ArticleNucleic acids research2018
Functional insights into the Streptococcus pneumoniae HicBA toxin-antitoxin system based on a structural study.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.
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Who cites it
31 citing papers in PubMed, 1 synthesis or guideline pooled it, 44 citations in OpenAlex.
- A Systematic Overview of Type II and III Toxin-Antitoxin Systems with a Focus on Druggability.Toxins · 2018Pooled it
- Potential role of a CRISPR-Cas-activated toxin-antitoxin system in bacterial immunity.Nature communications · 2026Article
- 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
- The Characterization of a Gonococcal HicAB Toxin-Antitoxin System Capable of Causing Bacteriostatic Growth Arrest.Microorganisms · 2025Article
- Functional analysis of the type II toxin-antitoxin system ParDE in Streptococcus suis serotype 2.BMC veterinary research · 2025Article
- The SpxA1-TenA toxin-antitoxin system regulates epigenetic variations of Streptococcus pneumoniae by targeting protein synthesis.PLoS pathogens · 2024Article
- Structural insight into the distinct regulatory mechanism of the HEPN-MNT toxin-antitoxin system in Legionella pneumophila.Nature communications · 2024Article
- The HicAB System: Characteristics and Biological Roles of an Underappreciated Toxin-Antitoxin System.International journal of molecular sciences · 2024Review
- Discovery of Antimicrobial Agents Based on Structural and Functional Study of theAntibiotics (Basel, Switzerland) · 2024Article
- Article
- Toxin-antitoxin system gene mutations drivingFrontiers in microbiology · 2024Article
- Type II bacterial toxin-antitoxins: hypotheses, facts, and the newfound plethora of the PezAT system.FEMS microbiology reviews · 2023Article
- Applications of toxin-antitoxin systems in synthetic biology.Engineering microbiology · 2023Review
- Structural and functional determinants inferred from deep mutational scans.Protein science : a publication of the Protein Society · 2022Article
- Insights into the Neutralization and DNA Binding of Toxin-Antitoxin System ParEMicroorganisms · 2021Article
- Bacterial toxin-antitoxin modules: classification, functions, and association with persistence.Current research in microbial sciences · 2021Review
- Prokaryote toxin-antitoxin modules: Complex regulation of an unclear function.Protein science : a publication of the Protein Society · 2021Review
- Modulators of protein-protein interactions as antimicrobial agents.RSC chemical biology · 2021Review
- Toxin-Activating Stapled Peptides Discovered by Structural Analysis Were Identified as New Therapeutic Candidates That Trigger Antibacterial Activity againstMicroorganisms · 2021Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Streptococcus pneumonia has attracted increasing attention due to its resistance to existing antibiotics. TA systems are essential for bacterial persistence under stressful conditions such as nutrient deprivation, antibiotic treatment, and immune system attacks. In particular, S. pneumoniae expresses the HicBA TA gene, which encodes the stable HicA toxin and the labile HicB antitoxin. These proteins interact to form a non-toxic TA complex under normal conditions, but the toxin is activated by release from the antitoxin in response to unfavorable growth conditions. Here, we present the first crystal structure showing the complete conformation of the HicBA complex from S. pneumonia. The structure reveals that the HicA toxin contains a double-stranded RNA-binding domain that is essential for RNA recognition and that the C-terminus of the HicB antitoxin folds into a ribbon-helix-helix DNA-binding motif. The active site of HicA is sterically blocked by the N-terminal region of HicB. RNase activity assays show that His36 is essential for the ribonuclease activity of HicA, and nuclear magnetic resonance (NMR) spectra show that several residues of HicB participate in binding to the promoter DNA of the HicBA operon. A toxin-mimicking peptide that inhibits TA complex formation and thereby increases toxin activity was designed, providing a novel approach to the development of new antibiotics.
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