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Toxins
Special Issues
Diphtheria Toxin
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Diphtheria Toxin

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

Deadline for manuscript submissions: closed (20 September 2014) | Viewed by 38813

Special Issue Editor

Prof. Dr. Daniel Gillet

E-Mail Website
Guest Editor
Section of Molecular Engineering for Health (SIMoS), JOLIOT, CEA, Université Paris-Saclay, F-91191 Gif Sur Yvette, France
Interests: bacterial toxins; diphtheria toxin; ricin toxin; Shiga toxins; botulinum toxins; intracellular trafficking; biodefense; toxin inhibitors; antitoxin drug development
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Diphtheria toxin was the first bacterial toxin to be discovered. It is among the best-known bacterial toxins acting inside cells. This exquisitely sophisticated piece of molecular machinery regroups three main distinct activities, each relying on very different biological properties: the recognition of a ubiquitous cell-surface protein in order to get internalized by cells, the capacity to cross the membrane barrier of intracellular trafficking compartments and a highly specific catalytic activity capable of neutralizing protein synthesis. Anti-diphtheria toxin vaccination with toxoid started almost a century ago and still has a tremendous impact on public health, preventing each year the deaths of tens of thousands of children. More recently, sophisticated protein engineering of diphtheria toxin led to many biotechnological applications for research, and to the first approved anti-tumor targeted toxin for the treatment of lymphomas. However, there is still a lot to discover about the molecular details of the various steps of the mechanism of action of the toxin, as modern biology enables to understand molecular events at atomic resolution and in living cells. There is little doubt that in the future, several new biological drugs will be based on modified fragments of this fascinating protein.

Dr. Daniel Gillet
Guest Editor

Submission

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. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as 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 refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on theInstructions 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 800 CHF (Swiss Francs). English correction and/or formatting fees of 250 CHF (Swiss Francs) will be charged in certain cases for those articles accepted for publication that require extensive additional formatting and/or English corrections.

Keywords

  • diphtheria toxin
  • toxoid
  • targeted toxin
  • membrane translocation
  • HB-EGF
  • ADP-ribosylation

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Published Papers (3 papers)

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2208 KiB  
Review
pH-Triggered Conformational Switching along the Membrane Insertion Pathway of the Diphtheria Toxin T-Domain
by Alexey S. Ladokhin
Toxins 2013, 5(8), 1362-1380; https://doi.org/10.3390/toxins5081362 - 6 Aug 2013
Cited by 54 | Viewed by 12287
Abstract
The translocation (T)-domain plays a key role in the action of diphtheria toxin and is responsible for transferring the catalytic domain across the endosomal membrane into the cytosol in response to acidification. Deciphering the molecular mechanism of pH-dependent refolding and membrane insertion of [...] Read more.
The translocation (T)-domain plays a key role in the action of diphtheria toxin and is responsible for transferring the catalytic domain across the endosomal membrane into the cytosol in response to acidification. Deciphering the molecular mechanism of pH-dependent refolding and membrane insertion of the T-domain, which is considered to be a paradigm for cell entry of other bacterial toxins, reveals general physicochemical principles underlying membrane protein assembly and signaling on membrane interfaces. Structure-function studies along the T-domain insertion pathway have been affected by the presence of multiple conformations at the same time, which hinders the application of high-resolution structural techniques. Here, we review recent progress in structural, functional and thermodynamic studies of the T-domain archived using a combination of site-selective fluorescence labeling with an array of spectroscopic techniques and computer simulations. We also discuss the principles of conformational switching along the insertion pathway revealed by studies of a series of T-domain mutants with substitutions of histidine residues. Full article
(This article belongs to the Special Issue Diphtheria Toxin)
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927 KiB  
Review
Heparin-Binding Epidermal Growth Factor-like Growth Factor/Diphtheria Toxin Receptor in Normal and Neoplastic Hematopoiesis
by Fabrizio Vinante and Antonella Rigo
Toxins 2013, 5(6), 1180-1201; https://doi.org/10.3390/toxins5061180 - 18 Jun 2013
Cited by 35 | Viewed by 11405
Abstract
Heparin-binding EGF-like growth factor (HB-EGF) belongs to the EGF family of growth factors. It is biologically active either as a molecule anchored to the membrane or as a soluble form released by proteolytic cleavage of the extracellular domain. HB-EGF is involved in relevant [...] Read more.
Heparin-binding EGF-like growth factor (HB-EGF) belongs to the EGF family of growth factors. It is biologically active either as a molecule anchored to the membrane or as a soluble form released by proteolytic cleavage of the extracellular domain. HB-EGF is involved in relevant physiological and pathological processes spanning from proliferation and apoptosis to morphogenesis. We outline here the main activities of HB-EGF in connection with normal or neoplastic differentiative or proliferative events taking place primitively in the hematopoietic microenvironment. Full article
(This article belongs to the Special Issue Diphtheria Toxin)
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1001 KiB  
Brief Report
Insights into Diphthamide, Key Diphtheria Toxin Effector
by Wael Abdel-Fattah, Viktor Scheidt, Shanow Uthman, Michael J. R. Stark and Raffael Schaffrath
Toxins 2013, 5(5), 958-968; https://doi.org/10.3390/toxins5050958 - 3 May 2013
Cited by 21 | Viewed by 13469
Abstract
Diphtheria toxin (DT) inhibits eukaryotic translation elongation factor 2 (eEF2) by ADP-ribosylation in a fashion that requires diphthamide, a modified histidine residue on eEF2. In budding yeast, diphthamide formation involves seven genes, DPH1-DPH7. In an effort to further study diphthamide synthesis and [...] Read more.
Diphtheria toxin (DT) inhibits eukaryotic translation elongation factor 2 (eEF2) by ADP-ribosylation in a fashion that requires diphthamide, a modified histidine residue on eEF2. In budding yeast, diphthamide formation involves seven genes, DPH1-DPH7. In an effort to further study diphthamide synthesis and interrelation among the Dph proteins, we found, by expression in E. coli and co-immune precipitation in yeast, that Dph1 and Dph2 interact and that they form a complex with Dph3. Protein-protein interaction mapping shows that Dph1-Dph3 complex formation can be dissected by progressive DPH1 gene truncations. This identifies N- and C-terminal domains on Dph1 that are crucial for diphthamide synthesis, DT action and cytotoxicity of sordarin, another microbial eEF2 inhibitor. Intriguingly, dph1 truncation mutants are sensitive to overexpression of DPH5, the gene necessary to synthesize diphthine from the first diphthamide pathway intermediate produced by Dph1-Dph3. This is in stark contrast to dph6 mutants, which also lack the ability to form diphthamide but are resistant to growth inhibition by excess Dph5 levels. As judged from site-specific mutagenesis, the amidation reaction itself relies on a conserved ATP binding domain in Dph6 that, when altered, blocks diphthamide formation and confers resistance to eEF2 inhibition by sordarin. Full article
(This article belongs to the Special Issue Diphtheria Toxin)
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