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Toxins
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Pore-Forming Toxin Interactions with the Membrane
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Pore-Forming Toxin Interactions with the Membrane

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

Deadline for manuscript submissions: closed (30 September 2022) | Viewed by 5130

Special Issue Editor

Dr. Peter A. Keyel

E-Mail Website
Guest Editor
Department of Biological Sciences, Texas Tech University, Box 43131 Lubbock, TX 79409, USA
Interests: cholesterol-dependent cytolysin; membrane repair; inflammasome; macrophage; Dnase1L3
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Pore-forming toxins (PFTs) are used both to promote host defense and as key bacterial virulence factors. They disrupt lipid membranes and are difficult to target therapeutically. Understanding how PFTs engage with the membrane 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–membrane biology. For example, how do PFTs target the membrane? What structural changes and regulatory factors are needed to recruit PFTs to the membrane? How does membrane composition 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?

This Special Issue will focus on the interaction of pore-forming toxins with cell membranes, the functional outcomes of these interactions, and membrane responses to these toxins. Nonlethal toxin–membrane interactions, and novel insights into membrane organization, are areas of especial interest.

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
  • cholesterol-dependent cytolysin
  • hemolysin
  • plasma membrane
  • host–pathogen interaction
  • membrane repair
  • cell death
  • phase transition

Published Papers (2 papers)

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Research

22 pages, 3979 KiB  
Article
Cells Responding to Closely Related Cholesterol-Dependent Cytolysins Release Extracellular Vesicles with a Common Proteomic Content Including Membrane Repair Proteins
by Sara Alves, Joana M. Pereira, Rupert L. Mayer, Alexandre D. A. Gonçalves, Francis Impens, Didier Cabanes and Sandra Sousa
Toxins 2023, 15(1), 4; https://doi.org/10.3390/toxins15010004 - 20 Dec 2022
Cited by 1 | Viewed by 1947
Abstract
The plasma membrane (PM) protects cells from extracellular threats and supports cellular homeostasis. Some pathogens produce pore-forming toxins (PFTs) that disrupt PM integrity by forming transmembrane pores. High PFT concentrations cause massive damage leading to cell death and facilitating infection. Sub-lytic PFT doses [...] Read more.
The plasma membrane (PM) protects cells from extracellular threats and supports cellular homeostasis. Some pathogens produce pore-forming toxins (PFTs) that disrupt PM integrity by forming transmembrane pores. High PFT concentrations cause massive damage leading to cell death and facilitating infection. Sub-lytic PFT doses activate repair mechanisms to restore PM integrity, support cell survival and limit disease. Shedding of extracellular vesicles (EVs) has been proposed as a key mechanism to eliminate PFT pores and restore PM integrity. We show here that cholesterol-dependent cytolysins (CDCs), a specific family of PFTs, are at least partially eliminated through EVs release, and we hypothesize that proteins important for PM repair might be included in EVs shed by cells during repair. To identify new PM repair proteins, we collected EVs released by cells challenged with sub-lytic doses of two different bacterial CDCs, listeriolysin O and pneumolysin, and determined the EV proteomic repertoire by LC-MS/MS. Intoxicated cells release similar EVs irrespectively of the CDC used. Also, they release more and larger EVs than non-intoxicated cells. A cluster of 70 proteins including calcium-binding proteins, molecular chaperones, cytoskeletal, scaffold and membrane trafficking proteins, was detected enriched in EVs collected from intoxicated cells. While some of these proteins have well-characterized roles in repair, the involvement of others requires further study. As proof of concept, we show here that Copine-1 and Copine-3, proteins abundantly detected in EVs released by intoxicated cells, are required for efficient repair of CDC-induced PM damage. Additionally, we reveal here new proteins potentially involved in PM repair and give new insights into common mechanisms and machinery engaged by cells in response to PM damage. Full article
(This article belongs to the Special Issue Pore-Forming Toxin Interactions with the Membrane)
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19 pages, 3279 KiB  
Article
Interaction of Clostridium perfringens Epsilon Toxin with the Plasma Membrane: The Role of Amino Acids Y42, Y43 and H162
by Skye Marshall, Beth McGill, Helen Morcrette, C. Peter Winlove, Catalin Chimerel, Peter G. Petrov and Monika Bokori-Brown
Toxins 2022, 14(11), 757; https://doi.org/10.3390/toxins14110757 - 03 Nov 2022
Cited by 1 | Viewed by 2579
Abstract
Clostridium perfringens epsilon toxin (Etx) is a pore forming toxin that causes enterotoxaemia in ruminants and may be a cause of multiple sclerosis in humans. To date, most in vitro studies of Etx have used the Madin-Darby canine kidney (MDCK) cell line. However, [...] Read more.
Clostridium perfringens epsilon toxin (Etx) is a pore forming toxin that causes enterotoxaemia in ruminants and may be a cause of multiple sclerosis in humans. To date, most in vitro studies of Etx have used the Madin-Darby canine kidney (MDCK) cell line. However, studies using Chinese hamster ovary (CHO) cells engineered to express the putative Etx receptor, myelin and lymphocyte protein (MAL), suggest that amino acids important for Etx activity differ between species. In this study, we investigated the role of amino acids Y42, Y43 and H162, previously identified as important in Etx activity towards MDCK cells, in Etx activity towards CHO-human MAL (CHO-hMAL) cells, human red blood cells (hRBCs) and synthetic bilayers using site-directed mutants of Etx. We show that in CHO-hMAL cells Y42 is critical for Etx binding and not Y43 as in MDCK cells, indicating that surface exposed tyrosine residues in the receptor binding domain of Etx impact efficiency of cell binding to MAL-expressing cells in a species-specific manner. We also show that Etx mutant H162A was unable to lyse CHO-hMAL cells, lysed hRBCs, whilst it was able to form pores in synthetic bilayers, providing evidence of the complexity of Etx pore formation in different lipid environments. Full article
(This article belongs to the Special Issue Pore-Forming Toxin Interactions with the Membrane)
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