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Toxins
Special Issues
Pore Forming Proteins: Structure, Function and Applications
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Pore Forming Proteins: Structure, Function and Applications

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

Deadline for manuscript submissions: closed (31 March 2022) | Viewed by 4317

Special Issue Editors

Prof. Dr. Bart Hoogenboom

E-Mail Website
Guest Editor
Dept of Physics & Astronomy, UCL, London Centre for Nanotechnology, London, UK
Interests: Nanoscale Biophysics; Atomic Force Microscopy; Host-Pathogen Interactions
Dr. Michelle Dunstone

E-Mail Website
Guest Editor
Department of Biochemistry and Molecular Biology, Monash University, Melbourne 3800, Australia
Interests: pore forming proteins; pore forming toxins; cryo-EM; crystallography; structural biology; MACPF/CDC family; beta-pore forming proteins
Dr. Michael Landsberg

E-Mail Website
Guest Editor
School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Australia

Special Issue Information

Dear Colleagues, 

Pore-forming proteins are a class of proteins that self-assemble into ring-shaped oligomers and insert into membranes. They typically form a transmembrane channel that can lead to osmotically driven cell lysis or the delivery of toxins. Each pore-forming protein has a specific target or range of target cells, depending on its evolved function.

This Special Issue will explore the function and related mechanisms of pore-forming proteins from the cellular to the atomic level. It will further investigate how pore-forming proteins may be involved in disease, affecting a whole organism, as well as how they insert into cellular membranes by examining the time-resolved details of this process and their function in 4D. Finally, this Special Issue will discuss how pore-forming proteins facilitate the translocation of peptides and other solutes across membranes. An important topic of interest will be the established and potential biotechnological applications of pore-forming proteins.

Prof. Dr. Bart Hoogenboom
Dr. Michelle Dunstone
Dr. Michael Landsberg
Guest Editors

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 proteins
  • Pores
  • Transmembrane channels
  • Self-assembling complexes
  • Translocation

Published Papers (1 paper)

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Research

23 pages, 1901 KiB  
Article
Lipid-Binding Aegerolysin from Biocontrol Fungus Beauveria bassiana
by Nada Kraševec, Anastasija Panevska, Špela Lemež, Jaka Razinger, Kristina Sepčić, Gregor Anderluh and Marjetka Podobnik
Toxins 2021, 13(11), 820; https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13110820 - 20 Nov 2021
Cited by 6 | Viewed by 3122
Abstract
Fungi are the most common pathogens of insects and thus important regulators of their populations. Lipid-binding aegerolysin proteins, which are commonly found in the fungal kingdom, may be involved in several biologically relevant processes including attack and defense against other organisms. Aegerolysins act [...] Read more.
Fungi are the most common pathogens of insects and thus important regulators of their populations. Lipid-binding aegerolysin proteins, which are commonly found in the fungal kingdom, may be involved in several biologically relevant processes including attack and defense against other organisms. Aegerolysins act alone or together with membrane-attack-complex/perforin (MACPF)-like proteins to form transmembrane pores that lead to cell lysis. We performed an in-depth bioinformatics analysis of aegerolysins in entomopathogenic fungi and selected a candidate aegerolysin, beauveriolysin A (BlyA) from Beauveria bassiana. BlyA was expressed as a recombinant protein in Escherichia coli, and purified to further determine its functional and structural properties, including lipid-binding ability. Aegerolysins were found to be encoded in genomes of entomopathogenic fungi, such as Beauveria, Cordyceps, Metarhizium and Ophiocordyceps. Detailed bioinformatics analysis revealed that they are linked to MACPF-like genes in most genomes. We also show that BlyA interacts with an insect-specific membrane lipid. These results were placed in the context of other fungal and bacterial aegerolysins and their partner proteins. We believe that aegerolysins play a role in promoting the entomopathogenic and antagonistic activity of B. bassiana, which is an active ingredient of bioinsecticides. Full article
(This article belongs to the Special Issue Pore Forming Proteins: Structure, Function and Applications)
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