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Toxins
Special Issues
Pore-Forming Toxins: From Structure to Function
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Pore-Forming Toxins: From Structure to Function

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

Deadline for manuscript submissions: 15 June 2025 | Viewed by 2420

Special Issue Editor

Dr. Peter A. Keyel

E-Mail Website
Guest Editor
Department of Biological Sciences, Texas Tech University, Lubbock, TX 79409, USA
Interests: pore-forming toxins; cholesterol-dependent cytolysins; membrane repair; DNases; lupus
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

While pore-forming toxins (PFTs) were first thought to lyse cells, the elaborate defense mechanisms of host cells has broadened their function, including by altering key signaling pathways. The mechanisms PFTs use to impact host cell signaling and function are driven by structural elements in the toxins and their interaction with both the membrane and host proteins, although many of these pathways remain unknown. Understanding how PFTs alter cellular function in their target cells is critical to learning how to effectively target PFTs for therapy. While considerable progress has been made in this area, there remain key unknowns in several aspects of PFT structure and function. For example, what structural changes are needed for PFT function? How do host enzymes and factors impact PFT binding, oligomerization and pore formation? How and what signals are generated by PFT interactions with the membrane and receptors? What commonalities exist between PFTs from different classes and/or organisms? How do PFTs alter microbial communities? Finally, can we predict PFT structure and function from existing PFTs?

Dr. Peter A. Keyel
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

  • pore-forming toxin
  • cell signaling
  • hemolysin
  • host-pathogen interaction
  • cell death
  • cholesterol-dependent cytolysin
  • plasma membrane
  • toxin evolution

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Published Papers (2 papers)

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17 pages, 4715 KiB  
Article
Breaking Barriers: Candidalysin Disrupts Epithelial Integrity and Induces Inflammation in a Gut-on-Chip Model
by Moran Morelli and Karla Queiroz
Toxins 2025, 17(2), 89; https://doi.org/10.3390/toxins17020089 - 14 Feb 2025
Viewed by 1037
Abstract
Candida albicans is an opportunistic pathogenic yeast commonly found in the gastrointestinal tract of healthy humans. Under certain conditions, it can become invasive and cause life-threatening systemic infections. One mechanism used by C.albicans to breach the epithelial barrier is the secretion of candidalysin, [...] Read more.
Candida albicans is an opportunistic pathogenic yeast commonly found in the gastrointestinal tract of healthy humans. Under certain conditions, it can become invasive and cause life-threatening systemic infections. One mechanism used by C.albicans to breach the epithelial barrier is the secretion of candidalysin, a cytolytic peptide toxin. Candidalysin damages epithelial membranes and activates the innate immune response, making it key to C.albicans’ pathogenicity and a promising therapeutic target. Although candidalysin mediates C. albicans translocation through intestinal layers, its impact on epithelial responses is not fully understood. This study aims to characterize this response and develop scalable, quantitative methodologies to assess candidalysin’s toxicological effects using gut-on-chip models. We used the OrganoPlate® platform to expose Caco-2 tubules to candidalysin and evaluated their response with trans-epithelial electrical resistance (TEER), protein detection, and immunostaining. We then validated our findings in a proof-of-concept experiment using human intestinal organoid tubules. Candidalysin impaired barrier integrity, induced actin remodeling, and increased cell permeability. It also induced the release of LDH, cytokines, and the antimicrobial peptide LL37, suggesting cellular damage, inflammation, and antimicrobial activity. This study strengthens our understanding of candidalysin’s role in C. albicans pathogenesis and suggests new therapeutic strategies targeting this toxin. Moreover, patient-derived organoids show promise for capturing patient heterogeneity and developing personalized treatments. Full article
(This article belongs to the Special Issue Pore-Forming Toxins: From Structure to Function)
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20 pages, 6662 KiB  
Article
Pore-Forming Protein LIN-24 Enhances Starvation Resilience in Caenorhabditis elegans by Modulating Lipid Metabolism and Mitochondrial Dynamics
by Xinqiang Lan, Mengqi Yang, Jiali Wang, Chunping Huang, Andong Wu, Leilei Cui, Yingqi Guo, Lin Zeng, Xiaolong Guo, Yun Zhang, Yang Xiang and Qiquan Wang
Toxins 2025, 17(2), 72; https://doi.org/10.3390/toxins17020072 - 6 Feb 2025
Viewed by 1018
Abstract
The ability to survive starvation is a critical evolutionary adaptation, yet the molecular mechanisms underlying this capability remain incompletely understood. Pore-forming proteins (PFPs) are typically associated with immune defense, where they disturb the membranes of target cells. However, the role of PFPs in [...] Read more.
The ability to survive starvation is a critical evolutionary adaptation, yet the molecular mechanisms underlying this capability remain incompletely understood. Pore-forming proteins (PFPs) are typically associated with immune defense, where they disturb the membranes of target cells. However, the role of PFPs in non-immune functions, particularly in metabolic and structural adaptations to starvation, is less explored. Here, we investigate the aerolysin-like PFP LIN-24 in Caenorhabditis elegans and uncover its novel function in enhancing starvation resistance. We found that LIN-24 expression is upregulated during starvation, leading to increased expression of the lipase-encoding gene lipl-3. This upregulation accelerates the mobilization and degradation of lipid stores, thereby sustaining energy levels. Additionally, LIN-24 overexpression significantly preserves muscle integrity, as evidenced by the maintenance of muscle structure compared to wild-type worms. Furthermore, we demonstrate that LIN-24 induces the formation of donut-shaped mitochondria, a structural change likely aimed at reducing ATP production to conserve energy during prolonged nutrient deprivation. This mitochondrial remodeling depends on genes involved in mitochondrial dynamics, including mff-1, mff-2, drp-1, and clk-1. Collectively, these findings expand our understanding of PFPs, demonstrating their multifaceted role in stress resistance beyond immune defense. LIN-24’s involvement in regulating metabolism, preserving muscle structure, and remodeling mitochondria highlights its crucial role in the adaptive response to starvation, offering novel insights into the evolution of stress resistance mechanisms and potential therapeutic targets for conditions related to muscle preservation and metabolic regulation. Full article
(This article belongs to the Special Issue Pore-Forming Toxins: From Structure to Function)
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