ArticleNucleic acids research2017
Functional details of the Mycobacterium tuberculosis VapBC26 toxin-antitoxin system based on a structural study: insights into unique binding and antibiotic peptides.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 1 of them a synthesis that pooled it.
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Who cites it
36 citing papers in PubMed, 1 synthesis or guideline pooled it.
- A Systematic Overview of Type II and III Toxin-Antitoxin Systems with a Focus on Druggability.Toxins · 2018Pooled it
- A haloarchaeal VapBC toxin-antitoxin system: regulatory mechanism and role in establishing population heterogeneity to facilitate survival of subpopulations under stress conditions.Applied and environmental microbiology · 2026Article
- Structural and functional characterization of VapBC52 toxin-antitoxin system from Mycobacterium tuberculosis.Nucleic acids research · 2026Article
- Key Proteins and Enzymatic Mechanisms Underlying Drug Resistance in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Comparative in silico analysis of vapBC3 toxin-antitoxin system in Mycobacterium Bovis and Mycobacterium tuberculosis.Scientific reports · 2025Article
- Protein-Protein Interactions as Promising Molecular Targets for Novel Antimicrobials Aimed at Gram-Negative Bacteria.International journal of molecular sciences · 2025Review
- Bacterial programmed cell death and toxin-antitoxin system in bacteria.Archives of microbiology · 2025Review
- Understanding the physiological role and cross-interaction network of VapBC35 toxin-antitoxin system from Mycobacterium tuberculosis.Communications biology · 2025Article
- Molecular characteristics of drug-susceptible Mycobacterium tuberculosis clinical isolates based on treatment duration.Osong public health and research perspectives · 2024Article
- Discovery of Antimicrobial Agents Based on Structural and Functional Study of theAntibiotics (Basel, Switzerland) · 2024Article
- Are all VapC toxins ofJournal of biosciences · 2024Article
- Identification of Genes Encoded Toxin-Antitoxin System inInfectious disorders drug targets · 2024Article
- Focused Overview ofBiomimetics (Basel, Switzerland) · 2023Review
- Bacterial Toxin-Antitoxin Systems' Cross-Interactions-Implications for Practical Use in Medicine and Biotechnology.Toxins · 2023Review
- Applications of toxin-antitoxin systems in synthetic biology.Engineering microbiology · 2023Review
- Article
- Biology and evolution of bacterial toxin-antitoxin systems.Nature reviews. Microbiology · 2022Review
- tRNAAntimicrobial agents and chemotherapy · 2022Article
- Structural and functional analysis of theIUCrJ · 2021Article
- Modulators of protein-protein interactions as antimicrobial agents.RSC chemical biology · 2021Review
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Toxin-antitoxin (TA) systems are essential for bacterial persistence under stressful conditions. In particular, Mycobacterium tuberculosis express VapBC TA genes that encode the stable VapC toxin and the labile VapB antitoxin. Under normal conditions, these proteins interact to form a non-toxic TA complex, but the toxin is activated by release from the antitoxin in response to unfavorable conditions. Here, we present the crystal structure of the M. tuberculosis VapBC26 complex and show that the VapC26 toxin contains a pilus retraction protein (PilT) N-terminal (PIN) domain that is essential for ribonuclease activity and that, the VapB26 antitoxin folds into a ribbon-helix-helix DNA-binding motif at the N-terminus. The active site of VapC26 is sterically blocked by the flexible C-terminal region of VapB26. The C-terminal region of free VapB26 adopts an unfolded conformation but forms a helix upon binding to VapC26. The results of RNase activity assays show that Mg2+ and Mn2+ are essential for the ribonuclease activity of VapC26. As shown in the nuclear magnetic resonance spectra, several residues of VapB26 participate in the specific binding to the promoter region of the VapBC26 operon. In addition, toxin-mimicking peptides were designed that inhibit TA complex formation and thereby increase toxin activity, providing a novel approach to the development of new antibiotics.
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