ArticleProceedings of the National Academy of Sciences of the United States of America2018
Structural basis for the inhibition of poxvirus assembly by the antibiotic rifampicin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
32 citing papers in PubMed, 58 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
- Exploration of the protein and pharmacological landscape of monkeypox virus treatment: from entry point to end point.Molecular diversity · 2026Review
- Article
- Monkeypox (Mpox), a Resurging Global Public Health Concern: An Updated Outlook Through 2025.Current issues in molecular biology · 2026Review
- Repurposing of FDA-Approved Antiviral Drugs Against Monkeypox Virus: Comparative In Vitro Screening and Structure Based In Silico Studies.Pharmaceuticals (Basel, Switzerland) · 2025Article
- Giant virus genomes are unlikely to be reservoirs of antibiotic resistance genes.Nature communications · 2025Article
- Reply to: Giant virus genomes are unlikely to be reservoirs of antibiotic resistance genes.Nature communications · 2025Article
- Molecular chameleons adaptability in target binding.Structural dynamics (Melville, N.Y.) · 2025Article
- Computational repurposing of polyphenols for anti-Mpoxviral activity.In silico pharmacology · 2025Article
- Cryo-EM structures of a mycobacterial ABC transporter that mediates rifampicin resistance.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Abortive Infection of Animal Cells: What Goes Wrong.Annual review of virology · 2024Review
- Structure of the poxvirus core.Nature structural & molecular biology · 2024Article
- Treatment and Vaccination for Smallpox and Monkeypox.Advances in experimental medicine and biology · 2024Review
- Inhibition of porcine reproductive and respiratory syndrome virus replication by rifampicinFrontiers in veterinary science · 2024Article
- Identification of core therapeutic targets for Monkeypox virus and repurposing potential of drugs: A WEB prediction approach.PloS one · 2024Article
- VP37 Protein Inhibitors for Mpox Treatment: Highlights on Recent Advances, Patent Literature, and Future Directions.Biomedicines · 2023Review
- A Quantitative Method for the Study of HIV-1 and Mycobacterium tuberculosis Coinfection.The Journal of infectious diseases · 2023Article
- Emergence, phylogeography, and adaptive evolution of mpox virus.New microbes and new infections · 2023Article
- A succession of two viral lattices drives vaccinia virus assembly.PLoS biology · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Poxviruses are large DNA viruses that cause disease in animals and humans. They differ from classical enveloped viruses, because their membrane is acquired from cytoplasmic membrane precursors assembled onto a viral protein scaffold formed by the D13 protein rather than budding through cellular compartments. It was found three decades ago that the antibiotic rifampicin blocks this process and prevents scaffold formation. To elucidate the mechanism of action of rifampicin, we have determined the crystal structures of six D13-rifamycin complexes. These structures reveal that rifamycin compounds bind to a phenylalanine-rich region, or F-ring, at the membrane-proximal opening of the central channel of the D13 trimer. We show by NMR, surface plasmon resonance (SPR), and site-directed mutagenesis that A17, a membrane-associated viral protein, mediates the recruitment of the D13 scaffold by also binding to the F-ring. This interaction is the target of rifampicin, which prevents A17 binding, explaining the inhibition of viral morphogenesis. The F-ring of D13 is both conserved in sequence in mammalian poxviruses and essential for interaction with A17, defining a target for the development of assembly inhibitors. The model of the A17-D13 interaction describes a two-component system for remodeling nascent membranes that may be conserved in other large and giant DNA viruses.
Indexed as
Identifiers
What OpenQuestion holds
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.