Special Issue "Toxin-Antitoxin System"


A special issue of Toxins (ISSN 2072-6651).

Deadline for manuscript submissions: closed (31 October 2014)

Special Issue Editor

Guest Editor
Prof. Dr. Laurence Van Melderen
Laboratoire de Génétique et Physiologie Bactérienne, Faculté de Sciences, IBMM, Université Libre de Bruxelles (ULB), Gosselies, B-6041, Belgium
E-Mail: lvmelder@ulb.ac.be
Phone: +32-2-650-97-78

Special Issue Information

Dear Colleagues,

Toxin-antitoxin (TA) systems are small genetic modules encoding a stable toxic protein and its cognate unstable antitoxin, which can be either RNA or protein. Five TA types are currently recognized, among them type II systems are probably the best documented. TA systems are surprisingly abundant in eubacterial and archeal genomes. TA systems were originally discovered on plasmids in the mid 1980s. Their function when located on such mobile genetic elements is to contribute to their stability by a phenomenon denoted as addiction (or post-segregational killing). Addiction relies on the differential stability of the antitoxin and toxin components. In daughter-bacteria that did not receive a plasmid copy at cell division, antitoxins are degraded and as a consequence toxins are released from inhibition thereby leading to the killing of plasmid-free cells. Homologues of plasmidic systems as well as novel types of TA systems were subsequently found in chromosomes and for some of them extensively studied. The biological role of these systems is still under debate and conflicting hypotheses have been proposed, at least for type II systems, from persistence to stabilization of large genomic islands or competition between mobile genetic elements. TA systems might also operate at the selfish level to promote their own dissemination in bacterial genomes although in certain conditions, at the expense of host survival. In addition to the functional aspects, essential questions regarding these diverse and mysterious genetic entities remain to be answered such as their origin and evolution and maybe the most intriguing which concerns the basis of their evolutionary success.

Prof. Dr. Laurence Van Melderen
Guest Editor



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. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as 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 refereed through a 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 1000 CHF (Swiss Francs).


  • endoribonuclease
  • selfish genes
  • programmed cell death
  • biofilm formation
  • stress responses
  • DNA-gyrase inhibitor
  • translation inhibition

Published Papers (5 papers)

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Displaying article 1-5
p. 2787-2803
by ,  and
Toxins 2014, 6(9), 2787-2803; doi:10.3390/toxins6092787
Received: 18 June 2014 / Revised: 14 August 2014 / Accepted: 9 September 2014 / Published: 18 September 2014
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(This article belongs to the Special Issue Toxin-Antitoxin System)
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p. 2310-2335
by  and
Toxins 2014, 6(8), 2310-2335; doi:10.3390/toxins6082310
Received: 30 June 2014 / Revised: 15 July 2014 / Accepted: 17 July 2014 / Published: 4 August 2014
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(This article belongs to the Special Issue Toxin-Antitoxin System)
p. 1002-1020
by ,  and
Toxins 2014, 6(3), 1002-1020; doi:10.3390/toxins6031002
Received: 19 December 2013 / Revised: 20 February 2014 / Accepted: 24 February 2014 / Published: 6 March 2014
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(This article belongs to the Special Issue Toxin-Antitoxin System)
p. 337-358
by  and
Toxins 2014, 6(1), 337-358; doi:10.3390/toxins6010337
Received: 6 December 2013 / Revised: 20 December 2013 / Accepted: 8 January 2014 / Published: 15 January 2014
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(This article belongs to the Special Issue Toxin-Antitoxin System)
p. 304-324
by  and
Toxins 2014, 6(1), 304-324; doi:10.3390/toxins6010304
Received: 2 December 2013 / Revised: 19 December 2013 / Accepted: 27 December 2013 / Published: 10 January 2014
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Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Type of Paper: Review
Title: sRNA Antitoxins: More than One Way to Repress a Toxin
Jia Wen and Elizabeth M. Fozo
Department of Microbiology, University of Tennessee, Knoxville, TN 37996, USA; E-Mail: efozo@utk.edu (E.M.F.)
Bacterial toxin-antitoxin loci consist of two genes: one encodes a potentially toxic protein, and the second, an antitoxin to repress its function or expression. The antitoxin can either be a RNA or a protein. For type I and type III loci, the antitoxins are RNAs, however, they have very different modes of action. Type I antitoxins repress toxin protein expression through interacting with the toxin mRNA, thereby targeting for degradation or preventing its translation or both; type III antitoxins directly bind to the toxin protein, sequestering it. Along with these two very different modes of action for the antitoxin, there are differences in function of the toxin proteins and the mobility of these loci between species. Within this review, we discuss the major differences as to how the RNAs repress toxin activity, the potential consequences for utilizing different regulatory strategies, as well as the confirmed and potential biological roles for these loci across bacterial species.

Last update: 31 March 2014

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