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Special Issue Editor

Prof. J. Daniel Dubreuil

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Guest Editor

Department of pathology and microbiology, Faculté de médecine vétérinaire, Université de Montréal, Québec J2S 2M2, Canada
Interests: biological and molecular studies of bacterial heat-stable protein toxins

Special Issue Information

Dear Colleagues,

Many animals, plants, and microbes produce toxins that exert their toxic and sometimes lethal effects toward other living organisms. Toxins are believed to contribute to the survival and proliferation of a particular organism. Often, the same organism can produce more than one toxin and a number of these toxins are thermally resistant. This characteristic is related to the size and biochemical nature of the molecules synthesize, corresponding to peptides stabilized by disulfide bridges and more complex backbone-cyclized peptides. These peptides, typically comprising 60 amino acids or fewer, keep their 3D structure and remain active at temperatures as high as 100 °C. Understanding the actions of these toxins opens new ways to decipher cellular processes that were not achievable with previously available tools. This Special Issue of Toxins aimed at comparing animal (including insect), plant and microbe heat-resistant toxins, from the structure to the mechanism of action, including the adverse effects observed on the intoxicated organisms.

Prof. Dr. J. Daniel Dubreuil
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 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

heat-resistant toxins
animals
plants
microbes
honey bees
scorpions
spiders
sea anemones
mycotoxins
conotoxins

Published Papers (2 papers)

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Research

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1 pages, 1722 KiB

Open AccessArticle

Purification and Characterization of Native and Vaccine Candidate Mutant Enterotoxigenic Escherichia coli Heat-Stable Toxins

by Morten L. Govasli, Yuleima Diaz, Ephrem Debebe Zegeye, Christine Darbakk, Arne M. Taxt and Pål Puntervoll

Toxins 2018, 10(7), 274; https://doi.org/10.3390/toxins10070274 - 03 Jul 2018

Cited by 13 | Viewed by 4814

Abstract

Enterotoxigenic Escherichia coli (ETEC), which secretes the heat-stable toxin (ST) is among the four most important enteropathogens that cause moderate-to-severe diarrhea in children in low- and middle-income countries. ST is an intestinal molecular antagonist causing diarrhea and hence an attractive vaccine target. A non-toxic and safe ST vaccine should include one or more detoxifying mutations, and rigorous characterization of such mutants requires structurally intact peptides. To this end, we established a system for purification of ST and ST mutants by fusing the sequence encoding the mature ST peptide to the disulfide isomerase DsbC. A Tobacco Etch Virus protease cleavage site facilitates the proteolytic release of free ST with no additional residues. The purified ST peptides have the expected molecular masses, the correct number of disulfide bridges, and have biological activities and antigenic properties comparable to ST isolated from ETEC. We also show that free DsbC can assist in refolding denatured and misfolded ST in vitro. Finally, we demonstrate that the purification system can be used to produce ST mutants with an intact neutralizing epitope, that two single mutations, L9S and A14T, reduce toxicity more than 100-fold, and that the L9S/A14T double mutant has no measurable residual toxicity. Full article

(This article belongs to the Special Issue Heat-Resistant Toxins of Animal, Plant and Microbial Origins)

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Review

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12 pages, 885 KiB

Open AccessEditor’s ChoiceReview

Heat-Stable Enterotoxins of Enterotoxigenic Escherichia coli and Their Impact on Host Immunity

by Haixiu Wang, Zifu Zhong, Yu Luo, Eric Cox and Bert Devriendt

Toxins 2019, 11(1), 24; https://doi.org/10.3390/toxins11010024 - 08 Jan 2019

Cited by 69 | Viewed by 10381

Abstract

Enterotoxigenic Escherichia coli (ETEC) are an important diarrhea-causing pathogen and are regarded as a global threat for humans and farm animals. ETEC possess several virulence factors to infect its host, including colonization factors and enterotoxins. Production of heat-stable enterotoxins (STs) by most ETEC plays an essential role in triggering diarrhea and ETEC pathogenesis. In this review, we summarize the heat-stable enterotoxins of ETEC strains from different species as well as the molecular mechanisms used by these heat-stable enterotoxins to trigger diarrhea. As recently described, intestinal epithelial cells are important modulators of the intestinal immune system. Thus, we also discuss the impact of the heat-stable enterotoxins on this role of the intestinal epithelium and how these enterotoxins might affect intestinal immune cells. Finally, the latest developments in vaccination strategies to protect against infections with ST secreting ETEC strains are discussed. This review might inform and guide future research on heat-stable enterotoxins to further unravel their molecular pathogenesis, as well as to accelerate vaccine design. Full article

(This article belongs to the Special Issue Heat-Resistant Toxins of Animal, Plant and Microbial Origins)

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