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Toxins
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Toxin–Host Interaction of Clostridium Toxins: 2nd Edition
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Toxin–Host Interaction of Clostridium Toxins: 2nd Edition

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

Deadline for manuscript submissions: 31 January 2027 | Viewed by 3798

Special Issue Editor

Dr. Jonatan Dorca-Arévalo

E-Mail Website
Guest Editor
1. Department of Pathology and Experimental Therapeutics, Faculty of Medicine and Health Sciences-Campus Bellvitge, University of Barcelona, 08907 Barcelona, Spain
2. Laboratory of Molecular and Cellular Neurobiology, Bellvitge Biomedical Research Institute (IDIBELL), 08907 L’Hospitalet de Llobregat, Spain
3. Institute of Neuroscience, Bellvitge Health Sciences Campus, University of Barcelona, Carrer de la Feixa Llarga, s/n, 08907 L’Hospitalet de Llobregat, Spain
Interests: bacterial protein toxins; pore-forming toxins; neurotoxins; microvesicles; exosomes; demyelinating diseases; oli-godendrocytes; glial cells; gut–brain axis; blood–brain barrier crossing; immune system; lipid rafts
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Following on from the first Special Issue, this Special Issue, “Toxin–Host Interaction of Clostridium Toxins: 2nd Edition”, will continue to focus on the study of the toxin–host interactions of Clostridium toxins and bring together the latest research findings in this field.

In this Special Issue, we welcome expert reviews of clinical aspects of host intoxication, as well as research papers on the following subtopics:

  • Structural studies of the toxin binding to the host cell receptor;
  • The effects of the clostridial toxins in the host cells;
  • The implication of the clostridial toxins in the gut–brain axis;
  • The effects of clostridial toxins in the blood and in the immune system;
  • New methods of toxin detection and diagnosis in host animals;
  • Novel toxin neutralizing molecules;
  • New vaccines against clostridial diseases;
  • New clostridial toxin mutants;
  • The study of clostridial toxins as therapeutic agents.

Dr. Jonatan Dorca-Arévalo
Guest Editor

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 250 words) can be sent to the Editorial Office for assessment.

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

  • clostridial toxins
  • gut–brain axis
  • clostridial vaccines
  • clostridial diseases
  • clostridial toxin structure
  • clostridial toxin effects

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Related Special Issue

Published Papers (3 papers)

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Research

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24 pages, 8737 KB  
Article
Interference of Large Clostridial Glucosyltransferases with the Endolysosomal Pathway: Toxin-Induced Imbalance of Early Endosomes, Functional Lysosomes and Autophagosomes
by Anna Langejürgen, Gudula Schmidt, Leon Unsöld, Helma Tatge, Ethel Oyson and Ralf Gerhard
Toxins 2026, 18(4), 186; https://doi.org/10.3390/toxins18040186 - 15 Apr 2026
Viewed by 526
Abstract
Toxin A and B from Clostridioides difficile are the main pathogenicity factors for clinical symptoms of C. difficile infections. Receptor-mediated endocytosis and endosomal escape are required for targeting substrate proteins of the Rho-GTPase family. We previously reported that Toxin B (TcdB) affects endo-lysosomal [...] Read more.
Toxin A and B from Clostridioides difficile are the main pathogenicity factors for clinical symptoms of C. difficile infections. Receptor-mediated endocytosis and endosomal escape are required for targeting substrate proteins of the Rho-GTPase family. We previously reported that Toxin B (TcdB) affects endo-lysosomal transport and autophagic flux of target cells. These effects are independent from pathogenic Rho inhibition. Here, we aimed at further characterization of this event by immunofluorescent characterization of the vesicular structures that are affected. We found large aggregates of damaged endolysosomal structures positive for EEA1, LAMP1, CHMP4B and TcdB, as well as an increase in perinuclear concentration of non-mature autophagosomes (amphisomes) positive for SQSTM, Rab7, and LC3B. We investigated whether Rab7, a regulator of late endosome transport, is causative for decreased lysosome function. Although TcdB induced an increase in active Rab7, as tested by an RILP pull-down assay, inhibition of Rab7 did not prevent TcdB-induced decrease in cathepsin D as a surrogate for lysosome dysfunction. It also indicates that the observed increase in Rab7 positive amphisomes is secondary to lysosomal dysfunction. By applying an autoproteolytic deficient mutant of TcdB we proved that the release of the glucosyltransferase domain is mandatory for triggering all of these effects. This suggests that after membrane perforation the toxin remnants leave an open leak in endolysosomes affecting ion homeostasis. Investigation of all large clostridial glucosyltransferases and other toxins revealed lysosomal dysfunction as a general effect of many but not of all toxins that integrate into the endosome membrane. Full article
(This article belongs to the Special Issue Toxin–Host Interaction of Clostridium Toxins: 2nd Edition)
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11 pages, 1634 KB  
Article
Botulinum Toxin Complex Serotype B-Okra Exerts Systemic Toxicity via the Oral Route by Disrupting the Intestinal Epithelial Barrier
by Chiyono Morimoto, Sho Amatsu, Takuhiro Matsumura, Masahiko Zuka and Yukako Fujinaga
Toxins 2025, 17(9), 443; https://doi.org/10.3390/toxins17090443 - 4 Sep 2025
Cited by 3 | Viewed by 1735
Abstract
Botulinum toxin (BoNT) causes flaccid paralysis by blocking the release of neurotransmitters. BoNTs associate with neurotoxin-associated proteins to form medium and large progenitor toxin complexes. The large progenitor toxin complex serotype A-62A (L-PTC/A-62A) specifically targets intestinal M cells for invasion, whereas large progenitor [...] Read more.
Botulinum toxin (BoNT) causes flaccid paralysis by blocking the release of neurotransmitters. BoNTs associate with neurotoxin-associated proteins to form medium and large progenitor toxin complexes. The large progenitor toxin complex serotype A-62A (L-PTC/A-62A) specifically targets intestinal M cells for invasion, whereas large progenitor toxin complex serotype B-Okra (L-PTC/B-Okra) is mainly taken up by enterocytes and exhibits higher toxicity via the oral route. Hemagglutinin (HA) is a neurotoxin-associated protein that promotes BoNT absorption from the intestine and has carbohydrate-binding and barrier-disrupting activities. In this study, we established an in vitro reconstitution and purification system for recombinant L-PTC/B-Okra and created a recombinant L-PTC/B-Okra mutant rL-PTC/B-KA with carbohydrate-binding activity but not barrier-disrupting activity. rL-PTC/B-KA showed significantly reduced oral toxicity. Our results demonstrate that the B-Okra toxin disrupts the epithelial barrier of enterocytes and exerts oral toxicity. Full article
(This article belongs to the Special Issue Toxin–Host Interaction of Clostridium Toxins: 2nd Edition)
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Review

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12 pages, 1524 KB  
Review
From Gut to Systemic Circulation: Molecular Strategies of Botulinum Neurotoxin Complexes
by Juliette Mondy and Emmanuel Lemichez
Toxins 2026, 18(3), 116; https://doi.org/10.3390/toxins18030116 - 24 Feb 2026
Viewed by 878
Abstract
Botulinum neurotoxins (BoNTs), among the most potent biological toxins, rely on co-produced nontoxic proteins to survive harsh gastrointestinal conditions and achieve efficient systemic dissemination after oral exposure. Recent structural and functional studies have revealed how BoNTs bind to the nontoxic non-hemagglutinin (NTNH) factors [...] Read more.
Botulinum neurotoxins (BoNTs), among the most potent biological toxins, rely on co-produced nontoxic proteins to survive harsh gastrointestinal conditions and achieve efficient systemic dissemination after oral exposure. Recent structural and functional studies have revealed how BoNTs bind to the nontoxic non-hemagglutinin (NTNH) factors to engage in interactions with either OrfXs/P47 or hemagglutinins (HAs) components for systemic dissemination. This review synthesizes recent findings that elucidate the molecular basis of NTNH-specific anchoring to the HA70 triskelion-like element or to the host protease-activated form of OrfX2, thereby highlighting divergent pathways that enhance oral toxicity. We also discuss current perspectives on the molecular mechanisms through which BoNTs, in cooperation with associated nontoxic proteins, are absorbed from the intestine. Full article
(This article belongs to the Special Issue Toxin–Host Interaction of Clostridium Toxins: 2nd Edition)
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