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Special Issue "Bacterial Protein Toxins"

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

Deadline for manuscript submissions: closed (30 November 2009)

Special Issue Editors

Guest Editor
Dr. Yasuhiko Horiguchi

Research Institute for Microbial Diseases, Osaka University, Yamada-oka 3-1, Suita, Osaka 565-0871, Japan
Website | E-Mail
Fax: + 81 6 6879 8283
Interests: structure and domain organization of proteins; cell-to -cell or intracellular signaling; receptors for toxins; membrane-damaging toxins
Guest Editor
Prof. Dr. Yukako Fujinaga

Department of Bacteriology, Graduate School of Medical Sciences, Kanazawa University, Kanazawa, 920-8640, Japan
Website | E-Mail
Fax: +81 6 6879 4252
Interests: bacterial protein toxins; enterotoxins; mechanism of toxicity; interaction of toxins with epithelial cell barriers

Special Issue Information

Dear Colleagues,

Bacterial protein toxins play an important role in infectious diseases. Several are highly potent human poisons, such as botulinum, tetanus, Shiga, and diphtheria toxins. These toxins are multi-functional proteins that are self-programmed to reach their target organs and/or enter cells. Another set of toxins is called effector, which is directly delivered into the cell by type III/IV mechanisms. To exert their potency, many of them interact specifically with key components of the cell. Thus, these toxins are not only responsible for disease, but also provide a powerful set of tools with which to elucidate complicated machinery of the cell system. In addition, some toxins can be used medicinally to treat human diseases, such as Botox (botulinum toxin) in recent years. This issue of Toxins will deal with major achievements and recent exciting discoveries in protein toxins and effectors produced by bacteria, including three-dimensional structures, structure-activity relationships, toxin receptors, toxin substrates, toxin trafficking, and clinical applications.

Yukako Fujinaga, Ph. D.
Yasuhiko Horiguchi, Ph. D.
Guest Editors

Keywords

  • exotoxin
  • virulence factor
  • enzyme
  • pore formation
  • effector protein

Published Papers (8 papers)

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Research

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Open AccessArticle Escherichia coli Cytotoxic Necrotizing Factor 1 (CNF1): Toxin Biology, in Vivo Applications and Therapeutic Potential
Toxins 2010, 2(2), 283-296; doi:10.3390/toxins2020282
Received: 4 February 2010 / Revised: 20 February 2010 / Accepted: 20 February 2010 / Published: 23 February 2010
Cited by 10
Abstract
CNF1 is a protein toxin produced by certain pathogenic strains of Escherichia coli. It permanently activates the regulatory Rho, Rac, and Cdc42 GTPases in eukaryotic cells, by deamidation of a glutamine residue. This modification promotes new activities in cells, such as gene
[...] Read more.
CNF1 is a protein toxin produced by certain pathogenic strains of Escherichia coli. It permanently activates the regulatory Rho, Rac, and Cdc42 GTPases in eukaryotic cells, by deamidation of a glutamine residue. This modification promotes new activities in cells, such as gene transcription, cell proliferation and survival. Since the Rho GTPases play a pivotal role also in several processes in vivo, the potentiality of CNF1 to act as a new pharmacological tool has been explored in experimental animals and in diverse pathological contexts. In this review, we give an update overview on the potential in vivo applications of CNF1. Full article
(This article belongs to the Special Issue Bacterial Protein Toxins)
Open AccessArticle The Versatility of the Helicobacter pylori Vacuolating Cytotoxin VacA in Signal Transduction and Molecular Crosstalk
Toxins 2010, 2(1), 69-92; doi:10.3390/toxins2010069
Received: 3 December 2009 / Revised: 31 December 2009 / Accepted: 14 January 2010 / Published: 15 January 2010
Cited by 13
Abstract
By modulating important properties of eukaryotic cells, many bacterial protein toxins highjack host signalling pathways to create a suitable niche for the pathogen to colonize and persist. Helicobacter pylori VacA is paradigm of pore-forming toxins which contributes to the pathogenesis of peptic ulceration.
[...] Read more.
By modulating important properties of eukaryotic cells, many bacterial protein toxins highjack host signalling pathways to create a suitable niche for the pathogen to colonize and persist. Helicobacter pylori VacA is paradigm of pore-forming toxins which contributes to the pathogenesis of peptic ulceration. Several cellular receptors have been described for VacA, which exert different effects on epithelial and immune cells. The crystal structure of VacA p55 subunit might be important for elucidating details of receptor interaction and pore formation. Here we discuss the multiple signalling activities of this important toxin and the molecular crosstalk between VacA and other virulence factors. Full article
(This article belongs to the Special Issue Bacterial Protein Toxins)

Review

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Open AccessReview Clostridial Neurotoxins: Mechanism of SNARE Cleavage and Outlook on Potential Substrate Specificity Reengineering
Toxins 2010, 2(4), 665-682; doi:10.3390/toxins2040665
Received: 7 February 2010 / Revised: 30 March 2010 / Accepted: 9 April 2010 / Published: 13 April 2010
Cited by 21
Abstract
The clostridial neurotoxin family consists of tetanus neurotoxin and seven distinct botulinum neurotoxins which cause the diseases tetanus and botulism. The extreme potency of these toxins primarily relies not only on their ability to specifically enter motoneurons but also on the activity their
[...] Read more.
The clostridial neurotoxin family consists of tetanus neurotoxin and seven distinct botulinum neurotoxins which cause the diseases tetanus and botulism. The extreme potency of these toxins primarily relies not only on their ability to specifically enter motoneurons but also on the activity their catalytic domains display inside presynaptic motoneuronal terminals. Subsequent to neurotoxin binding and endocytosis the catalytic domains become translocated across endosomal membranes and proteolyze unique peptide bonds of one of three soluble N-ethylmaleimide-sensitive fusion protein attachment receptors (SNAREs), vesicle associated membrane protein/synaptobrevin, synaptosome associated protein of 25 kDa, or syntaxin. As these substrate proteins are core components of the vesicular membrane fusion apparatus, cleavage of any of the substrate molecules results in the blockade of neurotransmitter release. This review summarizes the present knowledge about the molecular basis of the specific substrate recognition and cleavage mechanism and assesses the feasibility of reengineering catalytic domains to hydrolyze non-substrate members of the three SNARE families in order to expand the therapeutic application of botulinum neurotoxins. Full article
(This article belongs to the Special Issue Bacterial Protein Toxins)
Open AccessReview Escherichia coli Subtilase Cytotoxin
Toxins 2010, 2(2), 215-228; doi:10.3390/toxins2020215
Received: 1 December 2009 / Revised: 13 January 2010 / Accepted: 27 January 2010 / Published: 28 January 2010
Cited by 20
Abstract
Subtilase cytotoxin (SubAB) is the prototype of a new AB5 toxin family produced by a subset of Shiga toxigenic Escherichia coli (STEC) strains. Its A subunit is a subtilase-like serine protease and cytotoxicity for eukaryotic cells is due to a highly specific,
[...] Read more.
Subtilase cytotoxin (SubAB) is the prototype of a new AB5 toxin family produced by a subset of Shiga toxigenic Escherichia coli (STEC) strains. Its A subunit is a subtilase-like serine protease and cytotoxicity for eukaryotic cells is due to a highly specific, single-site cleavage of BiP/GRP78, an essential Hsp70 family chaperone located in the endoplasmic reticulum (ER). This cleavage triggers a severe and unresolved ER stress response, ultimately triggering apoptosis. The B subunit has specificity for glycans terminating in the sialic acid N-glycolylneuraminic acid. Although its actual role in human disease pathogenesis is yet to be established, SubAB is lethal for mice and induces pathological features overlapping those seen in the haemolytic uraemic syndrome, a life-threatening complication of STEC infection. The toxin is also proving to be a useful tool for probing the role of BiP and ER stress in a variety of cellular functions. Full article
(This article belongs to the Special Issue Bacterial Protein Toxins)
Open AccessReview Pasteurella multocida Toxin Activates Various Heterotrimeric G Proteins by Deamidation
Toxins 2010, 2(2), 205-214; doi:10.3390/toxins2020205
Received: 24 November 2009 / Revised: 19 January 2010 / Accepted: 27 January 2010 / Published: 28 January 2010
Cited by 9
Abstract
Pasteurella multocida produces a 146-kDa protein toxin (Pasteurella multocida toxin, PMT), which stimulates diverse cellular signal transduction pathways by activating heterotrimeric G proteins. PMT deamidates a conserved glutamine residue of the α-subunit of heterotrimeric G proteins that is essential for GTP-hydrolysis, thereby
[...] Read more.
Pasteurella multocida produces a 146-kDa protein toxin (Pasteurella multocida toxin, PMT), which stimulates diverse cellular signal transduction pathways by activating heterotrimeric G proteins. PMT deamidates a conserved glutamine residue of the α-subunit of heterotrimeric G proteins that is essential for GTP-hydrolysis, thereby arresting the G protein in the active state. The toxin substrates are Gαq13 and the Gαi-family proteins. Activation of these α-subunits causes stimulation of phospholipase Cβ, Rho-guanine nucleotide exchange factors or inhibition of adenylyl cyclase. This article provides the current knowledge on PMT concerning the structure-function analysis based on the crystal structure and recently elucidated molecular mode of action. Furthermore, the impact of PMT on cellular signaling is discussed. Full article
(This article belongs to the Special Issue Bacterial Protein Toxins)
Open AccessReview Cytotoxic Necrotizing Factors (CNFs)−A Growing Toxin Family
Toxins 2010, 2(1), 116-127; doi:10.3390/toxins2010116
Received: 14 December 2009 / Revised: 15 January 2010 / Accepted: 20 January 2010 / Published: 21 January 2010
Cited by 13
Abstract
The Escherichia coli Cytotoxic Necrotizing Factors, CNF1, CNF2, CNF3 and CNFY from Yersinia pseudotuberculosis belong to a family of deamidating toxins. CNFs deamidate glutamine 63/61 in the switch II region of Rho GTPases that is essential for GTP hydrolysing activity. Deamidation leads to
[...] Read more.
The Escherichia coli Cytotoxic Necrotizing Factors, CNF1, CNF2, CNF3 and CNFY from Yersinia pseudotuberculosis belong to a family of deamidating toxins. CNFs deamidate glutamine 63/61 in the switch II region of Rho GTPases that is essential for GTP hydrolysing activity. Deamidation leads to constitutive activation of Rho GTPases. However, cellular mechanisms like proteasomal degradation of the activated Rho proteins restrict the action of the GTPases. This review describes the differences between the toxin family members concerning expression, cellular entry and substrate specificity. Full article
(This article belongs to the Special Issue Bacterial Protein Toxins)
Open AccessReview Clostridium perfringens Iota-Toxin: Structure and Function
Toxins 2009, 1(2), 208-228; doi:10.3390/toxins1020208
Received: 27 November 2009 / Revised: 16 December 2009 / Accepted: 21 December 2009 / Published: 23 December 2009
Cited by 19
Abstract
Clostridium perfringens iota-toxin is composed of the enzyme component (Ia) and the binding component (Ib). Ib binds to receptor on targeted cells and translocates Ia into the cytosol of the cells. Ia ADP-ribosylates actin, resulting in cell rounding and death. Comparisons of the
[...] Read more.
Clostridium perfringens iota-toxin is composed of the enzyme component (Ia) and the binding component (Ib). Ib binds to receptor on targeted cells and translocates Ia into the cytosol of the cells. Ia ADP-ribosylates actin, resulting in cell rounding and death. Comparisons of the deduced amino acid sequence from the gene and three-dimensional structure of Ia with those of ADP-ribosylating toxins (ARTs) suggests that there is striking structural similarity among these toxins. Our objectives are to review the recent advances in the character, structure-function, and the mode of action of iota-toxin by consideration of the findings about ARTs. Full article
(This article belongs to the Special Issue Bacterial Protein Toxins)
Open AccessReview Actin Crosslinking Toxins of Gram-Negative Bacteria
Toxins 2009, 1(2), 123-133; doi:10.3390/toxins1020123
Received: 2 November 2009 / Revised: 13 November 2009 / Accepted: 26 November 2009 / Published: 1 December 2009
Cited by 13
Abstract
Actin crosslinking toxins produced by Gram-negative bacteria represent a small but unique class of bacterial protein toxins. For each of these toxins, a discrete actin crosslinking domain (ACD) that is a distant member of the ATP-dependent glutamine synthetase family of protein ligases is
[...] Read more.
Actin crosslinking toxins produced by Gram-negative bacteria represent a small but unique class of bacterial protein toxins. For each of these toxins, a discrete actin crosslinking domain (ACD) that is a distant member of the ATP-dependent glutamine synthetase family of protein ligases is translocated to the eukaryotic cell cytosol. This domain then incorporates a glutamate-lysine crosslink between actin monomers, resulting in destruction of the actin cytoskeleton. Recent studies argue that the function of these toxins during infection is not destruction of epithelial layers, but rather may specifically target phagocytic cells to promote survival of bacteria after the onset of innate immune defenses. This review will summarize key experiments performed over the past 10 years to reveal the function of these toxins. Full article
(This article belongs to the Special Issue Bacterial Protein Toxins)

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