ArticleProceedings of the National Academy of Sciences of the United States of America2017
Enigmatic origin of the poxvirus membrane from the endoplasmic reticulum shown by 3D imaging of vaccinia virus assembly mutants.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 38 citations in OpenAlex.
- Infection cycles of viruses of the phylum Nucleocytoviricota.Nature reviews. Microbiology · 2026Review
- Structural transition of the immature poxvirus scaffold from preassembly to the scaffold lattice.Nature communications · 2026Article
- The ER-Golgi intermediate compartment: a central hub integrating membrane trafficking and stress responses.EMBO reports · 2026Review
- Article
- Annexin A2 stabilizes the endoplasmic reticulum and actin cytoskeleton and influences the formation of reovirus factories.Journal of virology · 2025Article
- A Pyrido-Quinoxaline Derivative That Downregulates Reticulon 3 Protein Exhibits Potent Antiviral Activity Against Zika Virus.Journal of medical virology · 2025Article
- Expression of an Efficient Selection Marker Out of a Duplicated Site in the ITRs of a Modified Vaccinia Virus Ankara (MVA).Vaccines · 2024Article
- Structural analysis of conformational changes in the mpox virus A7 protein.Virologica Sinica · 2024Article
- Article
- Assembly and Evolution of Poxviruses.Advances in experimental medicine and biology · 2024Review
- Mpox virus infection and drug treatment modelled in human skin organoids.Nature microbiology · 2023Article
- Potential Anti-Mpox Virus Activity of Atovaquone, Mefloquine, and Molnupiravir, and Their Potential Use as Treatments.The Journal of infectious diseases · 2023Article
- Identification of IMP Dehydrogenase as a Potential Target for Anti-Mpox Virus Agents.Microbiology spectrum · 2023Article
- Vaccinia virus induces endoplasmic reticulum stress and activates unfolded protein responses through the ATF6α transcription factor.Virology journal · 2023Article
- A succession of two viral lattices drives vaccinia virus assembly.PLoS biology · 2023Article
- Three-dimensional analysis of membrane structures associated with tomato spotted wilt virus infection.Plant, cell & environment · 2023Article
- Poxvirus under the eyes of electron microscope.Applied microscopy · 2022Review
- Assembly mechanism of the pleomorphic immature poxvirus scaffold.Nature communications · 2022Article
- Viral use and subversion of membrane organization and trafficking.Journal of cell science · 2021Review
- Inducible intracellular membranes: molecular aspects and emerging applications.Microbial cell factories · 2020Review
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
The long-standing inability to visualize connections between poxvirus membranes and cellular organelles has led to uncertainty regarding the origin of the viral membrane. Indeed, there has been speculation that viral membranes form de novo in cytoplasmic factories. Another possibility, that the connections are too short-lived to be captured by microscopy during a normal infection, motivated us to identify and characterize virus mutants that are arrested in assembly. Five conserved vaccinia virus proteins, referred to as Viral Membrane Assembly Proteins (VMAPs), that are necessary for formation of immature virions were found. Transmission electron microscopy studies of two VMAP deletion mutants had suggested retention of connections between viral membranes and the endoplasmic reticulum (ER). We now analyzed cells infected with each of the five VMAP deletion mutants by electron tomography, which is necessary to validate membrane continuity, in addition to conventional transmission electron microscopy. In all cases, connections between the ER and viral membranes were demonstrated by 3D reconstructions, supporting a role for the VMAPs in creating and/or stabilizing membrane scissions. Furthermore, coexpression of the viral reticulon-like transmembrane protein A17 and the capsid-like scaffold protein D13 was sufficient to form similar ER-associated viral structures in the absence of other major virion proteins. Determination of the mechanism of ER disruption during a normal VACV infection and the likely participation of both viral and cell proteins in this process may provide important insights into membrane dynamics.
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