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Development of a Quantitative PCR Assay for the Detection And
bioRxiv preprint doi: https://doi.org/10.1101/544247; this version posted February 8, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. Development of a quantitative PCR assay for the detection and enumeration of a potentially ciguatoxin-producing dinoflagellate, Gambierdiscus lapillus (Gonyaulacales, Dinophyceae). Key words:Ciguatera fish poisoning, Gambierdiscus lapillus, Quantitative PCR assay, Great Barrier Reef Kretzschmar, A.L.1,2, Verma, A.1, Kohli, G.S.1,3, Murray, S.A.1 1Climate Change Cluster (C3), University of Technology Sydney, Ultimo, 2007 NSW, Australia 2ithree institute (i3), University of Technology Sydney, Ultimo, 2007 NSW, Australia, [email protected] 3Alfred Wegener-Institut Helmholtz-Zentrum fr Polar- und Meeresforschung, Am Handelshafen 12, 27570, Bremerhaven, Germany Abstract Ciguatera fish poisoning is an illness contracted through the ingestion of seafood containing ciguatoxins. It is prevalent in tropical regions worldwide, including in Australia. Ciguatoxins are produced by some species of Gambierdiscus. Therefore, screening of Gambierdiscus species identification through quantitative PCR (qPCR), along with the determination of species toxicity, can be useful in monitoring potential ciguatera risk in these regions. In Australia, the identity, distribution and abundance of ciguatoxin producing Gambierdiscus spp. is largely unknown. In this study we developed a rapid qPCR assay to quantify the presence and abundance of Gambierdiscus lapillus, a likely ciguatoxic species. We assessed the specificity and efficiency of the qPCR assay. The assay was tested on 25 environmental samples from the Heron Island reef in the southern Great Barrier Reef, a ciguatera endemic region, in triplicate to determine the presence and patchiness of these species across samples from Chnoospora sp., Padina sp. -
Treatment Protocol Copyright © 2018 Kostoff Et Al
Prevention and reversal of Alzheimer's disease: treatment protocol Copyright © 2018 Kostoff et al PREVENTION AND REVERSAL OF ALZHEIMER'S DISEASE: TREATMENT PROTOCOL by Ronald N. Kostoffa, Alan L. Porterb, Henry. A. Buchtelc (a) Research Affiliate, School of Public Policy, Georgia Institute of Technology, USA (b) Professor Emeritus, School of Public Policy, Georgia Institute of Technology, USA (c) Associate Professor, Department of Psychiatry, University of Michigan, USA KEYWORDS Alzheimer's Disease; Dementia; Text Mining; Literature-Based Discovery; Information Technology; Treatments Prevention and reversal of Alzheimer's disease: treatment protocol Copyright © 2018 Kostoff et al CITATION TO MONOGRAPH Kostoff RN, Porter AL, Buchtel HA. Prevention and reversal of Alzheimer's disease: treatment protocol. Georgia Institute of Technology. 2018. PDF. https://smartech.gatech.edu/handle/1853/59311 COPYRIGHT AND CREATIVE COMMONS LICENSE COPYRIGHT Copyright © 2018 by Ronald N. Kostoff, Alan L. Porter, Henry A. Buchtel Printed in the United States of America; First Printing, 2018 CREATIVE COMMONS LICENSE This work can be copied and redistributed in any medium or format provided that credit is given to the original author. For more details on the CC BY license, see: http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License<http://creativecommons.org/licenses/by/4.0/>. DISCLAIMERS The views in this monograph are solely those of the authors, and do not represent the views of the Georgia Institute of Technology or the University of Michigan. This monograph is not intended as a substitute for the medical advice of physicians. The reader should regularly consult a physician in matters relating to his/her health and particularly with respect to any symptoms that may require diagnosis or medical attention. -
1 Gambierol 1 2 3 4 Makoto Sasaki, Eva Cagide, and 5 M
34570 FM i-xviii.qxd 2/9/07 9:16 AM Page i PHYCOTOXINS Chemistry and Biochemistry 34570 FM i-xviii.qxd 2/9/07 9:16 AM Page iii PHYCOTOXINS Chemistry and Biochemistry Luis M. Botana Editor 34570 FM i-xviii.qxd 2/9/07 9:16 AM Page iv 1 2 3 Dr. Luis M. Botana is professor of Pharmacology, University of Santiago de Compostela, Spain. His group is a 4 world leader in the development of new methods to monitor the presence of phycotoxins, having developed 5 methods to date for saxitoxins, yessotoxin, pectenotoxin, ciguatoxins, brevetoxins, okadaic acid and dinophy- 6 sistoxins. Dr. Botana is the editor of Seafood and Freshwater Toxins: Pharmacology, Physiology and Detection, 7 to date the only comprehensive reference book entirely devoted to marine toxins. 8 ©2007 Blackwell Publishing 9 All rights reserved 10 1 Blackwell Publishing Professional 2 2121 State Avenue, Ames, Iowa 50014, USA 3 4 Orders: 1-800-862-6657 5 Office: 1-515-292-0140 6 Fax: 1-515-292-3348 7 Web site: www.blackwellprofessional.com 8 Blackwell Publishing Ltd 9 9600 Garsington Road, Oxford OX4 2DQ, UK 20 Tel.: +44 (0)1865 776868 1 2 Blackwell Publishing Asia 3 550 Swanston Street, Carlton, Victoria 3053, Australia 4 Tel.: +61 (0)3 8359 1011 5 6 Authorization to photocopy items for internal or personal use, or the internal or personal use of specific clients, 7 is granted by Blackwell Publishing, provided that the base fee is paid directly to the Copyright Clearance Cen- 8 ter, 222 Rosewood Drive, Danvers, MA 01923. -
STEC) Detection in Food Shiga Toxin-Producing Escherichia Coli (STEC) Are Synonymous with Verocytotoxigenic Escherichia Coli (VTEC)
Report of the Scientific Committee of the Food Safety Authority of Ireland 2019 Advice on Shiga toxin-producing Escherichia coli (STEC) detection in food Shiga toxin-producing Escherichia coli (STEC) are synonymous with verocytotoxigenic Escherichia coli (VTEC). Similarly, stx genes are synonymous with vtx genes. The terms STEC and stx have been used throughout this report. Report of the Scientific Committee of the Food Safety Authority of Ireland Advice on Shiga toxin-producing Escherichia coli (STEC) detection in food Published by: Food Safety Authority of Ireland The Exchange, George’s Dock, IFSC Dublin 1, D01 P2V6 Tel: +353 1 817 1300 Email: [email protected] www.fsai.ie © FSAI 2019 Applications for reproduction should be made to the FSAI Information Unit ISBN 978-1-910348-22-2 Report of the Scientific Committee of the Food Safety Authority of Ireland CONTENTS ABBREVIATIONS 3 EXECUTIVE SUMMARY 5 GENERAL RECOMMENDATIONS 8 BACKGROUND 9 1. STEC AND HUMAN ILLNESS 11 1.1 Pathogenic Escherichia coli . .11 1.2 STEC: toxin production.............................................12 1.3 STEC: public health concern . 13 1.4 STEC notification trends . .14 1.5 Illness severity ....................................................16 1.6 Human disease and STEC virulence ..................................17 1.7 Source of STEC human infection . 22 1.8 Foodborne STEC outbreaks .........................................22 1.9 STEC outbreaks in Ireland . 24 2. STEC METHODS OF ANALYSIS 28 2.1 Detection method for E. coli O157 in food . .29 2.2 PCR-based detection of STEC O157 and non-O157 in food.............29 2.3 Discrepancies between PCR screening and culture-confirmed results for STEC in food ............................................32 2.4 Alternative methods for the detection and isolation of STEC . -
A A–803467, 98 Absorption, Distribution, Metabolism, Elimination
Index A Anxiety disorders, 55 A–803467, 98 APD. See Action potential duration Absorption, distribution, metabolism, Arrhythmias, 45, 46 elimination and toxicity Aryl sulfonamido indanes, 126–128, 130 (ADMET), 193 ATP-sensitive potassium channels (KATP Absorption, distribution, metabolism, channels), 61 excretion, and toxicity Atrial effective refractory period (AERP), 122, (ADMET), 68 124–126, 128, 129, 132, 138 Acetylcholine binding protein (AChBP), Autoimmune diseases, 254 61, 62, 64 AZD7009, 101 Acetylcholine receptor (AChR), 57, 64 Azimilide, 139 Action potential duration (APD), 120, 122, 123, 128, 132 B Action potentials, 243, 256, 259 Basis set, 69–70 ADME/T, 299, 304 b-Barrel membrane proteins AERP. See Atrial effective refractory period genome-wide annotation, 13 Agitoxin (AgTX), 60 machine-learning techniques Agonists, 59–61, 64 residue pair preference, 11 Alinidine, 40–42 TMBs, 10 ALS. See Amyotrophic lateral sclerosis pipeline, genomic sequences, 14 Alzheimer, 55, 61 statistical method, 9–10 AMBER, 61, 65 Bending hinge, 64 2-Amino–2-imidazolidinone, 123, 125 Benzanilide, 256–257 Ammi visnaga, 254 Benzimidazolone, 256–257 b-Amyloid peptide (Ab), 62–63, 65 Benzocaine, 140 Amyotrophic lateral sclerosis (ALS), 90, 94, Benzodiazepines, 245 101 Benzopyrane, 127–128 Anionic channel blockers Benzopyrans, 61, 246–251, 261 mechanism of action of, 329–330 Benzothiadiazine 1,1-dioxide, 252–254 Antagonists, 59, 60 Benzothiadiazines, 253 Antiarrhythmic, 65–66, 68, 99, 101 Benzothiazepine, 70 Antiarrhythmic agents Benzothiazine derivatives, 251–252 class I, 245 Benzotriazole, 256–257 class II, 245 Bestrophins, 321, 322, 330, 331 class III, 245 Big potassium channels (BK channels), Antidepressant, 65–67 256, 257 Antiepileptic, 46 Bupivacaine, 56, 58, 59, 64, 69, 140 S.P. -
Neutralizing Equine Anti-Shiga Toxin
al of D urn ru Jo g l D a e Yanina et al., Int J Drug Dev & Res 2019, 11:3 n v o e i l t o International Journal of Drug Development a p n m r e e e e t n n n n n I I t t t a n h d c r R a e e s and Research Research Article Preclinical Studies of NEAST (Neutralizing Equine Anti-Shiga Toxin): A Potential Treatment for Prevention of Stec-Hus Hiriart Yanina1,2, Pardo Romina1, Bukata Lucas1, Lauché Constanza2, Muñoz Luciana1, Berengeno Andrea L3, Colonna Mariana1, Ortega Hugo H3, Goldbaum Fernando A1,2, Sanguineti Santiago1 and Zylberman Vanesa1,2* 1Inmunova S.A., San Martin, Buenos Aires, Argentina 2National Council for Scientific and Technical Research (CONICET) Center for Comparative Medicine, Institute of Veterinary Sciences of the Coast (ICiVetLitoral), Argentina 3National University of the Coast (UNL)/Conicet, Esperanza, Santa Fe, Argentina *Corresponding author: Zylberman Vanesa, Inmunova S.A. 25 De Mayo 1021, CP B1650HMP, San Martin, Buenos Aires, Argentina, Interno 6053, Tel: +54-11- 2033-1455; E-mail: [email protected] Received July 29, 2019; Accepted August 30, 2019; Published Sepetmber 07, 2019 Abstract STEC-HUS is a clinical syndrome characterized by the triad of thrombotic microangiopathy, thrombocytopenia and acute kidney injury. Despite the magnitude of the social and economic problems caused by STEC infections, there are currently no specific therapeutic options on the market. HUS is a toxemic disorder and the therapeutic effect of the early intervention with anti-toxin neutralizing antibodies has been supported in several animal models. -
Enterohemolysin Operon of Shiga Toxin-Producing Escherichia Coli
FEBS 26317 FEBS Letters 524 (2002) 219^224 View metadata, citation and similar papers at core.ac.uk brought to you by CORE Enterohemolysin operon of Shiga toxin-producing Escherichiaprovided by coliElsevier :- Publisher Connector a virulence function of in£ammatory cytokine production from human monocytes Ikue Taneike, Hui-Min Zhang, Noriko Wakisaka-Saito, Tatsuo Yamamotoà Division of Bacteriology, Department of Infectious Disease Control and International Medicine, Niigata University Graduate School of Medical and Dental Sciences, 757 Ichibanchou, Asahimachidori, Niigata, Japan Received 5 April 2002; revised 14 June 2002; accepted 19 June 2002 First published online 8 July 2002 Edited by Veli-Pekka Lehto Stx [6]. In the case of the outbreak strains in Japan in 1996, Abstract Shiga toxin-producing Escherichia coli (STEC) is associated with hemolytic uremic syndrome (HUS). Although more than 98% of STEC were positive for enterohemolysin most clinical isolates ofSTEC produce hemolysin (called en- [8]. terohemolysin), the precise role ofenterohemolysin in the patho- Enterohemolysin and K-hemolysin (which is produced from genesis ofSTEC infectionsis unknown. Here we demonstrated approximately 50% of E. coli isolates from extraintestinal in- that E. coli carrying the cloned enterohemolysin operon (hlyC, fections [9], or from porcine STEC strains [6]) are members of A, B, D genes) from an STEC human strain induced the pro- the RTX family, associated with the ATP-dependent HlyB/ duction ofinterleukin-1 L (IL-1L) through its mRNA expression HlyD/TolC secretion system through which hemolysin K but not tumor necrosis factor- from human monocytes. No (HlyA) is secreted across the bacterial membranes. Both the L IL-1 release was observed with an enterohemolysin (HlyA)- enterohemolysin and K-hemolysin operons consist of the hlyC, negative, isogenic E. -
Safe Handling of Acutely Toxic Chemicals Safe Handling of Acutely
Safe Handling of Acutely Toxic Chemicals , Mutagens, Teratogens and Reproductive Toxins October 12, 2011 BSBy Sco ttBthlltt Batcheller R&D Manager Milwaukee WI Hazards Classes for Chemicals Flammables • Risk of ignition in air when in contact with common energy sources Corrosives • Generally destructive to materials and tissues Energetic and Reactive Materials • Sudden release of destructive energy possible (e.g. fire, heat, pressure) Toxic Substances • Interaction with cells and organs may lead to tissue damage • EfftEffects are t tilltypically not general ltllti to all tissues, bttbut target tdted to specifi c ones • Examples: – Cancers – Organ diseases – Inflammation, skin rashes – Debilitation from long-term Poison Acute Cancer, health or accumulation with delayed (ingestion) risk reproductive risk emergence 2 Toxic Substances Are All Around Us Pollutants Natural toxins • Cigare tte smo ke • V(kidbt)Venoms (snakes, spiders, bees, etc.) • Automotive exhaust • Poison ivy Common Chemicals • Botulinum toxin • Pesticides • Ricin • Fluorescent lights (mercury) • Radon gas • Asbestos insulation • Arsenic and heavy metals • BPA ((pBisphenol A used in some in ground water plastics) 3 Application at UNL Chemicals in Chemistry Labs Toxin-producing Microorganisms • Chloro form • FiFungi • Formaldehyde • Staphylococcus species • Acetonitrile • Shiga-toxin from E. coli • Benzene Select Agent Toxins (see register) • Sodium azide • Botulinum neurotoxins • Osmium/arsenic/cadmium salts • T-2 toxin Chemicals in Biology Labs • Tetrodotoxin • Phenol -
Shiga Toxin E. Coli Detection Differentiation Implications for Food
SL440 Shiga Toxin-Producing Escherichia coli: Detection, Differentiation, and Implications for Food Safety1 William J. Zaragoza, Max Teplitski, and Clifton K. Fagerquist2 Introduction for the effective detection of the Shiga-toxin-producing pathogens in a variety of food matrices. Shiga toxin is a protein found within the genome of a type of virus called a bacteriophage. These bacteriophages can There are two types of Shiga toxins—Shiga toxin 1 (Stx1) integrate into the genomes of the bacterium E. coli, giving and Shiga toxin 2 (Stx2). Stx1 is composed of several rise to Shiga toxin-producing E. coli (STEC). Even though subtypes knows as Stx1a, Stx1c, and Stx1d. Stx2 has seven most E. coli are benign or even beneficial (“commensal”) subtypes: a–g. Strains carrying all of the Stx1 subtypes affect members of our gut microbial communities, strains of E. humans, though they are less potent than that of Stx2. Stx2 coli carrying Shiga-toxin encoding genes (as well as other subtypes a,c, and d are frequently associated with human virulence determinants) are highly pathogenic in humans illness, while the other subtypes affect different animals. and other animals. When mammals ingest these bacteria, Subtypes Stx2b and Stx2e affect neonatal piglets, while STECs can undergo phage-driven lysis and deliver these target hosts for Stx2f and Stx2g subtypes are not currently toxins to mammalian guts. The Shiga toxin consists of an known (Fuller et al. 2011). Stx2f was originally isolated A subunit and 5 identical B subunits. The B subunits are from feral pigeons (Schmidt et al. 2000), and Stx2g was involved in binding to gut epithelial cells. -
Marine Natural Products and Their Potential Application in the Future
AJSTD Vol. 22 Issue 4 pp. 297-311 (2005) MARINE NATURAL PRODUCTS AND THEIR POTENTIAL APPLICATION IN THE FUTURE Chau Van Minh*, Phan Van Kiem, and Nguyen Hai Dang Institute of Natural Products Chemistry, Vietnamese Academy of Science and Technology 18 Hoang Quoc Viet Road, Cau Giay, Hanoi, Vietnam Received 04 November 2005 1. INTRODUCTION Oceans are the diverse resource, which cover more than 70% of the earth’s surface. No doubt, with 34 of 36 phyla of life represented, oceans are the greatest biodiversity in the world [1]. They are the extraordinary natural source of microorganism, algae, sponge, coelenterate, bryozoan, mollusk, and echinoderm… Especially, on coral reef, where shelter more than 1000 species per m2. Surprisingly, there is only a small number of researches in this field. Therefore increasing research on marine natural source may provide good results for exploiting and developing valuable natural products which benefit for human. Marine environment is a rich source of biological and chemical diversity. The diversity has been unique source of chemical compounds of potential for pharmaceuticals, cosmetics, dietary supplements, and agrochemicals. Ecological pressure, including competitions for food and space, the fouling of predator and surface, has led to the evolution of secondary metabolites with various biological activities. Many organisms are soft bodies and/or unmoved, hardly survive with the threat from around environment. Hence they have evolved the ability to synthesize toxic compounds or obtain them from microorganism to defense against predator or to paralyze their prey. The questions such as, why do fish not eat particular algae? Why do two sponges grow and expand until they reach but not grow over each other? may be explained by these reasons. -
National Shiga Toxin-Producing Escherichia Coli (STEC) Surveillance
National Enteric Disease Surveillance: STEC Surveillance Overview Surveillance System Overview: National Shiga toxin-producing Escherichia coli (STEC) Surveillance Shiga toxin-producing Escherichia coli (STEC) are estimated to cause more than 265,000 illnesses each year in the United States, with more than 3,600 hospitalizations and 30 deaths (1). STEC infections often cause diarrhea, sometimes bloody. Some patients with STEC infection develop hemolytic uremic syndrome (HUS), a severe complication characterized by renal failure, hemolytic anemia, and thrombocytopenia that can be fatal. Most outbreaks of STEC infection and most cases of HUS in the United States have been caused by STEC O157. Non- O157 STEC have also caused US outbreaks. Although all STEC infections are nationally notifiable, for several reasons many cases are likely not recognized (2). Not all persons ill with STEC infection seek medical care, healthcare providers may not obtain a specimen for laboratory diagnosis, or the clinical diagnostic laboratory may not perform the necessary diagnostic tests. Accounting for under-diagnosis and under-reporting, an estimated 96,534 STEC O157 and 168,698 non-O157 infections occur each year (1). STEC transmission occurs through consumption of contaminated foods, ingestion of contaminated water, or direct contact with infected persons (e.g., in child-care settings) or animals or their environments. Colored scanning electron micrograph (SEM) of Escherichia coli bacteria. National STEC surveillance data are collected through passive surveillance of laboratory-confirmed human STEC isolates in the United States. Clinical diagnostic laboratories submit STEC O157 isolates and Shiga toxin-positive broths to state and territorial public health laboratories, where they are further characterized. -
Combined Action of Shiga Toxin Type 2 and Subtilase Cytotoxin in the Pathogenesis of Hemolytic Uremic Syndrome
toxins Article Combined Action of Shiga Toxin Type 2 and Subtilase Cytotoxin in the Pathogenesis of Hemolytic Uremic Syndrome Romina S. Álvarez 1, Fernando D. Gómez 1, Elsa Zotta 1,2, Adrienne W. Paton 3, James C. Paton 3, Cristina Ibarra 1 , Flavia Sacerdoti 1 and María M. Amaral 1,* 1 Laboratorio de Fisiopatogenia, Departamento de Fisiología, Instituto de Fisiología y Biofísica Bernardo Houssay (IFIBIO Houssay-CONICET), Facultad de Medicina, Universidad de Buenos Aires, Buenos Aires 1121, Argentina; [email protected] (R.S.Á.); [email protected] (F.D.G.); [email protected] (E.Z.); [email protected] (C.I.); [email protected] (F.S.) 2 Cátedra de Fisiopatología, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Buenos Aires 1113, Argentina 3 Research Centre for Infectious Diseases, Department of Molecular and Biomedical Science, University of Adelaide, Adelaide 5005, Australia; [email protected] (A.W.P.); [email protected] (J.C.P.) * Correspondence: [email protected]; Tel.: +54-11-5285-3280 Abstract: Shiga toxin-producing E. coli (STEC) produces Stx1 and/or Stx2, and Subtilase cytotoxin (SubAB). Since these toxins may be present simultaneously during STEC infections, the purpose of this work was to study the co-action of Stx2 and SubAB. Stx2 + SubAB was assayed in vitro on monocultures and cocultures of human glomerular endothelial cells (HGEC) with a human proximal tubular epithelial cell line (HK-2) and in vivo in mice after weaning. The effects in vitro of both toxins, co-incubated and individually, were similar, showing that Stx2 and SubAB contribute similarly to renal cell damage.