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Special Issue "Cellular Entry of Binary and Pore-Forming Bacterial Toxins"

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

Deadline for manuscript submissions: 30 July 2017

Special Issue Editor

Guest Editor
Dr. Alexey S. Ladokhin

Department of Biochemistry and Molecular Biology, The University of Kansas Medical Center, Kansas City, Kansas 66160-7421, USA
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Special Issue Information

Dear Colleagues,

Bridging cellular membranes is a key step in the pathogenic action of both binary (e.g., diphtheria, botulin, tetanus, anthrax) and pore-forming toxins (e.g., cytolysin A, α-hemolysin,  perfringolysin O). The former use their translocation domains, containing various structural motifs, to ensure efficient delivery of the toxic component into the host cell, while the latter act on the cellular membrane itself. In either case, the integrity of the membrane is compromised via targeted protein–lipid and protein–protein interactions triggered by specific signals, such as proteolytic cleavage or endosomal acidification. This Special Issue presents recent advances in characterizing functional, structural and thermodynamic aspects of the conformational switching and membrane interactions involved in the cellular entry of bacterial protein toxins. Deciphering the physicochemical principles underlying these processes is also a prerequisite for the use of protein engineering to develop toxin-based molecular vehicles capable of targeted delivery of therapeutic agents to tumors and other diseased tissues.

Apicomplexans are pathogenic protozoan parasites that can cause severe disease, including malaria and toxoplasmosis, in wide range of hosts. These parasites utilize pore-forming proteins that disrupt host cell membranes to either traverse host cells while migrating through tissues or egress from the parasite-containing vacuole after intracellular replication. This review will highlight recent insight gained from newly available three-dimensional structures of several pore forming required for apicomplexan cell traversal or egress. These structural advances suggest that parasite pore forming proteins use distinct mechanisms to disrupt host cell membranes and that lipid composition of target membrane can influence cytolytic activity.

Dr. Alexey S. Ladokhin
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 papers will be 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 single-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 1500 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

  • bacterial protein toxins
  • cellular uptake
  • toxin-membrane interactions
  • membrane permeabilization and translocation
  • conformational switching
  • toxin-based targeted delivery of therapeutic agents

Published Papers (1 paper)

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Research

Open AccessArticle The Vip3Ag4 Insecticidal Protoxin from Bacillus thuringiensis Adopts A Tetrameric Configuration That Is Maintained on Proteolysis
Toxins 2017, 9(5), 165; doi:10.3390/toxins9050165
Received: 17 January 2017 / Revised: 11 May 2017 / Accepted: 12 May 2017 / Published: 14 May 2017
PDF Full-text (3159 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
The Vip3 proteins produced during vegetative growth by strains of the bacterium Bacillus thuringiensis show insecticidal activity against lepidopteran insects with a mechanism of action that may involve pore formation and apoptosis. These proteins are promising supplements to our arsenal of insecticidal proteins,
[...] Read more.
The Vip3 proteins produced during vegetative growth by strains of the bacterium Bacillus thuringiensis show insecticidal activity against lepidopteran insects with a mechanism of action that may involve pore formation and apoptosis. These proteins are promising supplements to our arsenal of insecticidal proteins, but the molecular details of their activity are not understood. As a first step in the structural characterisation of these proteins, we have analysed their secondary structure and resolved the surface topology of a tetrameric complex of the Vip3Ag4 protein by transmission electron microscopy. Sites sensitive to proteolysis by trypsin are identified and the trypsin-cleaved protein appears to retain a similar structure as an octomeric complex comprising four copies each of the ~65 kDa and ~21 kDa products of proteolysis. This processed form of the toxin may represent the active toxin. The quality and monodispersity of the protein produced in this study make Vip3Ag4 a candidate for more detailed structural analysis using cryo-electron microscopy. Full article
(This article belongs to the Special Issue Cellular Entry of Binary and Pore-Forming Bacterial Toxins)
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