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Interactions of Insecticidal Spider Peptide Neurotoxins with Insect Voltage- and Neurotransmitter-Gated Ion Channels
Interactions of insecticidal spider peptide neurotoxins with insect voltage- and neurotransmitter-gated ion channels (Molecular representation of - HXTX-Hv1c including key binding residues, adapted from Gunning et al, 2008) PhD Thesis Monique J. Windley UTS 2012 CERTIFICATE OF AUTHORSHIP/ORIGINALITY I certify that the work in this thesis has not previously been submitted for a degree nor has it been submitted as part of requirements for a degree except as fully acknowledged within the text. I also certify that the thesis has been written by me. Any help that I have received in my research work and the preparation of the thesis itself has been acknowledged. In addition, I certify that all information sources and literature used are indicated in the thesis. Monique J. Windley 2012 ii ACKNOWLEDGEMENTS There are many people who I would like to thank for contributions made towards the completion of this thesis. Firstly, I would like to thank my supervisor Prof. Graham Nicholson for his guidance and persistence throughout this project. I would like to acknowledge his invaluable advice, encouragement and his neverending determination to find a solution to any problem. He has been a valuable mentor and has contributed immensely to the success of this project. Next I would like to thank everyone at UTS who assisted in the advancement of this research. Firstly, I would like to acknowledge Phil Laurance for his assistance in the repair and modification of laboratory equipment. To all the laboratory and technical staff, particulary Harry Simpson and Stan Yiu for the restoration and sourcing of equipment - thankyou. I would like to thank Dr Mike Johnson for his continual assistance, advice and cheerful disposition. -
Using the Deadly M-Conotoxins As Probes of Voltage-Gated Sodium Channels
Toxicon 44 (2004) 117–122 www.elsevier.com/locate/toxicon Mini-review Using the deadly m-conotoxins as probes of voltage-gated sodium channels Ronald A. Li*, Gordon F. Tomaselli The Johns Hopkins University School of Medicine, 720 Rutland Avenue, Ross 871, Baltimore, MD 21205, USA Accepted 23 March 2004 Available online 19 June 2004 Abstract m-Conotoxins (m-CTX) are potent Na channel inhibitory peptides isolated from the venom of the predatory marine snail Conus geographus. m-CTXs exert their biological action by physically occluding the ion-conducting pore of voltage-gated Na (Nav) channels with a 1:1 stoichiometry in an all-or-none fashion. This article reviews our current knowledge of the mechanism of m-CTX and the associated structural and functional insights into its molecular target—Nav channels. q 2004 Elsevier Ltd. All rights reserved. Keywords: Na channel; Pore; m-Conotoxin Contents 1. Well-defined primary and 3-dimensional structures of m-CTX .............................. 117 2. Molecular target of m-CTX: voltage-gated Naþ channels . ................................. 119 3. m-CTX-pore interactions are site-specific.............................................. 119 4. Docking orientation of m-CTX ..................................................... 119 5. Isoform-specificity of m-CTX block ................................................. 121 6. m-CTX versus Kþ channel pore-blocking toxins ........................................ 121 7. Conclusion.................................................................... 121 Acknowledgements -
Biological Toxins Fact Sheet
Work with FACT SHEET Biological Toxins The University of Utah Institutional Biosafety Committee (IBC) reviews registrations for work with, possession of, use of, and transfer of acute biological toxins (mammalian LD50 <100 µg/kg body weight) or toxins that fall under the Federal Select Agent Guidelines, as well as the organisms, both natural and recombinant, which produce these toxins Toxins Requiring IBC Registration Laboratory Practices Guidelines for working with biological toxins can be found The following toxins require registration with the IBC. The list in Appendix I of the Biosafety in Microbiological and is not comprehensive. Any toxin with an LD50 greater than 100 µg/kg body weight, or on the select agent list requires Biomedical Laboratories registration. Principal investigators should confirm whether or (http://www.cdc.gov/biosafety/publications/bmbl5/i not the toxins they propose to work with require IBC ndex.htm). These are summarized below. registration by contacting the OEHS Biosafety Officer at [email protected] or 801-581-6590. Routine operations with dilute toxin solutions are Abrin conducted using Biosafety Level 2 (BSL2) practices and Aflatoxin these must be detailed in the IBC protocol and will be Bacillus anthracis edema factor verified during the inspection by OEHS staff prior to IBC Bacillus anthracis lethal toxin Botulinum neurotoxins approval. BSL2 Inspection checklists can be found here Brevetoxin (http://oehs.utah.edu/research-safety/biosafety/ Cholera toxin biosafety-laboratory-audits). All personnel working with Clostridium difficile toxin biological toxins or accessing a toxin laboratory must be Clostridium perfringens toxins Conotoxins trained in the theory and practice of the toxins to be used, Dendrotoxin (DTX) with special emphasis on the nature of the hazards Diacetoxyscirpenol (DAS) associated with laboratory operations and should be Diphtheria toxin familiar with the signs and symptoms of toxin exposure. -
Questions in the Chemical Enzymology of MAO
Review Questions in the Chemical Enzymology of MAO Rona R. Ramsay 1,* and Alen Albreht 2 1 Biomedical Sciences Research Complex, School of Biology, University of St Andrews, St Andrews KY16 9ST, UK 2 Laboratory for Food Chemistry, Department of Analytical Chemistry, National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, Slovenia; [email protected] * Correspondence: [email protected]; Tel.: +44-(0)-1334-474740 Abstract: We have structure, a wealth of kinetic data, thousands of chemical ligands and clinical information for the effects of a range of drugs on monoamine oxidase activity in vivo. We have comparative information from various species and mutations on kinetics and effects of inhibition. Nevertheless, there are what seem like simple questions still to be answered. This article presents a brief summary of existing experimental evidence the background and poses questions that remain intriguing for chemists and biochemists researching the chemical enzymology of and drug design for monoamine oxidases (FAD-containing EC 4.1.3.4). Keywords: chemical mechanism; kinetic mechanism; oxidation; protein flexibility; cysteine modifica- tion; reversible/irreversible inhibition; molecular dynamics; simulation 1. Introduction Monoamine oxidase (E.C. 1.4.3.4) enzymes MAO A and MAO B are FAD-containing Citation: Ramsay, R.R.; Albreht, A. proteins located on the outer face of the mitochondrial inner membrane, retained there Questions in the Chemical Enzymology of MAO. Chemistry 2021, by hydrophobic interactions and a transmembrane helix. The redox co-factor (FAD) is 3, 959–978. https://doi.org/10.3390/ covalently attached to a cysteine and buried deep inside the protein [1]. -
Animal Venom Derived Toxins Are Novel Analgesics for Treatment Of
Short Communication iMedPub Journals 2018 www.imedpub.com Journal of Molecular Sciences Vol.2 No.1:6 Animal Venom Derived Toxins are Novel Upadhyay RK* Analgesics for Treatment of Arthritis Department of Zoology, DDU Gorakhpur University, Gorakhpur, UP, India Abstract *Corresponding authors: Ravi Kant Upadhyay Present review article explains use of animal venom derived toxins as analgesics of the treatment of chronic pain and inflammation occurs in arthritis. It is a [email protected] progressive degenerative joint disease that put major impact on joint function and quality of life. Patients face prolonged inappropriate inflammatory responses and bone erosion. Longer persistent chronic pain is a complex and debilitating Department of Zoology, DDU Gorakhpur condition associated with a large personal, mental, physical and socioeconomic University, Gorakhpur, UttarPradesh, India. burden. However, for mitigation of inflammation and sever pain in joints synthetic analgesics are used to provide quick relief from pain but they impose many long Tel: 9838448495 term side effects. Venom toxins showed high affinity to voltage gated channels, and pain receptors. These are strong inhibitors of ion channels which enable them as potential therapeutic agents for the treatment of pain. Present article Citation: Upadhyay RK (2018) Animal Venom emphasizes development of a new class of analgesic agents in form of venom Derived Toxins are Novel Analgesics for derived toxins for the treatment of arthritis. Treatment of Arthritis. J Mol Sci. Vol.2 No.1:6 Keywords: Analgesics; Venom toxins; Ion channels; Channel inhibitors; Pain; Inflammation Received: February 04, 2018; Accepted: March 12, 2018; Published: March 19, 2018 Introduction such as the back, spine, and pelvis. -
Treatment for Calcium Channel Blocker Poisoning a Systematic Review
Clinical Toxicology ISSN: 1556-3650 (Print) 1556-9519 (Online) Journal homepage: http://www.tandfonline.com/loi/ictx20 Treatment for calcium channel blocker poisoning: A systematic review M. St-Onge, P.-A. Dubé, S. Gosselin, C. Guimont, J. Godwin, P. M. Archambault, J.-M. Chauny, A. J. Frenette, M. Darveau, N. Le sage, J. Poitras, J. Provencher, D. N. Juurlink & R. Blais To cite this article: M. St-Onge, P.-A. Dubé, S. Gosselin, C. Guimont, J. Godwin, P. M. Archambault, J.-M. Chauny, A. J. Frenette, M. Darveau, N. Le sage, J. Poitras, J. Provencher, D. N. Juurlink & R. Blais (2014) Treatment for calcium channel blocker poisoning: A systematic review, Clinical Toxicology, 52:9, 926-944, DOI: 10.3109/15563650.2014.965827 To link to this article: http://dx.doi.org/10.3109/15563650.2014.965827 © 2014 The Author(s). Published by Taylor & View supplementary material Francis. Published online: 06 Oct 2014. Submit your article to this journal Article views: 8320 View related articles View Crossmark data Citing articles: 47 View citing articles Full Terms & Conditions of access and use can be found at http://www.tandfonline.com/action/journalInformation?journalCode=ictx20 Download by: [Bird Lib Ouhsc] Date: 14 November 2017, At: 06:23 Clinical Toxicology (2014), 52, 926–944 Copyright © 2014 Informa Healthcare USA, Inc. ISSN: 1556-3650 print / 1556-9519 online DOI: 10.3109/15563650.2014.965827 REVIEW ARTICLE Treatment for calcium channel blocker poisoning: A systematic review M. ST-ONGE,1,2,3 P.-A. DUBÉ,4,5,6 S. GOSSELIN,7,8,9 C. GUIMONT,10 J. -
An in Vivo Examination of the Differences Between Rapid
www.nature.com/scientificreports OPEN An in vivo examination of the diferences between rapid cardiovascular collapse and prolonged hypotension induced by snake venom Rahini Kakumanu1, Barbara K. Kemp-Harper1, Anjana Silva 1,2, Sanjaya Kuruppu3, Geofrey K. Isbister 1,4 & Wayne C. Hodgson1* We investigated the cardiovascular efects of venoms from seven medically important species of snakes: Australian Eastern Brown snake (Pseudonaja textilis), Sri Lankan Russell’s viper (Daboia russelii), Javanese Russell’s viper (D. siamensis), Gaboon viper (Bitis gabonica), Uracoan rattlesnake (Crotalus vegrandis), Carpet viper (Echis ocellatus) and Puf adder (Bitis arietans), and identifed two distinct patterns of efects: i.e. rapid cardiovascular collapse and prolonged hypotension. P. textilis (5 µg/kg, i.v.) and E. ocellatus (50 µg/kg, i.v.) venoms induced rapid (i.e. within 2 min) cardiovascular collapse in anaesthetised rats. P. textilis (20 mg/kg, i.m.) caused collapse within 10 min. D. russelii (100 µg/kg, i.v.) and D. siamensis (100 µg/kg, i.v.) venoms caused ‘prolonged hypotension’, characterised by a persistent decrease in blood pressure with recovery. D. russelii venom (50 mg/kg and 100 mg/kg, i.m.) also caused prolonged hypotension. A priming dose of P. textilis venom (2 µg/kg, i.v.) prevented collapse by E. ocellatus venom (50 µg/kg, i.v.), but had no signifcant efect on subsequent addition of D. russelii venom (1 mg/kg, i.v). Two priming doses (1 µg/kg, i.v.) of E. ocellatus venom prevented collapse by E. ocellatus venom (50 µg/kg, i.v.). B. gabonica, C. vegrandis and B. -
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. -
Toxicology in Antiquity
TOXICOLOGY IN ANTIQUITY Other published books in the History of Toxicology and Environmental Health series Wexler, History of Toxicology and Environmental Health: Toxicology in Antiquity, Volume I, May 2014, 978-0-12-800045-8 Wexler, History of Toxicology and Environmental Health: Toxicology in Antiquity, Volume II, September 2014, 978-0-12-801506-3 Wexler, Toxicology in the Middle Ages and Renaissance, March 2017, 978-0-12-809554-6 Bobst, History of Risk Assessment in Toxicology, October 2017, 978-0-12-809532-4 Balls, et al., The History of Alternative Test Methods in Toxicology, October 2018, 978-0-12-813697-3 TOXICOLOGY IN ANTIQUITY SECOND EDITION Edited by PHILIP WEXLER Retired, National Library of Medicine’s (NLM) Toxicology and Environmental Health Information Program, Bethesda, MD, USA Academic Press is an imprint of Elsevier 125 London Wall, London EC2Y 5AS, United Kingdom 525 B Street, Suite 1650, San Diego, CA 92101, United States 50 Hampshire Street, 5th Floor, Cambridge, MA 02139, United States The Boulevard, Langford Lane, Kidlington, Oxford OX5 1GB, United Kingdom Copyright r 2019 Elsevier Inc. All rights reserved. No part of this publication may be reproduced or transmitted in any form or by any means, electronic or mechanical, including photocopying, recording, or any information storage and retrieval system, without permission in writing from the publisher. Details on how to seek permission, further information about the Publisher’s permissions policies and our arrangements with organizations such as the Copyright Clearance Center and the Copyright Licensing Agency, can be found at our website: www.elsevier.com/permissions. This book and the individual contributions contained in it are protected under copyright by the Publisher (other than as may be noted herein). -
Slow Inactivation in Voltage Gated Potassium Channels Is Insensitive to the Binding of Pore Occluding Peptide Toxins
Biophysical Journal Volume 89 August 2005 1009–1019 1009 Slow Inactivation in Voltage Gated Potassium Channels Is Insensitive to the Binding of Pore Occluding Peptide Toxins Carolina Oliva, Vivian Gonza´lez, and David Naranjo Centro de Neurociencias de Valparaı´so, Facultad de Ciencias, Universidad de Valparaı´so, Valparaı´so, Chile ABSTRACT Voltage gated potassium channels open and inactivate in response to changes of the voltage across the membrane. After removal of the fast N-type inactivation, voltage gated Shaker K-channels (Shaker-IR) are still able to inactivate through a poorly understood closure of the ion conduction pore. This, usually slower, inactivation shares with binding of pore occluding peptide toxin two important features: i), both are sensitive to the occupancy of the pore by permeant ions or tetraethylammonium, and ii), both are critically affected by point mutations in the external vestibule. Thus, mutual interference between these two processes is expected. To explore the extent of the conformational change involved in Shaker slow inactivation, we estimated the energetic impact of such interference. We used kÿconotoxin-PVIIA (kÿPVIIA) and charybdotoxin (CTX) peptides that occlude the pore of Shaker K-channels with a simple 1:1 stoichiometry and with kinetics 100-fold faster than that of slow inactivation. Because inactivation appears functionally different between outside-out patches and whole oocytes, we also compared the toxin effect on inactivation with these two techniques. Surprisingly, the rate of macroscopic inactivation and the rate of recovery, regardless of the technique used, were toxin insensitive. We also found that the fraction of inactivated channels at equilibrium remained unchanged at saturating kÿPVIIA. -
Glycine311, a Determinant of Paxilline Block in BK Channels: a Novel Bend in the BK S6 Helix Yu Zhou Washington University School of Medicine in St
Washington University School of Medicine Digital Commons@Becker Open Access Publications 2010 Glycine311, a determinant of paxilline block in BK channels: A novel bend in the BK S6 helix Yu Zhou Washington University School of Medicine in St. Louis Qiong-Yao Tang Washington University School of Medicine in St. Louis Xiao-Ming Xia Washington University School of Medicine in St. Louis Christopher J. Lingle Washington University School of Medicine in St. Louis Follow this and additional works at: http://digitalcommons.wustl.edu/open_access_pubs Recommended Citation Zhou, Yu; Tang, Qiong-Yao; Xia, Xiao-Ming; and Lingle, Christopher J., ,"Glycine311, a determinant of paxilline block in BK channels: A novel bend in the BK S6 helix." Journal of General Physiology.135,5. 481-494. (2010). http://digitalcommons.wustl.edu/open_access_pubs/2878 This Open Access Publication is brought to you for free and open access by Digital Commons@Becker. It has been accepted for inclusion in Open Access Publications by an authorized administrator of Digital Commons@Becker. For more information, please contact [email protected]. Published April 26, 2010 A r t i c l e Glycine311, a determinant of paxilline block in BK channels: a novel bend in the BK S6 helix Yu Zhou, Qiong-Yao Tang, Xiao-Ming Xia, and Christopher J. Lingle Department of Anesthesiology, Washington University School of Medicine, St. Louis, MO 63110 The tremorogenic fungal metabolite, paxilline, is widely used as a potent and relatively specific blocker of Ca2+- and voltage-activated Slo1 (or BK) K+ channels. The pH-regulated Slo3 K+ channel, a Slo1 homologue, is resistant to blockade by paxilline. -
UC Davis UC Davis Previously Published Works
UC Davis UC Davis Previously Published Works Title Heterogeneity in Kv2 Channel Expression Shapes Action Potential Characteristics and Firing Patterns in CA1 versus CA2 Hippocampal Pyramidal Neurons. Permalink https://escholarship.org/uc/item/2m94393j Journal eNeuro, 4(4) ISSN 2373-2822 Authors Palacio, Stephanie Chevaleyre, Vivien Brann, David H et al. Publication Date 2017-07-01 DOI 10.1523/ENEURO.0267-17.2017 Peer reviewed eScholarship.org Powered by the California Digital Library University of California New Research Neuronal Excitability Heterogeneity in Kv2 Channel Expression Shapes Action Potential Characteristics and Firing Patterns in CA1 versus CA2 Hippocampal Pyramidal Neurons Stephanie Palacio,1 Vivien Chevaleyre,2 David H. Brann,3 Karl D. Murray,4 Rebecca A. Piskorowski,2 and James S. Trimmer1,5 DOI:http://dx.doi.org/10.1523/ENEURO.0267-17.2017 1Department of Neurobiology, Physiology, and Behavior, University of California, Davis, CA 95616, 2INSERM U894, Team Synaptic Plasticity and Neural Networks, Université Paris Descartes, Paris 75014, France, 3Department of Neuroscience, Columbia University, New York, NY 10032, 4Center for Neuroscience, University of California, Davis, CA 95616, and 5Department of Physiology and Membrane Biology, University of California Davis School of Medicine, Davis, CA 95616 Abstract The CA1 region of the hippocampus plays a critical role in spatial and contextual memory, and has well- established circuitry, function and plasticity. In contrast, the properties of the flanking CA2 pyramidal neurons (PNs), important for social memory, and lacking CA1-like plasticity, remain relatively understudied. In particular, little is known regarding the expression of voltage-gated Kϩ (Kv) channels and the contribution of these channels to the distinct properties of intrinsic excitability, action potential (AP) waveform, firing patterns and neurotrans- mission between CA1 and CA2 PNs.