membrane fusion involved in viral entry into host cell / DNA-templated transcription termination / helicase activity / hydrolase activity / host cell endoplasmic reticulum membrane / fusion of virus membrane with host plasma membrane / viral envelope / symbiont entry into host cell / virion membrane / DNA binding ...membrane fusion involved in viral entry into host cell / DNA-templated transcription termination / helicase activity / hydrolase activity / host cell endoplasmic reticulum membrane / fusion of virus membrane with host plasma membrane / viral envelope / symbiont entry into host cell / virion membrane / DNA binding / ATP binding / membrane 類似検索 - 分子機能
Poxvirus A21 / Poxvirus A21 Protein / Poxvirus L5 / Poxvirus G3 / Poxvirus L5 protein family / Chordopoxvirus G3 protein / Viral late protein H2 / Poxvirus A28 / Viral late protein H2 / Poxvirus A28 family ...Poxvirus A21 / Poxvirus A21 Protein / Poxvirus L5 / Poxvirus G3 / Poxvirus L5 protein family / Chordopoxvirus G3 protein / Viral late protein H2 / Poxvirus A28 / Viral late protein H2 / Poxvirus A28 family / Virion membrane protein, poxvirus L1-related / Lipid membrane protein of large eukaryotic DNA viruses / Pox virus entry-fusion-complex G9/A16 / Pox virus entry-fusion-complex G9/A16 類似検索 - ドメイン・相同性
Entry-fusion complex protein OPG094 / Protein OPG104 / Protein OPG107 / Entry-fusion complex protein OPG076 / Virion membrane protein OPG143 / Entry-fusion complex associated protein OPG083 / Entry-fusion complex protein OPG086 / Entry-fusion complex protein OPG094 / Envelope protein OPG155 / Virion membrane protein OPG147 類似検索 - 構成要素
ジャーナル: Sci Adv / 年: 2026 タイトル: Cryo-EM structure of the vaccinia virus entry fusion complex reveals a multicomponent fusion machinery. 著者: Chang Sheng-Huei Lin / Ching-An Li / Chun-Hsiung Wang / Chi-Fei Kao / Hsiao-Jung Chiu / Min-Chi Yeh / Hua-De Gao / Meng-Chiao Ho / Hsien-Ming Lee / Wen Chang 要旨: Membrane fusion is essential for viral entry. Unlike class I-III fusion proteins, vaccinia virus (VACV) uses a multicomponent entry fusion complex (EFC). Using cryo-electron microscopy, we determined ...Membrane fusion is essential for viral entry. Unlike class I-III fusion proteins, vaccinia virus (VACV) uses a multicomponent entry fusion complex (EFC). Using cryo-electron microscopy, we determined the full-length structure of the VACV EFC at near-atomic resolution, revealing a 15-protein asymmetric assembly organized into three layers. The central A16/G9/J5 heterotrimer forms the fusion core, stabilized by conserved PXXCW and Delta motifs, and anchors two A28/H2 adaptor dimers linked to peripheral G3/L5/A21/O3 scaffolds. Structural and evolutionary analyses identify a conserved N-terminal domain in A16 containing a myristoyl-binding pocket and a phenylalanine-rich region that stabilizes the trimer and may regulate lipid engagement. An additional component, F9, binds peripherally to J5, A21, and H2 through Delta-like motifs, reinforcing the prefusion architecture. Together, these results define the VACV EFC as a unique multiprotein fusion machinery and provide a structural framework for understanding the mechanism of poxvirus entry and membrane fusion.