ArticleMolecular biotechnology2020
Biochemical Characterization of VapC46 Toxin from Mycobacterium tuberculosis.
Article in Molecular biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- Protein-Mediated Virulence in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Role of VapBC4 toxin-antitoxin system ofmBio · 2024Article
- The Toxin of VapBC-1 Toxin-Antitoxin Module fromMicroorganisms · 2024Article
- Impact of Genomic Deletion RD16 on the Expression of theCurrent issues in molecular biology · 2023Article
- Review
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
Emergence of multidrug resistant strains and extremely drug resistant strains of Mycobacterium tuberculosis is due to its ability to form persister cells. The formation of persister cells is assumed to be triggered due to the presence of large number of toxin-antitoxin (TA) systems in its genome. Mtb genome encodes 47 VapBC TA systems. In this work, we aim to biochemically characterize VapC46 toxin of the VapBC46 TA operon from Mycobacterium tuberculosis. Heterologous expression of VapC46 in E. coli is shown to exhibit bacteriostasis and toxicity alters the surface morphology of the E. coli cells. VapC46 is shown to possess ribonuclease activity in a magnesium-dependent manner. Using FRET and pull down assay, VapC46 is shown to interact with VapB46 antitoxin. A model of VapC46 is shown to resemble PIN domain family of proteins and reveals the putative active site required for its ribonuclease activity.
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