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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
Website | E-Mail

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

No papers have been published in this special issue yet.

Journal Contact

MDPI AG
Toxins Editorial Office
St. Alban-Anlage 66, 4052 Basel, Switzerland
E-Mail: 
Tel. +41 61 683 77 34
Fax: +41 61 302 89 18
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