Advanced Proteomics as a Powerful Tool for Studying Bacterial Toxins

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

Deadline for manuscript submissions: closed (30 November 2020) | Viewed by 11505

Special Issue Editor


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Guest Editor
Avignon Université/INRA, SQPOV UMR408, Avignon, France, INRA, SQPOV UMR408, Avignon, France
Interests: microbiology; proteomics; metabolism; redox; toxins

Special Issue Information

Dear Colleagues,

Compared with genomics and transcriptomics, proteomics has the advantage of defining protein toxins that are differentially produced, not just purely transcriptionally regulated. It can also define toxins that are differentially located or secreted outside of the cell. In many cases, protein toxins that fall into these categories can be predicted from their sequences obtained directly by genome sequencing, but proteomics is quite able to show the presence of some unpredicted toxins. Furthermore, only proteomics can detect post-translational modifications (PTMs) of proteins. PTMs may potentially affect the activity, localization, and interactions of protein toxins with other proteins, and thus may modulate their function. The recent developments in mass spectrometry instrumentation, methods, and bioinformatics tools has enabled the identification and quantification of all the toxins of any producer and many of their PTMs.

This Special Issue will focus on proteomics as a toolbox for global toxin identification and quantification, as well as the determination of toxin PTMs. This powerful technology should help to tackle new challenges and to improve our understanding of the relationships between the repertoire of toxins and other virulence factors and the pathogenicity power of producers.

Prof. Dr. Catherine Duport
Guest Editor

Manuscript Submission Information

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Keywords

  • protein toxins
  • (meta)proteomics
  • quantitative analysis
  • post-translational modification
  • pathogenesis
  • mass spectrometry

Published Papers (3 papers)

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Research

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19 pages, 3235 KiB  
Article
Genomics and Proteomics Analyses Revealed Novel Candidate Pesticidal Proteins in a Lepidopteran-Toxic Bacillus thuringiensis Strain
by Ayda Khorramnejad, Joaquín Gomis-Cebolla, Reza Talaei-Hassanlouei, Yolanda Bel and Baltasar Escriche
Toxins 2020, 12(11), 673; https://doi.org/10.3390/toxins12110673 - 26 Oct 2020
Cited by 7 | Viewed by 2924
Abstract
Discovery and identification of novel insecticidal proteins in Bacillus thuringiensis (Bt) strains are of crucial importance for efficient biological control of pests and better management of insect resistance. In this study, the Bt strain KhF, toxic for Plodia interpunctella and Grapholita molesta larvae, [...] Read more.
Discovery and identification of novel insecticidal proteins in Bacillus thuringiensis (Bt) strains are of crucial importance for efficient biological control of pests and better management of insect resistance. In this study, the Bt strain KhF, toxic for Plodia interpunctella and Grapholita molesta larvae, underwent genomics and proteomics analyses to achieve a better understanding of the bases of its pathogenicity. The whole-genome sequencing results revealed that the KhF strain contained nine coding sequences with homologies to Bt insecticidal genes. The lepidopteran toxic mixture of spores and crystals of this Bt strain was subjected to liquid chromatography and tandem mass spectrometry (LC-MS/MS) to assess the protein composition. The results of the proteomic analyses, combined with the toxin gene sequences, revealed that two of the main components of the crystals were two new candidate pesticidal proteins, named KhFA and KhFB. These proteins showed a similarity lower than 36% to the other known Bt toxins. The phylogenetic analysis showed that the KhFA and KhFB grouped with the newly denominated Xpp and Mpp (former ETX/Mtx) pesticidal protein groups, respectively. Altogether, this study has led to the discovery of two novel candidate pesticidal toxins in the lepidopteran toxic KhF strain. Full article
(This article belongs to the Special Issue Advanced Proteomics as a Powerful Tool for Studying Bacterial Toxins)
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17 pages, 2188 KiB  
Article
Bacillus cereus Decreases NHE and CLO Exotoxin Synthesis to Maintain Appropriate Proteome Dynamics During Growth at Low Temperature
by Catherine Duport, Ludivine Rousset, Béatrice Alpha-Bazin and Jean Armengaud
Toxins 2020, 12(10), 645; https://doi.org/10.3390/toxins12100645 - 6 Oct 2020
Cited by 7 | Viewed by 3045
Abstract
Cellular proteomes and exoproteomes are dynamic, allowing pathogens to respond to environmental conditions to sustain growth and virulence. Bacillus cereus is an important food-borne pathogen causing intoxication via emetic toxin and/or multiple protein exotoxins. Here, we compared the dynamics of the cellular proteome [...] Read more.
Cellular proteomes and exoproteomes are dynamic, allowing pathogens to respond to environmental conditions to sustain growth and virulence. Bacillus cereus is an important food-borne pathogen causing intoxication via emetic toxin and/or multiple protein exotoxins. Here, we compared the dynamics of the cellular proteome and exoproteome of emetic B. cereus cells grown at low (16 °C) and high (30 °C) temperature. Tandem mass spectrometry (MS/MS)-based shotgun proteomics analysis identified 2063 cellular proteins and 900 extracellular proteins. Hierarchical clustering following principal component analysis indicated that in B. cereus the abundance of a subset of these proteins—including cold-stress responders, and exotoxins non-hemolytic enterotoxin (NHE) and hemolysin I (cereolysin O (CLO))—decreased at low temperature, and that this subset governs the dynamics of the cellular proteome. NHE, and to a lesser extent CLO, also contributed significantly to exoproteome dynamics; with decreased abundances in the low-temperature exoproteome, especially in late growth stages. Our data therefore indicate that B. cereus may reduce its production of secreted protein toxins to maintain appropriate proteome dynamics, perhaps using catabolite repression to conserve energy for growth in cold-stress conditions, at the expense of virulence. Full article
(This article belongs to the Special Issue Advanced Proteomics as a Powerful Tool for Studying Bacterial Toxins)
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Review

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19 pages, 1278 KiB  
Review
Exoproteomics for Better Understanding Pseudomonas aeruginosa Virulence
by Salomé Sauvage and Julie Hardouin
Toxins 2020, 12(9), 571; https://doi.org/10.3390/toxins12090571 - 4 Sep 2020
Cited by 17 | Viewed by 5050
Abstract
Pseudomonas aeruginosa is the most common human opportunistic pathogen associated with nosocomial diseases. In 2017, the World Health Organization has classified P. aeruginosa as a critical agent threatening human health, and for which the development of new treatments is urgently necessary. One interesting [...] Read more.
Pseudomonas aeruginosa is the most common human opportunistic pathogen associated with nosocomial diseases. In 2017, the World Health Organization has classified P. aeruginosa as a critical agent threatening human health, and for which the development of new treatments is urgently necessary. One interesting avenue is to target virulence factors to understand P. aeruginosa pathogenicity. Thus, characterising exoproteins of P. aeruginosa is a hot research topic and proteomics is a powerful approach that provides important information to gain insights on bacterial virulence. The aim of this review is to focus on the contribution of proteomics to the studies of P. aeruginosa exoproteins, highlighting its relevance in the discovery of virulence factors, post-translational modifications on exoproteins and host-pathogen relationships. Full article
(This article belongs to the Special Issue Advanced Proteomics as a Powerful Tool for Studying Bacterial Toxins)
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