refolding region to facilitate neutralization. We propose that prefusion HSV-1 gB evades neutralization by most antibodies through an iso-surface display that is coupled to structural plasticity.
リンク	Nat Microbiol / PubMed:41174178 / PubMed Central
手法	EM (単粒子)
解像度	2.9 - 4.1 Å
構造データ	46758 9dd6 EMDB-46758, PDB-9dd6: Cryo-EM structure of neutralizing murine antibody WS.HSV-1.24 in complex with HSV-1 glycoprotein B trimer gB-Ecto.516P.531E 手法: EM (単粒子) / 解像度: 3.1 Å 46759 9dd7 EMDB-46759, PDB-9dd7: Cryo-EM structure of neutralizing human antibody D48 in complex with HSV-1 glycoprotein B trimer gB-Ecto.516P.531E.DS 手法: EM (単粒子) / 解像度: 4.1 Å 46760 9dd8 EMDB-46760, PDB-9dd8: Cryo-EM structure of neutralizing human antibody D48 in complex with HSV-1 glycoprotein B trimer gB-Ecto.516P 手法: EM (単粒子) / 解像度: 3.08 Å 46761 9dd9 EMDB-46761, PDB-9dd9: Cryo-EM structure of neutralizing human antibody D48 in complex with HSV-1 glycoprotein B trimer gB-Ecto.516P.531E 手法: EM (単粒子) / 解像度: 3.77 Å 46762 9dda EMDB-46762, PDB-9dda: Cryo-EM structure of gB-Ecto.516P.531E.DS, a prefusion-stabilized HSV-1 glycoprotein B extracellular domain 手法: EM (単粒子) / 解像度: 2.99 Å 46763 9ddb EMDB-46763, PDB-9ddb: Cryo-EM structure of gB-Ecto.516P.531E, a prefusion-stabilized HSV-1 glycoprotein B extracellular domain 手法: EM (単粒子) / 解像度: 3.71 Å 46765 9ddc EMDB-46765, PDB-9ddc: Cryo-EM structure of gB-Ecto.516P, an HSV-1 glycoprotein B extracellular domain 手法: EM (単粒子) / 解像度: 2.9 Å
化合物	ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose
由来	mus musculus (ハツカネズミ) human alphaherpesvirus 1 (ヘルペスウイルス) homo sapiens (ヒト)
キーワード	VIRAL PROTEIN / immune complex / neutralization / herpes fusogen / gB trimer / fusogen / postfusion-destabilization / neo-disulfide bond / trimer / postfusion