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Toxins
Special Issues
Bacterial Toxin–Antitoxin Systems: Biological Functions and Mechanisms of Action
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Bacterial Toxin–Antitoxin Systems: Biological Functions and Mechanisms of Action

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Bacterial Toxins".

Deadline for manuscript submissions: closed (30 November 2023) | Viewed by 2504

Special Issue Editors

Prof. Dr. Hanna Engelberg-Kulka

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Guest Editor
Department of Microbiology and Molecular Genetics, IMRIC, The Hebrew University-Hadassah Medical School, Jerusalem, Israel
Interests: bacterial toxin–antitoxin systems; programmed cell death
Prof. Dr. Juan Carlos Alonso

E-Mail Website
Guest Editor
Department of Microbial Biotechnology, Centro Nacional de Biotecnología, CNB-CSIC, 28049 Madrid, Spain
Interests: genome stability; recombination-dependent replication; chromosome segregation; toxin-antitoxins
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Bacterial toxin–antitoxin (TA) systems encode a toxic protein and an antitoxin, which is either a protein or an RNA that counteracts the toxin. They are abundant in bacterial chromosomes and in extra-chromosomal genetic elements.

In this Special Issue, we will describe the characterized TA systems, their targets and mechanisms of action, their evolution and their roles in post-segragational killing, growth control, and programmed cell death.

Prof. Dr. Hanna Engelberg-Kulka
Prof. Dr. Juan Carlos Alonso
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a double-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • toxin–antitoxin systems
  • toxic protein
  • antitoxin
  • bacterial toxins

Published Papers (2 papers)

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Research

15 pages, 3134 KiB  
Article
MazEF Homologs in Symbiobacterium thermophilum Exhibit Cross-Neutralization with Non-Cognate MazEFs
by Yu-Nong Jiang, Hiroko Tamiya-Ishitsuka, Rie Aoi, Takuma Okabe, Akiko Yokota and Naohiro Noda
Toxins 2024, 16(2), 81; https://doi.org/10.3390/toxins16020081 - 03 Feb 2024
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Abstract
Toxin–antitoxin systems are preserved by nearly every prokaryote. The type II toxin MazF acts as a sequence-specific endoribonuclease, cleaving ribonucleotides at specific sequences that vary from three to seven bases, as has been reported in different host organisms to date. The present study [...] Read more.
Toxin–antitoxin systems are preserved by nearly every prokaryote. The type II toxin MazF acts as a sequence-specific endoribonuclease, cleaving ribonucleotides at specific sequences that vary from three to seven bases, as has been reported in different host organisms to date. The present study characterized the MazEF module (MazEF-sth) conserved in the Symbiobacterium thermophilum IAM14863 strain, a Gram-negative syntrophic bacterium that can be supported by co-culture with multiple bacteria, including Bacillus subtilis. Based on a method combining massive parallel sequencing and the fluorometric assay, MazF-sth was determined to cleave ribonucleotides at the UACAUA motif, which is markedly similar to the motifs recognized by MazF from B. subtilis (MazF-bs), and by several MazFs from Gram-positive bacteria. MazF-sth, with mutations at conserved amino acid residues Arg29 and Thr52, lost most ribonuclease activity, indicating that these residues that are crucial for MazF-bs also play significant roles in MazF-sth catalysis. Further, cross-neutralization between MazF-sth and the non-cognate MazE-bs was discovered, and herein, the neutralization mechanism is discussed based on a protein-structure simulation via AlphaFold2 and multiple sequence alignment. The conflict between the high homology shared by these MazF amino acid sequences and the few genetic correlations among their host organisms may provide evidence of horizontal gene transfer. Full article
(This article belongs to the Special Issue Bacterial Toxin–Antitoxin Systems: Biological Functions and Mechanisms of Action)
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14 pages, 2642 KiB  
Article
Unraveling the Role of the Zinc-Dependent Metalloproteinase/HTH-Xre Toxin/Antitoxin (TA) System of Brucella abortus in the Oxidative Stress Response: Insights into the Stress Response and Virulence
by Leonardo A. Gómez, Raúl E. Molina, Rodrigo I. Soto, Manuel R. Flores, Roberto F. Coloma-Rivero, David A. Montero and Ángel A. Oñate
Toxins 2023, 15(9), 536; https://doi.org/10.3390/toxins15090536 - 31 Aug 2023
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Abstract
Toxin/antitoxin (TA) systems have been scarcely studied in Brucella abortus, the causative agent of brucellosis, which is one of the most prevalent zoonotic diseases worldwide. In this study, the roles of a putative type II TA system composed by a Zinc-dependent metalloproteinase [...] Read more.
Toxin/antitoxin (TA) systems have been scarcely studied in Brucella abortus, the causative agent of brucellosis, which is one of the most prevalent zoonotic diseases worldwide. In this study, the roles of a putative type II TA system composed by a Zinc-dependent metalloproteinase (ZnMP) and a transcriptional regulator HTH-Xre were evaluated. The deletion of the open reading frame (ORF) BAB1_0270, coding for ZnMP, used to produce a mutant strain, allowed us to evaluate the survival and gene expression of B. abortus 2308 under oxidative conditions. Our results showed that the B. abortus mutant strain exhibited a significantly reduced capacity to survive under hydrogen peroxide-induced oxidative stress. Furthermore, this mutant strain showed a decreased expression of genes coding for catalase (katE), alkyl hydroperoxide reductase (ahpC) and transcriptional regulators (oxyR and oxyR-like), as well as genes involved in the general stress response, phyR and rpoE1, when compared to the wild-type strain. These findings suggest that this type II ZnMP/HTH-Xre TA system is required by B. abortus to resist oxidative stress. Additionally, previous evidence has demonstrated that this ZnMP also participates in the acidic stress resistance and virulence of B. abortus 2308. Therefore, we propose a hypothetical regulatory function for this ZnMP/HTH-Xre TA system, providing insight into the stress response and its potential roles in the pathogenesis of B. abortus. Full article
(This article belongs to the Special Issue Bacterial Toxin–Antitoxin Systems: Biological Functions and Mechanisms of Action)
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