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Special Issue "Pasteurella multocida and Its Virulence Factors"

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

Deadline for manuscript submissions: closed (30 June 2017)

Special Issue Editor

Guest Editor
Dr. Katharina Kubatzky

Dept. of Medical Microbiology and Hygiene, Heidelberg University Hospital, Germany
Website | E-Mail
Phone: +49-6221-5638361
Fax: +49-6221-5633749
Interests: mechanisms of bacterial immune evasion; the function of Rho GTPases; cytokine receptors in the innate immune system

Special Issue Information

Dear Colleagues,

Bacterial toxins can be classified into endotoxins and exotoxins. While the endotoxin lipopolysaccharide is an integral part of the cell wall of all gram-negative bacteria, exotoxins are proteins that possess a catalytic activity towards their respective target cell. Pasteurella multocida can infect a broad range of animals causing various diseases with specific syndromes. While atrophic rhinitis of pigs is connected specifically to toxigenic Pasteurella multocida strains that express the exotoxin PMT (Pasteurella multocida toxin), the pathogenic mechanisms for other diseases are less well understood, although LPS is required for pathogenesis. The host’s immune system recognizes LPS through the pattern recognition receptor toll like receptor (TLR) 4. Other emerging virulence factors that can be detected by the endotoxin receptor TLR4 are proteins, such as outer membrane proteins (Omp), fimbriae or porins. These factors are discussed as potential candidates to generate efficient vaccines.

This Special Issue aims to summarize what is known about the interaction of Pasteurella multocida endotoxins and its exotoxin with cells of the immune system. We welcome articles (research or review) that center on the effects of LPS, PMT, or other emerging virulence factors and the generation of vaccines, respectively.

Dr. Katharina Hieke-Kubatzky
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

  • Pasteurella multocida
  • pathogenicity factor
  • Pasteurella multocida toxin
  • atrophic rhinitis
  • endotoxin
  • vaccination

Published Papers (2 papers)

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Research

Open AccessArticle Auranofin Inhibits the Enzyme Activity of Pasteurella multocida Toxin PMT in Human Cells and Protects Cells from Intoxication
Toxins 2017, 9(1), 32; doi:10.3390/toxins9010032
Received: 16 November 2016 / Revised: 23 December 2016 / Accepted: 10 January 2017 / Published: 13 January 2017
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Abstract
The AB-type protein toxin from Pasteurella multocida (PMT) contains a functionally important disulfide bond within its catalytic domain, which must be cleaved in the host cell cytosol to render the catalytic domain of PMT into its active conformation. Here, we found that the
[...] Read more.
The AB-type protein toxin from Pasteurella multocida (PMT) contains a functionally important disulfide bond within its catalytic domain, which must be cleaved in the host cell cytosol to render the catalytic domain of PMT into its active conformation. Here, we found that the reductive potential of the cytosol of target cells, and more specifically, the activity of the thioredoxin reductase (TrxR) is crucial for this process. This was demonstrated by the strong inhibitory effect of the pharmacological TrxR inhibitor auranofin, which inhibited the intoxication of target cells with PMT, as determined by analyzing the PMT-catalyzed deamidation of GTP-binding proteins (G-proteins) in the cytosol of cells. The amount of endogenous substrate levels modified by PMT in cells pretreated with auranofin was reduced compared to cells treated with PMT alone. Auranofin had no inhibitory effect on the activity of the catalytic domain of constitutively active PMT in vitro, demonstrating that auranofin did not directly inhibit PMT activity, but interferes with the mode of action of PMT in cells. In conclusion, the results show that TrxR is crucial for the mode of action of PMT in mammalian cells, and that the drug auranofin can serve as an efficient inhibitor, which might be a starting point for novel therapeutic options against toxin-associated diseases. Full article
(This article belongs to the Special Issue Pasteurella multocida and Its Virulence Factors)
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Figure 1

Open AccessArticle Selective Membrane Redistribution and Depletion of Gαq-Protein by Pasteurella multocida Toxin
Toxins 2016, 8(8), 233; doi:10.3390/toxins8080233
Received: 15 June 2016 / Revised: 22 July 2016 / Accepted: 25 July 2016 / Published: 1 August 2016
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Abstract
Pasteurella multocida toxin (PMT), the major virulence factor responsible for zoonotic atrophic rhinitis, is a protein deamidase that activates the alpha subunit of heterotrimeric G proteins. Initial activation of G alpha-q-coupled phospholipase C-beta-1 signaling by PMT is followed by uncoupling of G alpha-q-dependent
[...] Read more.
Pasteurella multocida toxin (PMT), the major virulence factor responsible for zoonotic atrophic rhinitis, is a protein deamidase that activates the alpha subunit of heterotrimeric G proteins. Initial activation of G alpha-q-coupled phospholipase C-beta-1 signaling by PMT is followed by uncoupling of G alpha-q-dependent signaling, causing downregulation of downstream calcium and mitogenic signaling pathways. Here, we show that PMT decreases endogenous and exogenously expressed G alpha-q protein content in host cell plasma membranes and in detergent resistant membrane (DRM) fractions. This membrane depletion of G alpha-q protein was dependent upon the catalytic activity of PMT. Results indicate that PMT-modified G alpha-q redistributes within the host cell membrane from the DRM fraction into the soluble membrane and cytosolic fractions. In contrast, PMT had no affect on G alpha-s or G beta protein levels, which are not substrate targets of PMT. PMT also had no affect on G alpha-11 levels, even though G alpha-11 can serve as a substrate for deamidation by PMT, suggesting that membrane depletion of PMT-modified G-alpha-q has specificity. Full article
(This article belongs to the Special Issue Pasteurella multocida and Its Virulence Factors)
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