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The Food Poisoning Toxins of Bacillus Cereus
toxins Review The Food Poisoning Toxins of Bacillus cereus Richard Dietrich 1,†, Nadja Jessberger 1,*,†, Monika Ehling-Schulz 2 , Erwin Märtlbauer 1 and Per Einar Granum 3 1 Department of Veterinary Sciences, Faculty of Veterinary Medicine, Ludwig Maximilian University of Munich, Schönleutnerstr. 8, 85764 Oberschleißheim, Germany; [email protected] (R.D.); [email protected] (E.M.) 2 Department of Pathobiology, Functional Microbiology, Institute of Microbiology, University of Veterinary Medicine Vienna, 1210 Vienna, Austria; [email protected] 3 Department of Food Safety and Infection Biology, Faculty of Veterinary Medicine, Norwegian University of Life Sciences, P.O. Box 5003 NMBU, 1432 Ås, Norway; [email protected] * Correspondence: [email protected] † These authors have contributed equally to this work. Abstract: Bacillus cereus is a ubiquitous soil bacterium responsible for two types of food-associated gastrointestinal diseases. While the emetic type, a food intoxication, manifests in nausea and vomiting, food infections with enteropathogenic strains cause diarrhea and abdominal pain. Causative toxins are the cyclic dodecadepsipeptide cereulide, and the proteinaceous enterotoxins hemolysin BL (Hbl), nonhemolytic enterotoxin (Nhe) and cytotoxin K (CytK), respectively. This review covers the current knowledge on distribution and genetic organization of the toxin genes, as well as mechanisms of enterotoxin gene regulation and toxin secretion. In this context, the exceptionally high variability of toxin production between single strains is highlighted. In addition, the mode of action of the pore-forming enterotoxins and their effect on target cells is described in detail. The main focus of this review are the two tripartite enterotoxin complexes Hbl and Nhe, but the latest findings on cereulide and CytK are also presented, as well as methods for toxin detection, and the contribution of further putative virulence factors to the diarrheal disease. -
Rapid and Simultaneous Detection of Ricin, Staphylococcal Enterotoxin B
Analyst PAPER View Article Online View Journal | View Issue Rapid and simultaneous detection of ricin, staphylococcal enterotoxin B and saxitoxin by Cite this: Analyst,2014,139, 5885 chemiluminescence-based microarray immunoassay† a a b b c c A. Szkola, E. M. Linares, S. Worbs, B. G. Dorner, R. Dietrich, E. Martlbauer,¨ R. Niessnera and M. Seidel*a Simultaneous detection of small and large molecules on microarray immunoassays is a challenge that limits some applications in multiplex analysis. This is the case for biosecurity, where fast, cheap and reliable simultaneous detection of proteotoxins and small toxins is needed. Two highly relevant proteotoxins, ricin (60 kDa) and bacterial toxin staphylococcal enterotoxin B (SEB, 30 kDa) and the small phycotoxin saxitoxin (STX, 0.3 kDa) are potential biological warfare agents and require an analytical tool for simultaneous detection. Proteotoxins are successfully detected by sandwich immunoassays, whereas Creative Commons Attribution-NonCommercial 3.0 Unported Licence. competitive immunoassays are more suitable for small toxins (<1 kDa). Based on this need, this work provides a novel and efficient solution based on anti-idiotypic antibodies for small molecules to combine both assay principles on one microarray. The biotoxin measurements are performed on a flow-through chemiluminescence microarray platform MCR3 in 18 minutes. The chemiluminescence signal was Received 18th February 2014 amplified by using a poly-horseradish peroxidase complex (polyHRP), resulting in low detection limits: Accepted 3rd September 2014 2.9 Æ 3.1 mgLÀ1 for ricin, 0.1 Æ 0.1 mgLÀ1 for SEB and 2.3 Æ 1.7 mgLÀ1 for STX. The developed multiplex DOI: 10.1039/c4an00345d system for the three biotoxins is completely novel, relevant in the context of biosecurity and establishes www.rsc.org/analyst the basis for research on anti-idiotypic antibodies for microarray immunoassays. -
Clostridium Perfringens Enterotoxin: the Toxin Forms Highly Cation-Selective Channels in Lipid Bilayers Roland Benz, Michel Popoff
Clostridium perfringens Enterotoxin: The Toxin Forms Highly Cation-Selective Channels in Lipid Bilayers Roland Benz, Michel Popoff To cite this version: Roland Benz, Michel Popoff. Clostridium perfringens Enterotoxin: The Toxin Forms Highly Cation- Selective Channels in Lipid Bilayers. Toxins, MDPI, 2018, 10 (9), pp.341. 10.3390/toxins10090341. pasteur-02448636 HAL Id: pasteur-02448636 https://hal-pasteur.archives-ouvertes.fr/pasteur-02448636 Submitted on 22 Jan 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Distributed under a Creative Commons Attribution| 4.0 International License toxins Article Clostridium perfringens Enterotoxin: The Toxin Forms Highly Cation-Selective Channels in Lipid Bilayers Roland Benz 1 ID and Michel R. Popoff 2,* 1 Department of Life Sciences and Chemistry, Jacobs University, Campusring 1, 28759 Bremen, Germany; [email protected] 2 Bacterial Toxins, Institut Pasteur, 28 rue du Dr Roux, 75015 Paris, France * Correspondence: [email protected] Received: 30 July 2018; Accepted: 14 August 2018; Published: 22 August 2018 Abstract: One of the numerous toxins produced by Clostridium perfringens is Clostridium perfringens enterotoxin (CPE), a polypeptide with a molecular mass of 35.5 kDa exhibiting three different domains. -
Biological Toxins As the Potential Tools for Bioterrorism
International Journal of Molecular Sciences Review Biological Toxins as the Potential Tools for Bioterrorism Edyta Janik 1, Michal Ceremuga 2, Joanna Saluk-Bijak 1 and Michal Bijak 1,* 1 Department of General Biochemistry, Faculty of Biology and Environmental Protection, University of Lodz, Pomorska 141/143, 90-236 Lodz, Poland; [email protected] (E.J.); [email protected] (J.S.-B.) 2 CBRN Reconnaissance and Decontamination Department, Military Institute of Chemistry and Radiometry, Antoniego Chrusciela “Montera” 105, 00-910 Warsaw, Poland; [email protected] * Correspondence: [email protected] or [email protected]; Tel.: +48-(0)426354336 Received: 3 February 2019; Accepted: 3 March 2019; Published: 8 March 2019 Abstract: Biological toxins are a heterogeneous group produced by living organisms. One dictionary defines them as “Chemicals produced by living organisms that have toxic properties for another organism”. Toxins are very attractive to terrorists for use in acts of bioterrorism. The first reason is that many biological toxins can be obtained very easily. Simple bacterial culturing systems and extraction equipment dedicated to plant toxins are cheap and easily available, and can even be constructed at home. Many toxins affect the nervous systems of mammals by interfering with the transmission of nerve impulses, which gives them their high potential in bioterrorist attacks. Others are responsible for blockage of main cellular metabolism, causing cellular death. Moreover, most toxins act very quickly and are lethal in low doses (LD50 < 25 mg/kg), which are very often lower than chemical warfare agents. For these reasons we decided to prepare this review paper which main aim is to present the high potential of biological toxins as factors of bioterrorism describing the general characteristics, mechanisms of action and treatment of most potent biological toxins. -
Anti-Inflammatory and Immune Regulatory Actions of Naja Naja
toxins Review Anti-Inflammatory and Immune Regulatory Actions of Naja naja atra Venom Shu-Zhi Wang 1,2 and Zheng-Hong Qin 3,* 1 Institute of Pharmacy and Pharmacology, University of South China, Hengyang 421001, China; [email protected] 2 Hunan Province Cooperative Innovation Center for Molecular Target New Drug Study, University of South China, Hengyang 421001, China 3 Department of Pharmacology and Laboratory of Aging and Nervous Diseases, Jiangsu Key Laboratory of Translational Research and Therapy for Neuro-Psycho-Diseases, Jiangsu Key Laboratory of Preventive and Translational Medicine for Geriatric Diseases, College of Pharmaceutical Science, Soochow University, Suzhou 215123, China * Correspondence: [email protected]; Tel./Fax: +86-512-65882071 Received: 23 December 2017; Accepted: 24 February 2018; Published: 28 February 2018 Abstract: Naja naja atra venom (NNAV) is composed of various proteins, peptides, and enzymes with different biological and pharmacological functions. A number of previous studies have reported that NNAV exerts potent analgesic effects on various animal models of pain. The clinical studies using whole venom or active components have confirmed that NNAV is an effective and safe medicine for treatment of chronic pain. Furthermore, recent studies have demonstrated that NNAV has anti-inflammatory and immune regulatory actions in vitro and in vivo. In this review article, we summarize recent studies of NNAV and its components on inflammation and immunity. The main new findings in NNAV research show that it may enhance innate and humoral immune responses while suppressing T lymphocytes-mediated cellular immunity, thus suggesting that NNAV and its active components may have therapeutic values in the treatment of inflammatory and autoimmune diseases. -
Venom Gland Transcriptomic and Proteomic
toxins Article Venom Gland Transcriptomic and Proteomic Analyses of the Enigmatic Scorpion Superstitionia donensis (Scorpiones: Superstitioniidae), with Insights on the Evolution of Its Venom Components Carlos E. Santibáñez-López 1, Jimena I. Cid-Uribe 1, Cesar V. F. Batista 2, Ernesto Ortiz 1,* and Lourival D. Possani 1,* 1 Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad 2001, Apartado Postal 510-3, Cuernavaca, Morelos 62210, Mexico; [email protected] (C.E.S.-L.); [email protected] (J.I.C.-U.) 2 Laboratorio Universitario de Proteómica, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad 2001, Apartado Postal 510-3, Cuernavaca, Morelos 62210, Mexico; [email protected] * Correspondence: [email protected] (E.O.); [email protected] (L.D.P.); Tel.: +52-777-329-1647 (E.O.); +52-777-317-1209 (L.D.P.) Academic Editor: Richard J. Lewis Received: 25 October 2016; Accepted: 1 December 2016; Published: 9 December 2016 Abstract: Venom gland transcriptomic and proteomic analyses have improved our knowledge on the diversity of the heterogeneous components present in scorpion venoms. However, most of these studies have focused on species from the family Buthidae. To gain insights into the molecular diversity of the venom components of scorpions belonging to the family Superstitioniidae, one of the neglected scorpion families, we performed a transcriptomic and proteomic analyses for the species Superstitionia donensis. The total mRNA extracted from the venom glands of two specimens was subjected to massive sequencing by the Illumina protocol, and a total of 219,073 transcripts were generated. -
Report from the 26Th Meeting on Toxinology,“Bioengineering Of
toxins Meeting Report Report from the 26th Meeting on Toxinology, “Bioengineering of Toxins”, Organized by the French Society of Toxinology (SFET) and Held in Paris, France, 4–5 December 2019 Pascale Marchot 1,* , Sylvie Diochot 2, Michel R. Popoff 3 and Evelyne Benoit 4 1 Laboratoire ‘Architecture et Fonction des Macromolécules Biologiques’, CNRS/Aix-Marseille Université, Faculté des Sciences-Campus Luminy, 13288 Marseille CEDEX 09, France 2 Institut de Pharmacologie Moléculaire et Cellulaire, Université Côte d’Azur, CNRS, Sophia Antipolis, 06550 Valbonne, France; [email protected] 3 Bacterial Toxins, Institut Pasteur, 75015 Paris, France; michel-robert.popoff@pasteur.fr 4 Service d’Ingénierie Moléculaire des Protéines (SIMOPRO), CEA de Saclay, Université Paris-Saclay, 91191 Gif-sur-Yvette, France; [email protected] * Correspondence: [email protected]; Tel.: +33-4-9182-5579 Received: 18 December 2019; Accepted: 27 December 2019; Published: 3 January 2020 1. Preface This 26th edition of the annual Meeting on Toxinology (RT26) of the SFET (http://sfet.asso.fr/ international) was held at the Institut Pasteur of Paris on 4–5 December 2019. The central theme selected for this meeting, “Bioengineering of Toxins”, gave rise to two thematic sessions: one on animal and plant toxins (one of our “core” themes), and a second one on bacterial toxins in honour of Dr. Michel R. Popoff (Institut Pasteur, Paris, France), both sessions being aimed at emphasizing the latest findings on their respective topics. Nine speakers from eight countries (Belgium, Denmark, France, Germany, Russia, Singapore, the United Kingdom, and the United States of America) were invited as international experts to present their work, and other researchers and students presented theirs through 23 shorter lectures and 27 posters. -
Aspartic Acid Isomerization Characterized by High Definition
toxins Article Aspartic Acid Isomerization Characterized by High Definition Mass Spectrometry Significantly Alters the Bioactivity of a Novel Toxin from Poecilotheria Stephen R. Johnson 1,2,* and Hillary G. Rikli 3 1 Carbon Dynamics Institute LLC, Sherman, IL 62684, USA 2 Chemistry Department, University of Illinois Springfield, Springfield, IL 62703, USA 3 College of Liberal Arts & Sciences, University of Illinois Springfield, Springfield, IL 62703, USA; [email protected] * Correspondence: [email protected] Received: 2 March 2020; Accepted: 23 March 2020; Published: 25 March 2020 Abstract: Research in toxinology has created a pharmacological paradox. With an estimated 220,000 venomous animals worldwide, the study of peptidyl toxins provides a vast number of effector molecules. However, due to the complexity of the protein-protein interactions, there are fewer than ten venom-derived molecules on the market. Structural characterization and identification of post-translational modifications are essential to develop biological lead structures into pharmaceuticals. Utilizing advancements in mass spectrometry, we have created a high definition approach that fuses conventional high-resolution MS-MS with ion mobility spectrometry (HDMSE) to elucidate these primary structure characteristics. We investigated venom from ten species of “tiger” spider (Genus: Poecilotheria) and discovered they contain isobaric conformers originating from non-enzymatic Asp isomerization. One conformer pair conserved in five of ten species examined, denominated PcaTX-1a and PcaTX-1b, was found to be a 36-residue peptide with a cysteine knot, an amidated C-terminus, and isoAsp33Asp substitution. Although the isomerization of Asp has been implicated in many pathologies, this is the first characterization of Asp isomerization in a toxin and demonstrates the isomerized product’s diminished physiological effects. -
Scorpion Toxin Peptide Scaffolds
Toxins 2013, 5, 2456-2487; doi:10.3390/toxins5122456 OPEN ACCESS toxins ISSN 2072-6651 www.mdpi.com/journal/toxins Article Evolution Stings: The Origin and Diversification of Scorpion Toxin Peptide Scaffolds Kartik Sunagar 1,2,†, Eivind A. B. Undheim 3,4,†, Angelo H. C. Chan 3, Ivan Koludarov 3,4, Sergio A. Muñoz-Gómez 5, Agostinho Antunes 1,2 and Bryan G. Fry 3,4,* 1 CIMAR/CIIMAR, Centro Interdisciplinar de Investigação Marinha e Ambiental, Universidade do Porto, Rua dos Bragas, 177, 4050-123 Porto, Portugal; E-Mails: [email protected] (K.S.); [email protected] (A.A.) 2 Departamento de Biologia, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre, 4169-007, Porto, Portugal 3 Venom Evolution Lab, School of Biological Sciences, The University of Queensland, St. Lucia, Queensland 4072, Australia; E-Mails: [email protected] (E.A.B.U.); [email protected] (A.H.C.C.); [email protected] (I.K.) 4 Institute for Molecular Bioscience, The University of Queensland, St. Lucia, Queensland 4072, Australia 5 Department of Biochemistry and Molecular Biology, Centre for Comparative Genomics and Evolutionary Bioinformatics, Dalhousie University, Halifax, Nova Scotia, Canada; E-Mail: [email protected] † These authors contributed equally to this work. * Author to whom correspondence should be addressed; E-Mail: [email protected]; Tel.: +61-400-193-182. Received: 21 November 2013; in revised form: 9 December 2013 / Accepted: 9 December 2013 / Published: 13 December 2013 Abstract: The episodic nature of natural selection and the accumulation of extreme sequence divergence in venom-encoding genes over long periods of evolutionary time can obscure the signature of positive Darwinian selection. -