ArticleNature communications2022
Assembly mechanism of the pleomorphic immature poxvirus scaffold.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Structural transition of the immature poxvirus scaffold from preassembly to the scaffold lattice.Nature communications · 2026Article
- Article
- Virtual screening and identification of potent phytoconstituents from Acorus calamus L. as inhibitors of Monkeypox virus infection.Journal, genetic engineering & biotechnology · 2025Article
- Methods to Study Poxvirus Structures by Cryo-EM Imaging Modalities.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Structure of the poxvirus core.Nature structural & molecular biology · 2024Article
- Multi-modal cryo-EM reveals trimers of protein A10 to form the palisade layer in poxvirus cores.Nature structural & molecular biology · 2024Article
- Assembly and Evolution of Poxviruses.Advances in experimental medicine and biology · 2024Review
- A succession of two viral lattices drives vaccinia virus assembly.PLoS biology · 2023Article
- Poxvirus under the eyes of electron microscope.Applied microscopy · 2022Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Vaccinia virus (VACV), the prototype poxvirus, scaffold protein D13 forms a honeycomb-like lattice on the viral membrane that results in formation of the pleomorphic immature virion (IV). The structure of D13 is similar to those of major capsid proteins that readily form icosahedral capsids in nucleocytoplasmic large DNA viruses (NCLDVs). However, the detailed assembly mechanism of the nonicosahedral poxvirus scaffold has never been understood. Here we show the cryo-EM structures of the D13 trimer and scaffold intermediates produced in vitro. The structures reveal that the displacement of the short N-terminal α-helix is critical for initiation of D13 self-assembly. The continuous curvature of the IV is mediated by electrostatic interactions that induce torsion between trimers. The assembly mechanism explains the semiordered capsid-like arrangement of D13 that is distinct from icosahedral NCLDVs. Our structures explain how a single protein can self-assemble into different capsid morphologies and represent a local exception to the universal Caspar-Klug theory of quasi-equivalence.
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