+検索条件
-Structure paper
| タイトル | Cryo-EM structure of the vaccinia virus entry fusion complex reveals a multicomponent fusion machinery. |
|---|---|
| ジャーナル・号・ページ | Sci Adv, Vol. 12, Issue 3, Page eaec0254, Year 2026 |
| 掲載日 | 2026年1月16日 |
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 |
| PubMed 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. |
リンク | Sci Adv / PubMed:41533782 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 3.05 Å |
| 構造データ | EMDB-64647, PDB-9uzo: EMDB-64648, PDB-9uzp: |
| 由来 |
|
キーワード | VIRAL PROTEIN / Vaccinia Virus / Entry-Fusion Complex (EFC) / cryo-EM / Single-particle reconstruction |
ムービー
コントローラー
構造ビューア
万見文献について



著者
リンク



orthopoxvirus vaccinia (ウイルス)
キーワード