ArticleScience advances2026
Cryo-EM structure of the vaccinia virus entry fusion complex reveals a multicomponent fusion machinery.
Article in Science advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Infection cycles of viruses of the phylum Nucleocytoviricota.Nature reviews. Microbiology · 2026Review
- Structure and functional analyses of vaccinia virus J5 protein reveal distinct determinants for entry-fusion complex assembly and activation.Journal of virology · 2026Article
- Current Strategies for Selecting Recombinant Orthopoxvirus Proteins for Immunobiological and Diagnostic Applications.Viruses · 2026Review
- Immunogenicity of poxvirus A16/G9 entry-fusion subcomplex and its restriction by A56/K2 protein informs vaccine design.Nature microbiology · 2026Article
- Article
- Review
- The SPARK complex forms the molecular basis of vertebrate fertilization.bioRxiv : the preprint server for biology · 2026Article
- Structural Insights into the Impact of the M142I Mutation in Monkeypox Virus G9 Protein on Subcomplex Formation Revealed by AlphaFold 3 Modeling.Molecules (Basel, Switzerland) · 2026Article
- Cellular lipids: fundamental host factors for monkeypox virus replication and pathogenesis.Archives of microbiology · 2026Review
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.