Heat-Resistant Toxins of Animal, Plant and Microbial Origins

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

Deadline for manuscript submissions: closed (30 November 2018) | Viewed by 19272

Special Issue Editor


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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

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Keywords

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

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Published Papers (2 papers)

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Research

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1 pages, 1722 KiB  
Article
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 - 3 Jul 2018
Cited by 15 | Viewed by 5325
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 [...] Read more.
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  
Review
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 - 8 Jan 2019
Cited by 83 | Viewed by 11910
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 [...] Read more.
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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