ArticleScientific reports2020
Snapshots of ADP-ribose bound to Getah virus macro domain reveal an intriguing choreography.
Article in Scientific reports, 2020. 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, 10 citations in OpenAlex.
- Functional roles for viral RNA ribosylation in mammalian cells.Nucleic acids research · 2026Article
- Alphavirus nsP3 as a multifunctional orchestrator of virus-host interplay.Journal of virology · 2026Review
- Derivatives of MOPS: promising scaffolds for SARS coronaviruses Macro domain-targeted inhibition.The FEBS journal · 2025Article
- Zinc-finger PARP proteins ADP-ribosylate alphaviral proteins and are required for interferon-γ-mediated antiviral immunity.Science advances · 2025Article
- Crystal structure and biochemical activity of the macrodomain from rubella virus p150.Journal of virology · 2024Article
- Regulation of Biomolecular Condensates by Poly(ADP-ribose).Chemical reviews · 2023Review
- NMR study of macro domains (MDs) from betacoronavirus: backbone resonance assignments of SARS-CoV and MERS-CoV MDs in the free and the ADPr-bound state.Biomolecular NMR assignments · 2022Article
- ADP-ribosylation systems in bacteria and viruses.Computational and structural biotechnology journal · 2021Review
- Viral macrodomains: a structural and evolutionary assessment of the pharmacological potential.Open biology · 2020Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alphaviruses are (re-)emerging arboviruses of public health concern. The nsP3 gene product is one of the key players during viral replication. NsP3 comprises three domains: a macro domain, a zinc-binding domain and a hypervariable region. The macro domain is essential at both early and late stages of the replication cycle through ADP-ribose (ADPr) binding and de-ADP-ribosylation of host proteins. However, both its specific role and the precise molecular mechanism of de-ADP-ribosylation across specific viral families remains to be elucidated. Here we investigate by X-ray crystallography the mechanism of ADPr reactivity in the active site of Getah virus macro domain, which displays a peculiar substitution of one of the conserved residues in the catalytic loop. ADPr adopts distinct poses including a covalent bond between the C''1 of the ADPr and a conserved Togaviridae-specific cysteine. These different poses observed for ADPr may represent snapshots of the de-ADP-ribosylation mechanism, highlighting residues to be further characterised.
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Registered trials
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