Focus on Scorpion Toxins
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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 -
ANA CAROLINA MARTINS WILLE.Pdf
UNIVERSIDADE FEDERAL DO PARANÁ ANA CAROLINA MARTINS WILLE AVALIAÇÃO DA ATIVIDADE DE FOSFOLIPASE-D RECOMBINANTE DO VENENO DA ARANHA MARROM (Loxosceles intermedia) SOBRE A PROLIFERAÇÃO, INFLUXO DE CÁLCIO E METABOLISMO DE FOSFOLIPÍDIOS EM CÉLULAS TUMORAIS. CURITIBA 2014 i Wille, Ana Carolina Martins Avaliação da atividade de fosfolipase-D recombinante do veneno da aranha marrom (Loxosceles intermedia) sobre a proliferação, influxo de cálcio e metabolismo de fosfolipídios em células tumorais Curitiba, 2014. 217p. Tese (Doutorado) – Universidade Federal do Paraná – UFPR 1.veneno de aranha marrom. 2. fosfolipase-D. 3.proliferação celular. 4.metabolismo de lipídios. 5.influxo de cálcio. ANA CAROLINA MARTINS WILLE AVALIAÇÃO DA ATIVIDADE DE FOSFOLIPASE-D RECOMBINANTE DO VENENO DA ARANHA MARROM (Loxosceles intermedia) SOBRE A PROLIFERAÇÃO, INFLUXO DE CÁLCIO E METABOLISMO DE FOSFOLIPÍDIOS EM CÉLULAS TUMORAIS. Tese apresentada como requisito à obtenção do grau de Doutor em Biologia Celular e Molecular, Curso de Pós- Graduação em Biologia Celular e Molecular, Setor de Ciências Biológicas, Universidade Federal do Paraná. Orientador(a): Dra. Andrea Senff Ribeiro Co-orientador: Dr. Silvio Sanches Veiga CURITIBA 2014 ii O desenvolvimento deste trabalho foi possível devido ao apoio financeiro do Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), a Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES), Fundação Araucária e SETI-PR. iii Dedico este trabalho àquela que antes da sua existência foi o grande sonho que motivou minha vida. Sonho que foi a base para que eu escolhesse uma profissão e um trabalho. À você, minha amada filha GIOVANNA, hoje minha realidade, dedico todo meu trabalho. iv Dedico também este trabalho ao meu amado marido, amigo, professor e co- orientador Dr. -
The Anemonia Viridis Venom: Coupling Biochemical Purification
marine drugs Review The Anemonia viridis Venom: Coupling Biochemical Purification and RNA-Seq for Translational Research Aldo Nicosia 1,*,† , Alexander Mikov 2,†, Matteo Cammarata 3, Paolo Colombo 4 , Yaroslav Andreev 2,5, Sergey Kozlov 2 and Angela Cuttitta 1,* 1 National Research Council-Institute for the Study of Anthropogenic Impacts and Sustainability in the Marine Environment (IAS-CNR), Laboratory of Molecular Ecology and Biotechnology, Capo Granitola, Via del mare, Campobello di Mazara (TP), 91021 Sicily, Italy 2 Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, RAS, GSP-7, ul. Miklukho-Maklaya, 16/10, 117997 Moscow, Russia; [email protected] (A.M.); [email protected] (Y.A.); [email protected] (S.K.) 3 Department of Earth and Marine Sciences, University of Palermo, 90100 Palermo, Italy; [email protected] 4 Istituto di Biomedicina e di Immunologia Molecolare, Consiglio Nazionale delle Ricerche, Via Ugo La Malfa 153, 90146 Palermo, Italy; [email protected] 5 Institute of Molecular Medicine, Ministry of Healthcare of the Russian Federation, Sechenov First Moscow State Medical University, 119991 Moscow, Russia * Correspondence: [email protected] (A.N.); [email protected] (A.C.); Tel.: +39-0924-40600 (A.N. & A.C.) † These authors have made equal contribution. Received: 29 September 2018; Accepted: 24 October 2018; Published: 25 October 2018 Abstract: Blue biotechnologies implement marine bio-resources for addressing practical concerns. The isolation of biologically active molecules from marine animals is one of the main ways this field develops. Strikingly, cnidaria are considered as sustainable resources for this purpose, as they possess unique cells for attack and protection, producing an articulated cocktail of bioactive substances. -
(12) United States Patent (10) Patent No.: US 9,062,119 B2 Varga Et Al
USOO90621-19B2 (12) United States Patent (10) Patent No.: US 9,062,119 B2 Varga et al. (45) Date of Patent: Jun. 23, 2015 (54) MODIFIED PEPTIDE TOXINS OTHER PUBLICATIONS (71) Applicants:Zoltan Varga, Debrecen (HU); Gyorgy Bagdanyi, M. et al. Anuroctoxin, a new scorpion toxin of the alpha Panyi, Debrecen (HU); Gabor Toth, KTX 6 subfamily, is highly selective for Kv1.3 over IKCal ion Szeged (HU); Kinga Rakosi, Szeged channels of human T lymphocytes. Mol Pharmacol (2005), vol. 67. (HU) pp. 1034-1044. Batista, CV. et al. Two novel toxins from the Amazonian scorpion (72) Inventors: Zoltan Varga, Debrecen (HU); Gyorgy Tityus cambridgei that block Kv1.3 and Shaker BK(+)-channels with Panyi, Debrecen (HU); Gabor Toth, distinctly different affinities. Biochim Biophys Acta (2002), vol. Szeged (HU); Kinga Rakosi, Szeged 1601, pp. 123-131. Beeton, C. et al. Selective blockade of T lymphocyte K+ channels (HU) ameliorates experimental autoimmune encephalomyelitis, a model (73) Assignees: University of Debrecen, Debrecen for multiple sclerosis. Proc Natl Acad Sci USA (2001), vol. 98, pp. (HU); University of Szeged, Szeged 13942-13947. Beeton, C. et al. Kv1.3 channels are a therapeutic target for T cell (HU) mediated autoimmune diseases. Proc Natl AcadSci USA (2006), vol. 103, pp. 17414-17419. (*) Notice: Subject to any disclaimer, the term of this Corzo, G. et al. A selective blocker of Kv1.2 and Kv1.3 potassium patent is extended or adjusted under 35 channels from the venom of the Scorpion Centruroides suffusus suf U.S.C. 154(b) by 0 days. fusus. Biochem Pharmacol (2008), vol. -
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. -
Venom Week 2012 4Th International Scientific Symposium on All Things Venomous
17th World Congress of the International Society on Toxinology Animal, Plant and Microbial Toxins & Venom Week 2012 4th International Scientific Symposium on All Things Venomous Honolulu, Hawaii, USA, July 8 – 13, 2012 1 Table of Contents Section Page Introduction 01 Scientific Organizing Committee 02 Local Organizing Committee / Sponsors / Co-Chairs 02 Welcome Messages 04 Governor’s Proclamation 08 Meeting Program 10 Sunday 13 Monday 15 Tuesday 20 Wednesday 26 Thursday 30 Friday 36 Poster Session I 41 Poster Session II 47 Supplemental program material 54 Additional Abstracts (#298 – #344) 61 International Society on Thrombosis & Haemostasis 99 2 Introduction Welcome to the 17th World Congress of the International Society on Toxinology (IST), held jointly with Venom Week 2012, 4th International Scientific Symposium on All Things Venomous, in Honolulu, Hawaii, USA, July 8 – 13, 2012. This is a supplement to the special issue of Toxicon. It contains the abstracts that were submitted too late for inclusion there, as well as a complete program agenda of the meeting, as well as other materials. At the time of this printing, we had 344 scientific abstracts scheduled for presentation and over 300 attendees from all over the planet. The World Congress of IST is held every three years, most recently in Recife, Brazil in March 2009. The IST World Congress is the primary international meeting bringing together scientists and physicians from around the world to discuss the most recent advances in the structure and function of natural toxins occurring in venomous animals, plants, or microorganisms, in medical, public health, and policy approaches to prevent or treat envenomations, and in the development of new toxin-derived drugs. -
Ion Channels 3 1
r r r Cell Signalling Biology Michael J. Berridge Module 3 Ion Channels 3 1 Module 3 Ion Channels Synopsis Ion channels have two main signalling functions: either they can generate second messengers or they can function as effectors by responding to such messengers. Their role in signal generation is mainly centred on the Ca2 + signalling pathway, which has a large number of Ca2+ entry channels and internal Ca2+ release channels, both of which contribute to the generation of Ca2 + signals. Ion channels are also important effectors in that they mediate the action of different intracellular signalling pathways. There are a large number of K+ channels and many of these function in different + aspects of cell signalling. The voltage-dependent K (KV) channels regulate membrane potential and + excitability. The inward rectifier K (Kir) channel family has a number of important groups of channels + + such as the G protein-gated inward rectifier K (GIRK) channels and the ATP-sensitive K (KATP) + + channels. The two-pore domain K (K2P) channels are responsible for the large background K current. Some of the actions of Ca2 + are carried out by Ca2+-sensitive K+ channels and Ca2+-sensitive Cl − channels. The latter are members of a large group of chloride channels and transporters with multiple functions. There is a large family of ATP-binding cassette (ABC) transporters some of which have a signalling role in that they extrude signalling components from the cell. One of the ABC transporters is the cystic − − fibrosis transmembrane conductance regulator (CFTR) that conducts anions (Cl and HCO3 )and contributes to the osmotic gradient for the parallel flow of water in various transporting epithelia. -
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Dear Author, Please, note that changes made to the HTML content will be added to the article before publication, but are not reflected in this PDF. Note also that this file should not be used for submitting corrections. Our reference: TOXCON 4827 P-authorquery-v9 AUTHOR QUERY FORM Journal: TOXCON Please e-mail or fax your responses and any corrections to: E-mail: [email protected] Article Number: 4827 Fax: +31 2048 52789 Dear Author, Please check your proof carefully and mark all corrections at the appropriate place in the proof (e.g., by using on-screen annotation in the PDF file) or compile them in a separate list. Note: if you opt to annotate the file with software other than Adobe Reader then please also highlight the appropriate place in the PDF file. To ensure fast publication of your paper please return your corrections within 48 hours. For correction or revision of any artwork, please consult http://www.elsevier.com/artworkinstructions. Any queries or remarks that have arisen during the processing of your manuscript are listed below and highlighted by flags in the proof. Location Query / Remark: Click on the Q link to find the query’s location in text in article Please insert your reply or correction at the corresponding line in the proof Q1 Please check the telephone/fax number of the corresponding author, and correct if necessary. Q2 Please check the sections 'Abbreviations' and 'Conflict of interest', and correct if necessary. Q3 Please provide the volume number or issue number or page range for the bibliography in Ref. -
Marine Drugs ISSN 1660-3397 © 2006 by MDPI
Mar. Drugs 2006, 4, 70-81 Marine Drugs ISSN 1660-3397 © 2006 by MDPI www.mdpi.org/marinedrugs Special Issue on “Marine Drugs and Ion Channels” Edited by Hugo Arias Review Cnidarian Toxins Acting on Voltage-Gated Ion Channels Shanta M. Messerli and Robert M. Greenberg * Marine Biological Laboratory, 7 MBL Street, Woods Hole, MA 02543, USA Tel: 508 289-7981. E-mail: [email protected] * Author to whom correspondence should be addressed. Received: 21 February 2006 / Accepted: 27 February 2006 / Published: 6 April 2006 Abstract: Voltage-gated ion channels generate electrical activity in excitable cells. As such, they are essential components of neuromuscular and neuronal systems, and are targeted by toxins from a wide variety of phyla, including the cnidarians. Here, we review cnidarian toxins known to target voltage-gated ion channels, the specific channel types targeted, and, where known, the sites of action of cnidarian toxins on different channels. Keywords: Cnidaria; ion channels; toxin; sodium channel; potassium channel. Abbreviations: KV channel, voltage-gated potassium channel; NaV, voltage-gated sodium channel; CaV, voltage-gated calcium channel; ApA, Anthopleurin A; ApB, Anthopleurin B; ATX II, Anemone sulcata toxin II; Bg II, Bunodosoma granulifera toxin II; Sh I, peptide neurotoxin I from Stichodactyla helianthus; RP II, polypeptide toxin II from Radianthus paumotensis; RP III, polypeptide toxin III from Radianthus paumotensis; RTX I, neurotoxin I from Radianthus macrodactylus; PaTX, toxin from Paracicyonis actinostoloides; Er I, peptide toxin I from Entacmaea ramsayi; Da I, peptide toxin I from Dofleinia armata; ATX III, Anemone sulcata toxin III; ShK, potassium channel toxin from Stichodactyla helianthus; BgK, potassium channel toxin from Bunodosoma granulifera; AsKS, kalciceptine from Anemonia sulcata; HmK, potassium channel toxin from Heteractis magnifica; AeK, potassium channel toxin from Actinia equina; AsKC 1-3, kalcicludines 1-3 from Anemonia sulcata; BDS-I, BDS-II, blood depressing toxins I and II Mar. -
Androctonus Mauretanicus Mauretanicus
Hindawi Publishing Corporation Journal of Toxicology Volume 2012, Article ID 103608, 9 pages doi:10.1155/2012/103608 Review Article Potassium Channels Blockers from the Venom of Androctonus mauretanicus mauretanicus Marie-France Martin-Eauclaire and Pierre E. Bougis Aix-Marseille University, CNRS, UMR 7286, CRN2M, Facult´edeM´edecine secteur Nord, CS80011, Boulevard Pierre Dramard, 13344 Marseille Cedex 15, France Correspondence should be addressed to Marie-France Martin-Eauclaire, [email protected] and Pierre E. Bougis, [email protected] Received 2 February 2012; Accepted 16 March 2012 Academic Editor: Maria Elena de Lima Copyright © 2012 M.-F. Martin-Eauclaire and P. E. Bougis. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. K+ channels selectively transport K+ ions across cell membranes and play a key role in regulating the physiology of excitable and nonexcitable cells. Their activation allows the cell to repolarize after action potential firing and reduces excitability, whereas channel inhibition increases excitability. In eukaryotes, the pharmacology and pore topology of several structural classes of K+ channels have been well characterized in the past two decades. This information has come about through the extensive use of scorpion toxins. We have participated in the isolation and in the characterization of several structurally distinct families of scorpion toxin peptides exhibiting different K+ channel blocking functions. In particular, the venom from the Moroccan scorpion Androctonus ffi + + mauretanicus mauretanicus provided several high-a nity blockers selective for diverse K channels (SKCa,Kv4.x, and Kv1.x K channel families). -
Mechanism of M-Conotoxin PIIIA Binding to the Voltage-Gated Na+
Mechanism of m-Conotoxin PIIIA Binding to the + Voltage-Gated Na Channel NaV1.4 Rong Chen*, Anna Robinson, Shin-Ho Chung Research School of Biology, Australian National University, Canberra, ACT, Australia Abstract + Several subtypes of voltage-gated Na (NaV) channels are important targets for pain management. m-Conotoxins isolated from venoms of cone snails are potent and specific blockers of different NaV channel isoforms. The inhibitory effect of m- conotoxins on NaV channels has been examined extensively, but the mechanism of toxin specificity has not been understood in detail. Here the known structure of m-conotoxin PIIIA and a model of the skeletal muscle channel NaV1.4 are used to elucidate elements that contribute to the structural basis of m-conotoxin binding and specificity. The model of NaV1.4 is constructed based on the crystal structure of the bacterial NaV channel, NaVAb. Six different binding modes, in which the side chain of each of the basic residues carried by the toxin protrudes into the selectivity filter of NaV1.4, are examined in atomic detail using molecular dynamics simulations with explicit solvent. The dissociation constants (Kd) computed for two selected binding modes in which Lys9 or Arg14 from the toxin protrudes into the filter of the channel are within 2 fold; both values in close proximity to those determined from dose response data for the block of NaV currents. To explore the mechanism of PIIIA specificity, a double mutant of NaV1.4 mimicking NaV channels resistant to m-conotoxins and tetrodotoxin is constructed and the binding of PIIIA to this mutant channel examined. -
View of the Venom Gland Oms, but They Are Also Present in Vertebrates, Like the Transcriptome
BMC Genomics BioMed Central Research article Open Access Transcriptome analysis of the venom gland of the Mexican scorpion Hadrurus gertschi (Arachnida: Scorpiones) Elisabeth F Schwartz1,2, Elia Diego-Garcia1, Ricardo C Rodríguez de la Vega1 and Lourival D Possani*1 Address: 1Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad, 2001 Cuernavaca 62210, Mexico and 2Departamento de Ciências Fisiológicas, Instituto de Ciências Biológicas, Universidade de Brasília, Brasília, DF, 70910-900, Brasil Email: Elisabeth F Schwartz - [email protected]; Elia Diego-Garcia - [email protected]; Ricardo C Rodríguez de la Vega - [email protected]; Lourival D Possani* - [email protected] * Corresponding author Published: 16 May 2007 Received: 17 March 2007 Accepted: 16 May 2007 BMC Genomics 2007, 8:119 doi:10.1186/1471-2164-8-119 This article is available from: http://www.biomedcentral.com/1471-2164/8/119 © 2007 Schwartz et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Abstract Background: Scorpions like other venomous animals posses a highly specialized organ that produces, secretes and disposes the venom components. In these animals, the last postabdominal segment, named telson, contains a pair of venomous glands connected to the stinger. The isolation of numerous scorpion toxins, along with cDNA-based gene cloning and, more recently, proteomic analyses have provided us with a large collection of venom components sequences.