ArticleStructure (London, England : 1993)2021
Structural Basis for Toxin Inhibition in the VapXD Toxin-Antitoxin System.
Article in Structure (London, England : 1993), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 18 citations in OpenAlex.
- Plasmids inClinical microbiology reviews · 2026Review
- Expression of the VapD protein byMicrobiology (Reading, England) · 2026Article
- Functional Coupling and Evolutionary Relationships Between Toxin-Antitoxin Systems and CRISPR-Cas Systems.Toxins · 2025Review
- Article
- Structural Variations and Rearrangements in Bacterial Type II Toxin-Antitoxin Systems.Sub-cellular biochemistry · 2024Review
- Search for Origins of Anti-CRISPR Proteins by Structure Comparison.The CRISPR journal · 2023Article
- Evolution, persistence, and host adaption of a gonococcal AMR plasmid that emerged in the pre-antibiotic era.PLoS genetics · 2023Article
- Toxin-antitoxin systems in bacterial pathogenesis.Heliyon · 2023Review
- Structural biology of CRISPR-Cas immunity and genome editing enzymes.Nature reviews. Microbiology · 2022Review
- Molecular mechanism of toxin neutralization in the HipBST toxin-antitoxin system of Legionella pneumophila.Nature communications · 2022Article
- Biology and evolution of bacterial toxin-antitoxin systems.Nature reviews. Microbiology · 2022Review
- Structural and functional characterization of Cas2 of CRISPR-Cas subtype I-C lacking the CRISPR component.Frontiers in molecular biosciences · 2022Article
- Structural insights into the PrpTA toxin-antitoxin system inFrontiers in microbiology · 2022Article
- Auxiliary interfaces support the evolution of specific toxin-antitoxin pairing.Nature chemical biology · 2021Article
- Prokaryote toxin-antitoxin modules: Complex regulation of an unclear function.Protein science : a publication of the Protein Society · 2021Review
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8 authors at 2 institutions in 2 countries.
Funding
Abstract
Bacterial type II toxin-antitoxin (TA) modules encode a toxic protein that downregulates metabolism and a specific antitoxin that binds and inhibits the toxin during normal growth. In non-typeable Haemophilus influenzae, a common cause of infections in humans, the vapXD locus was found to constitute a functional TA module and contribute to pathogenicity; however, the mode of action of VapD and the mechanism of inhibition by the VapX antitoxin remain unknown. Here, we report the structure of the intact H. influenzae VapXD complex, revealing an unusual 2:1 TA molecular stoichiometry where a Cas2-like homodimer of VapD binds a single VapX antitoxin. VapX consists of an oligonucleotide/oligosaccharide-binding domain that docks into an asymmetrical cavity on the toxin dimer. Structures of isolated VapD further reveal how a symmetrical toxin homodimer adapts to interacting with an asymmetrical antitoxin and suggest how a primordial TA system evolved to become part of CRISPR-Cas immunity systems.
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