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Toxins
Volume 17
Issue 3
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Toxins, Volume 17, Issue 3 (March 2025) – 2 articles

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21 pages, 3970 KiB  
Review
It’s a Small World After All: The Remarkable but Overlooked Diversity of Venomous Organisms, with Candidates Among Plants, Fungi, Protists, Bacteria, and Viruses
by William K. Hayes, Eric C. K. Gren, David R. Nelsen, Aaron G. Corbit, Allen M. Cooper, Gerad A. Fox and M. Benjamin Streit
Toxins 2025, 17(3), 99; https://doi.org/10.3390/toxins17030099 - 20 Feb 2025
Abstract
Numerous organisms, including animals, plants, fungi, protists, and bacteria, rely on toxins to meet their needs. Biological toxins have been classified into three groups: poisons transferred passively without a delivery mechanism; toxungens delivered to the body surface without an accompanying wound; and venoms [...] Read more.
Numerous organisms, including animals, plants, fungi, protists, and bacteria, rely on toxins to meet their needs. Biological toxins have been classified into three groups: poisons transferred passively without a delivery mechanism; toxungens delivered to the body surface without an accompanying wound; and venoms conveyed to internal tissues via the creation of a wound. The distinctions highlight the evolutionary pathways by which toxins acquire specialized functions. Heretofore, the term venom has been largely restricted to animals. However, careful consideration reveals a surprising diversity of organisms that deploy toxic secretions via strategies remarkably analogous to those of venomous animals. Numerous plants inject toxins and pathogenic microorganisms into animals through stinging trichomes, thorns, spines, prickles, raphides, and silica needles. Some plants protect themselves via ants as venomous symbionts. Certain fungi deliver toxins via hyphae into infected hosts for nutritional and/or defensive purposes. Fungi can possess penetration structures, sometimes independent of the hyphae, that create a wound to facilitate toxin delivery. Some protists discharge harpoon-like extrusomes (toxicysts and nematocysts) that penetrate their prey and deliver toxins. Many bacteria possess secretion systems or contractile injection systems that can introduce toxins into targets via wounds. Viruses, though not “true” organisms according to many, include a group (the bacteriophages) which can inject nucleic acids and virion proteins into host cells that inflict damage rivaling that of conventional venoms. Collectively, these examples suggest that venom delivery systems—and even toxungen delivery systems, which we briefly address—are much more widespread than previously recognized. Thus, our understanding of venom as an evolutionary novelty has focused on only a small proportion of venomous organisms. With regard to this widespread form of toxin deployment, the words of the Sherman Brothers in Disney’s iconic tune, It’s a Small World, could hardly be more apt: “There’s so much that we share, that it’s time we’re aware, it’s a small world after all”. Full article
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Figure 1

Figure 1
<p>Four representative plant species showcasing proposed venom delivery systems. (<b>A</b>) <span class="html-italic">Acacia</span> (<span class="html-italic">Vachellia</span>) <span class="html-italic">cornigera</span>. Inset shows specializations for hosting colonies of symbiotic ants, including domatia (living quarters for the ants), extrafloral nectaries (nectar-producing glands), and Beltian bodies (providing food rich in lipids, sugars, and proteins and often red in color). The ants are venomous and protect the plant from herbivores, providing an effective defense analogous to that of facultatively venomous animals which co-opt the toxins of others. (<b>B</b>) <span class="html-italic">Viscum album</span>. Inset shows a cross-section of the specialized haustorium root structure invading the host plant’s vascular cambium. The haustorium secretes enzymes that degrade the protective bark layer and stimulate growth of new xylem tissue to connect with the parasite’s own vasculature. (<b>C</b>) <span class="html-italic">Urtica dioica</span>. Inset shows stinging trichomes, which comprise hollow, hypodermic needle-like structures which penetrate and break off in an animal’s skin upon physical contact, releasing irritating toxins. (<b>D</b>) <span class="html-italic">Dieffenbachia</span> sp. Inset portrays specialized calcium oxalate crystals (raphides) which penetrate the mucous membranes of animals that feed on the plant, causing irritation and potentially introducing proteolytic enzymes or pathogenic bacteria and fungi. Artwork: M. Benjamin Streit.</p> Full article ">Figure 2
<p>Two proposed venom delivery systems in fungi. (<b>A</b>) The appressorium of phytopathic taxa produces a peg-shaped structure (indicated by arrow) which penetrates the plant’s cell wall, allowing the fungal hyphae to deliver toxins into the target plant. (<b>B</b>) Entomopathic fungi use appressoria, adhesives, and/or cuticle-degrading enzymes (indicated by arrow) to create a wound through which the fungal hyphae can enter the tissues of the host and deliver toxins. Artwork: M. Benjamin Streit.</p> Full article ">Figure 3
<p>Two proposed venom delivery systems in unicellular eukaryotes. Both are offensive extrusomes that discharge their contents outside of the cell. (<b>A</b>) A group of ciliates (<span class="html-italic">Coleps</span>) attacking a <span class="html-italic">Paramecium</span> using venom. Inset shows the toxicysts, specialized organelles that penetrate the cell membrane of the target and deliver toxins. (<b>B</b>) The dinoflagellate <span class="html-italic">Polykrikos</span> displaying a discharged nematocyst, a harpoon-like organelle that potentially delivers venom into target prey and structurally resembles the nematocysts of venomous animals in the phylum Cnidaria (e.g., anemones, corals, jellyfishes). Artwork: M. Benjamin Streit.</p> Full article ">Figure 4
<p>Three bacterial secretion systems that penetrate target cell membranes to inject toxins. (<b>A</b>) Type-III secretion system. (<b>B</b>) Type-IV secretion system. (<b>C</b>) Type-VI secretion system. BCp: bacterial cytoplasm. EmS: extramembranal space. IM: inner membrane. OM: outer membrane. Pp: periplasm. TCp: target cytoplasm. TCM: target cell membrane. Bacteria rely on these systems to introduce toxins into the cells of other organisms. Artwork: M. Benjamin Streit.</p> Full article ">Figure 5
<p>Proposed venom delivery system of bacteriophage viruses. (<b>A</b>) Bacteriophage prior to injection of DNA into target cell. (<b>B</b>) Bacteriophage following injection of DNA. The DNA causes damage to the host which rivals that of many conventional venoms. Artwork: M. Benjamin Streit.</p> Full article ">
23 pages, 9989 KiB  
Article
Application of High-Resolution Mass Spectrometry for Ciguatoxin Detection in Fish from the Asia–Pacific Region
by Xin Li, Ker Lew, Yu Lee Leyau, Ping Shen, Joachim Chua, Kung Ju Lin, Yuansheng Wu and Sheot Harn Chan
Toxins 2025, 17(3), 100; https://doi.org/10.3390/toxins17030100 - 20 Feb 2025
Abstract
Fish is a major source of protein in Asia–Pacific countries. Ciguatera fish poisoning (CFP), caused by consuming reef fish contaminated with ciguatoxins (CTXs), poses a significant health risk, affecting the neurological, gastrointestinal, and cardiovascular systems. Climate change and the global food trade are [...] Read more.
Fish is a major source of protein in Asia–Pacific countries. Ciguatera fish poisoning (CFP), caused by consuming reef fish contaminated with ciguatoxins (CTXs), poses a significant health risk, affecting the neurological, gastrointestinal, and cardiovascular systems. Climate change and the global food trade are potentially major factors contributing to the expanding geographical range and frequency of CFP outbreaks. Therefore, the surveillance and monitoring of CTXs in fishery products are essential to safeguard food safety. In this study, liquid chromatography–high-resolution mass spectrometry (LC-HRMS) was used to screen for CTXs in wild-caught fish from the region. Analysis of two grouper fish samples from Okinawa, Japan, detected CTX-1B, a major CTX known to incur in fish from the Asia–Pacific region. Additionally, putative Indian Ocean CTXs (I-CTXs) were also identified. Further study with HRMS on wild-caught red emperor fish from Southeast Asia waters revealed low levels of I-CTXs as well. These findings underscore the urgent need for enhanced food safety measures and expansion of monitoring protocols to include I-CTXs. This research contributes to the global understanding of CTX distribution and confirms the importance of HRMS application in routine surveillance to mitigate the risks associated with ciguatera fish poisoning (CFP). Full article
(This article belongs to the Section Marine and Freshwater Toxins)
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Figure 1

Figure 1
<p>Detection of CTX-1B in grouper JS5 and JS6. (<b>A</b>) URMS; (<b>B</b>) HRMS.</p> Full article ">Figure 2
<p>P-CTXs detected in Okinawa groupers. (<b>A</b>) MS2 spectrum of CTX-1B; (<b>B</b>) MS2 spectrum of P-CTX-2/3; (<b>C</b>) MS2 spectrum of 7-hydroxyCTX-1B; (<b>D</b>) Chromatogram of P-CTXs in MeOH eluate from sample JS5; (<b>E</b>) Chromatogram of P-CTXs in MeOH eluate from sample JS6.</p> Full article ">Figure 3
<p>Pseudo spectra of P-CTXs in Okinawa groupers.</p> Full article ">Figure 4
<p>Indian Ocean CTXs detected in Okinawa groupers. (<b>A</b>) Chromatogram of I-CTXs in ACN eluate of sample JS5; (<b>B</b>) Chromatogram of I-CTXs in ACN eluate of sample JS6; (<b>C</b>) MS2 spectrum of I-CTX-1/2; (<b>D</b>) MS2 spectrum of I-CTX-5; (<b>E</b>) MS2 spectrum of I-CTX-6.</p> Full article ">Figure 5
<p>Pseudo spectra of putative I-CTXs in groupers.</p> Full article ">Figure 6
<p>Profile of CTX congeners in Okinawa groupers. (<b>A</b>) Relative peak area of the CTX congeners in fold change compared to CTX-1B; (<b>B</b>) Chromatogram of the CTX congeners from grouper JS6.</p> Full article ">Figure 7
<p>Detection of I-CTXs in red emperors (S13). (<b>A</b>) MS2 spectrum of I-CTX-1/2; (<b>B</b>) MS2 spectrum of I-CTX-5; (<b>C</b>) MS2 spectrum of I-CTX-6; (<b>D</b>) Chromatogram of I-CTXs in ACN eluate of sample S13.</p> Full article ">Figure 8
<p>Detection of I-CTXs in red emperors (S27). (<b>A</b>) MS2 spectrum of I-CTX-1/2; (<b>B</b>) MS2 spectrum of I-CTX-6; (<b>C</b>) Chromatogram of I-CTXs in MeOH eluate of sample S27.</p> Full article ">Figure 9
<p>A comparison of putative I-CTX 1/2 fragments to PPG fragments [<a href="#B57-toxins-17-00100" class="html-bibr">57</a>].</p> Full article ">
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