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Academic literature on the topic 'Venom toxins'

Author: Grafiati

Published: 4 June 2021

Last updated: 8 February 2022

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Journal articles on the topic "Venom toxins"

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Jaimes-Becerra, Adrian, Ranko Gacesa, Liam B. Doonan, Ashlie Hartigan, Antonio C. Marques, Beth Okamura, and Paul F. Long. "“Beyond Primary Sequence”—Proteomic Data Reveal Complex Toxins in Cnidarian Venoms." Integrative and Comparative Biology 59, no. 4 (July 8, 2019): 777–85. http://dx.doi.org/10.1093/icb/icz106.

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Abstract Venomous animals can deploy toxins for both predation and defense. These dual functions of toxins might be expected to promote the evolution of new venoms and alteration of their composition. Cnidarians are the most ancient venomous animals but our present understanding of their venom diversity is compromised by poor taxon sampling. New proteomic data were therefore generated to characterize toxins in venoms of a staurozoan, a hydrozoan, and an anthozoan. We then used a novel clustering approach to compare venom diversity in cnidarians to other venomous animals. Comparison of the presence or absence of 32 toxin protein families indicated venom composition did not vary widely among the 11 cnidarian species studied. Unsupervised clustering of toxin peptide sequences suggested that toxin composition of cnidarian venoms is just as complex as that in many venomous bilaterians, including marine snakes. The adaptive significance of maintaining a complex and relatively invariant venom remains unclear. Future study of cnidarian venom diversity, venom variation with nematocyst types and in different body regions are required to better understand venom evolution.

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Schendel, Rash, Jenner, and Undheim. "The Diversity of Venom: The Importance of Behavior and Venom System Morphology in Understanding Its Ecology and Evolution." Toxins 11, no. 11 (November 14, 2019): 666. http://dx.doi.org/10.3390/toxins11110666.

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Venoms are one of the most convergent of animal traits known, and encompass a much greater taxonomic and functional diversity than is commonly appreciated. This knowledge gap limits the potential of venom as a model trait in evolutionary biology. Here, we summarize the taxonomic and functional diversity of animal venoms and relate this to what is known about venom system morphology, venom modulation, and venom pharmacology, with the aim of drawing attention to the importance of these largely neglected aspects of venom research. We find that animals have evolved venoms at least 101 independent times and that venoms play at least 11 distinct ecological roles in addition to predation, defense, and feeding. Comparisons of different venom systems suggest that morphology strongly influences how venoms achieve these functions, and hence is an important consideration for understanding the molecular evolution of venoms and their toxins. Our findings also highlight the need for more holistic studies of venom systems and the toxins they contain. Greater knowledge of behavior, morphology, and ecologically relevant toxin pharmacology will improve our understanding of the evolution of venoms and their toxins, and likely facilitate exploration of their potential as sources of molecular tools and therapeutic and agrochemical lead compounds.

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Hu, Zhaotun, Bo Chen, Zhen Xiao, Xi Zhou, and Zhonghua Liu. "Transcriptomic Analysis of the Spider Venom Gland Reveals Venom Diversity and Species Consanguinity." Toxins 11, no. 2 (January 24, 2019): 68. http://dx.doi.org/10.3390/toxins11020068.

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Selenocosmia jiafu (S. jiafu) has been recently identified as a new species of spider in China. It lives in the same habitat as various other venomous spiders, including Chilobrachys jingzhao (C. jingzhao), Selenocosmia huwena (S. huwena), and Macrothele raveni (M. raveni). The venom from these different species of spiders exhibits some similarities and some differences in terms of their biochemical and electrophysiological properties. With the objective to illustrate the diversity in venom peptide toxins and to establish the evolutionary relationship between different spider species, we first performed transcriptomic analysis on a cDNA library from the venom gland of S. jiafu. We identified 146 novel toxin-like sequences, which were classified into eighteen different superfamilies. This transcriptome was then compared with that of C. jingzhao, which revealed that the putative toxins from both spider venoms may have originated from the same ancestor, although novel toxins evolved independently in the two species. A BLAST search and pharmacological analysis revealed that the two venoms have similar sodium channel modulation activity. This study provides insights into the venom of two closely related species of spider, which will prove useful towards understanding the structure and function of their toxins.

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Xie, Chunfang, Laura-Oana Albulescu, Kristina B. M. Still, Julien Slagboom, Yumei Zhao, Zhengjin Jiang, Govert W. Somsen, Freek J. Vonk, Nicholas R. Casewell, and Jeroen Kool. "Varespladib Inhibits the Phospholipase A2 and Coagulopathic Activities of Venom Components from Hemotoxic Snakes." Biomedicines 8, no. 6 (June 17, 2020): 165. http://dx.doi.org/10.3390/biomedicines8060165.

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Phospholipase A2 (PLA2) enzymes are important toxins found in many snake venoms, and they can exhibit a variety of toxic activities including causing hemolysis and/or anticoagulation. In this study, the inhibiting effects of the small molecule PLA2 inhibitor varespladib on snake venom PLA2s was investigated by nanofractionation analytics, which combined chromatography, mass spectrometry (MS), and bioassays. The venoms of the medically important snake species Bothrops asper, Calloselasma rhodostoma, Deinagkistrodon acutus, Daboia russelii, Echis carinatus, Echis ocellatus, and Oxyuranus scutellatus were separated by liquid chromatography (LC) followed by nanofractionation and interrogation of the fractions by a coagulation assay and a PLA2 assay. Next, we assessed the ability of varespladib to inhibit the activity of enzymatic PLA2s and the coagulopathic toxicities induced by fractionated snake venom toxins, and identified these bioactive venom toxins and those inhibited by varespladib by using parallel recorded LC-MS data and proteomics analysis. We demonstrated here that varespladib was not only capable of inhibiting the PLA2 activities of hemotoxic snake venoms, but can also effectively neutralize the coagulopathic toxicities (most profoundly anticoagulation) induced by venom toxins. While varespladib effectively inhibited PLA2 toxins responsible for anticoagulant effects, we also found some evidence that this inhibitory molecule can partially abrogate procoagulant venom effects caused by different toxin families. These findings further emphasize the potential clinical utility of varespladib in mitigating the toxic effects of certain snakebites.

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Barua, Agneesh, and Alexander S. Mikheyev. "An ancient, conserved gene regulatory network led to the rise of oral venom systems." Proceedings of the National Academy of Sciences 118, no. 14 (March 29, 2021): e2021311118. http://dx.doi.org/10.1073/pnas.2021311118.

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Oral venom systems evolved multiple times in numerous vertebrates, enabling the exploitation of unique predatory niches. Yet how and when they evolved remains poorly understood. Up to now, most research on venom evolution has focused strictly on toxins. However, using toxins present in modern-day animals to trace the origin of the venom system is difficult, since they tend to evolve rapidly, show complex patterns of expression, and were incorporated into the venom arsenal relatively recently. Here we focus on gene regulatory networks associated with the production of toxins in snakes, rather than the toxins themselves. We found that overall venom gland gene expression was surprisingly well conserved when compared to salivary glands of other amniotes. We characterized the “metavenom network,” a network of ∼3,000 nonsecreted housekeeping genes that are strongly coexpressed with toxins and are primarily involved in protein folding and modification. Conserved across amniotes, this network was coopted for venom evolution by exaptation of existing members and the recruitment of new toxin genes. For instance, starting from this common molecular foundation, Heloderma lizards, shrews, and solenodon evolved venoms in parallel by overexpression of kallikreins, which were common in ancestral saliva and induce vasodilation when injected, causing circulatory shock. Derived venoms, such as those of snakes, incorporated novel toxins, though they still rely on hypotension for prey immobilization. These similarities suggest repeated cooption of shared molecular machinery for the evolution of oral venom in mammals and reptiles, blurring the line between truly venomous animals and their ancestors.

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Walker, Andrew A. "The evolutionary dynamics of venom toxins made by insects and other animals." Biochemical Society Transactions 48, no. 4 (August 5, 2020): 1353–65. http://dx.doi.org/10.1042/bst20190820.

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Animal venoms are recognised as unique biological systems in which to study molecular evolution. Venom use has evolved numerous times among the insects, and insects today use venom to capture prey, defend themselves from predators, or to subdue and modulate host responses during parasitism. However, little is known about most insect venom toxins or the mode and tempo by which they evolve. Here, I review the evolutionary dynamics of insect venom toxins, and argue that insects offer many opportunities to examine novel aspects of toxin evolution. The key questions addressed are: How do venomous animals evolve from non-venomous animals, and how does this path effect the composition and pharmacology of the venom? What genetic processes (gene duplication, co-option, neofunctionalisation) are most important in toxin evolution? What kinds of selection pressures are acting on toxin-encoding genes and their cognate targets in envenomated animals? The emerging evidence highlights that venom composition and pharmacology adapts quickly in response to changing selection pressures resulting from new ecological interactions, and that such evolution occurs through a stunning variety of genetic mechanisms. Insects offer many opportunities to investigate the evolutionary dynamics of venom toxins due to their evolutionary history rich in venom-related adaptations, and their quick generation time and suitability for culture in the laboratory.

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Kunalan, Sugita, Iekhsan Othman, Sharifah Syed Hassan, and Wayne Hodgson. "Proteomic Characterization of Two Medically Important Malaysian Snake Venoms, Calloselasma rhodostoma (Malayan Pit Viper) and Ophiophagus hannah (King Cobra)." Toxins 10, no. 11 (October 26, 2018): 434. http://dx.doi.org/10.3390/toxins10110434.

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Calloselasma rhodostoma (CR) and Ophiophagus hannah (OH) are two medically important snakes found in Malaysia. While some studies have described the biological properties of these venoms, feeding and environmental conditions also influence the concentration and distribution of snake venom toxins, resulting in variations in venom composition. Therefore, a combined proteomic approach using shotgun and gel filtration chromatography, analyzed by tandem mass spectrometry, was used to examine the composition of venoms from these Malaysian snakes. The analysis revealed 114 proteins (15 toxin families) and 176 proteins (20 toxin families) in Malaysian Calloselasma rhodostoma and Ophiophagus hannah species, respectively. Flavin monoamine oxidase, phospholipase A2, phosphodiesterase, snake venom metalloproteinase, and serine protease toxin families were identified in both venoms. Aminopeptidase, glutaminyl-peptide cyclotransferase along with ankyrin repeats were identified for the first time in CR venom, and insulin, c-type lectins/snaclecs, hepatocyte growth factor, and macrophage colony-stimulating factor together with tumor necrosis factor were identified in OH venom for the first time. Our combined proteomic approach has identified a comprehensive arsenal of toxins in CR and OH venoms. These data may be utilized for improved antivenom production, understanding pathological effects of envenoming, and the discovery of biologically active peptides with medical and/or biotechnological value.

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Fidelis Bekeh Ada, Kenneth Igbang Sunday, and Emmanuel Akomaye Ugbong. "Animal venoms." GSC Biological and Pharmaceutical Sciences 14, no. 1 (January 30, 2021): 047–54. http://dx.doi.org/10.30574/gscbps.2021.14.1.0371.

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Venoms are poisons or toxins of animal origin in which the animal that produce the toxins are capable of introducing the toxins into the body of the victims. Animals that produce toxins but lack the ability to introduce the toxins into their victims are said to be poisonous animals. Venoms are classified based on their site of action in the bodies of their victims. Thus, they classified into local, auto pharmacological, antihaemostic, neurological mascular cardiac and renal types; and based on the type of animal producing the venom, it is difficult to classify venom based on chemical constitution because of the fact that a particular venom is highly complex chemically with many reactive sites. The role venoms play on organisms in the environment is highlighted.

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Kazandjian, Taline D., Arif Arrahman, Kristina B. M. Still, Govert W. Somsen, Freek J. Vonk, Nicholas R. Casewell, Mark C. Wilkinson, and Jeroen Kool. "Anticoagulant Activity of Naja nigricollis Venom Is Mediated by Phospholipase A2 Toxins and Inhibited by Varespladib." Toxins 13, no. 5 (April 23, 2021): 302. http://dx.doi.org/10.3390/toxins13050302.

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Bites from elapid snakes typically result in neurotoxic symptoms in snakebite victims. Neurotoxins are, therefore, often the focus of research relating to understanding the pathogenesis of elapid bites. However, recent evidence suggests that some elapid snake venoms contain anticoagulant toxins which may help neurotoxic components spread more rapidly. This study examines the effects of venom from the West African black-necked spitting cobra (Naja nigricollis) on blood coagulation and identifies potential coagulopathic toxins. An integrated RPLC-MS methodology, coupled with nanofractionation, was first used to separate venom components, followed by MS, proteomics and coagulopathic bioassays. Coagulation assays were performed on both crude and nanofractionated N. nigricollis venom toxins as well as PLA2s and 3FTx purified from the venom. Assays were then repeated with the addition of either the phospholipase A2 inhibitor varespladib or the snake venom metalloproteinase inhibitor marimastat to assess whether either toxin inhibitor is capable of neutralizing coagulopathic venom activity. Subsequent proteomic analysis was performed on nanofractionated bioactive venom toxins using tryptic digestion followed by nanoLC-MS/MS measurements, which were then identified using Swiss-Prot and species-specific database searches. Varespladib, but not marimastat, was found to significantly reduce the anticoagulant activity of N. nigricollis venom and MS and proteomics analyses confirmed that the anticoagulant venom components mostly consisted of PLA2 proteins. We, therefore, conclude that PLA2s are the most likely candidates responsible for anticoagulant effects stimulated by N. nigricollis venom.

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Modahl, Cassandra M., Rajeev Kungur Brahma, Cho Yeow Koh, Narumi Shioi, and R. Manjunatha Kini. "Omics Technologies for Profiling Toxin Diversity and Evolution in Snake Venom: Impacts on the Discovery of Therapeutic and Diagnostic Agents." Annual Review of Animal Biosciences 8, no. 1 (February 15, 2020): 91–116. http://dx.doi.org/10.1146/annurev-animal-021419-083626.

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Snake venoms are primarily composed of proteins and peptides, and these toxins have developed high selectivity to their biological targets. This makes venoms interesting for exploration into protein evolution and structure–function relationships. A single venom protein superfamily can exhibit a variety of pharmacological effects; these variations in activity originate from differences in functional sites, domains, posttranslational modifications, and the formations of toxin complexes. In this review, we discuss examples of how the major venom protein superfamilies have diversified, as well as how newer technologies in the omics fields, such as genomics, transcriptomics, and proteomics, can be used to characterize both known and unknown toxins.Because toxins are bioactive molecules with a rich diversity of activities, they can be useful as therapeutic and diagnostic agents, and successful examples of toxin applications in these areas are also reviewed. With the current rapid pace of technology, snake venom research and its applications will only continue to expand.

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Dissertations / Theses on the topic "Venom toxins"

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Anderson, A. J. "Toxins from mamba venoms that facilitate neurotransmission." Thesis, University of Strathclyde, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.381141.

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Rowan, E. G. "The effect of snake venom phospolipase A2Ì² on neuromusclar transmission." Thesis, University of Strathclyde, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.382387.

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Alape-Girón, Alberto. "Immunochemical, biochemical and evolutionary studies on Micrurus nigrocinctus nigrocinctus venom toxins /." Stockholm, 1997. http://diss.kib.ki.se/1997/19971205alap/.

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Almeida, Diego Dantas. "Sequenciamento do genoma da serpente Bothrops jararaca para caracterização da estrutura gênica de toxinas." Universidade de São Paulo, 2016. http://www.teses.usp.br/teses/disponiveis/87/87131/tde-06042017-133600/.

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A Bothrops jararaca é a serpente de maior importância médica no Brasil. Vários estudos foram realizados com o objetivo de caracterizar os componentes do veneno de serpentes, entretanto, a base molecular dos genomas das serpentes é pouco conhecida. Assim, foi realizado o sequenciamento e montagem do genoma da serpente Bothrops jararaca. Foram construídas bibliotecas tipo shotgun e mate-pair para realização de corridas de sequenciamento usando a tecnologia Illumina e sequências complementares foram obtidas em equipamento PACBIO RS II. Uma biblioteca de BACs também foi construída e 768 pools de 12 BACs foram sequenciados. Um grande conjunto de segmentos genômicos foi obtido e foi possível identificar genes de várias toxinas, entre elas SVMPs, SVSPs, BPPs, CRISPs e VEGF. Ainda foi possível depreender o contexto genômico de muitos destes genes e identificamos os principais elementos repetitivos genômicos. Estes achados são relevantes para o entendimento da função e evolução do sistema venenífero e podem servir de base para outros estudos futuramente.
The pit viper Bothrops jararaca is the most medically important snake in Brazil. Several studies were conducted in order to characterize the components of snake venom. However, the molecular basis of snake genomes is poorly known. Hence, it was carried out the sequencing and assembly of the Bothrops jararaca snake genome. Shotgun and mate-pair libraries were constructed to perform sequencing runs using Illumina technology and complementary sequences were obtained in PACBIO RS II equipment. A BAC library was also constructed and 768 pools of 12 BACs were sequenced. A large number of genomic segments was obtained. It was possible to identify genes of several toxins, including SVMPs, SVSPs, BPPs, CRISPs and VEGF. In addition, it was possible to infer the genomic context related to most of these genes and identify the main genomic repetitive elements. These findings are relevant for understanding the function and evolution of the venom system and it provides the basis for further studies.

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Cocchi, Fernando Kamimura [UNESP]. "Síntese e caracterização de pequenos peptídeos lineares do veneno de Tityus serrulatus (Buthidae)." Universidade Estadual Paulista (UNESP), 2016. http://hdl.handle.net/11449/137748.

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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
Os escorpiões são artrópodes da classe Arachnida, ordem Scorpiones. São animais peçonhentos, ou seja, possuem órgão secretório ou glândulas conectadas a um dispositivo de injeção, o qual pode inocular o veneno produzido pela glândula ou células especializadas. O veneno pode ser descrito como sendo uma mistura complexa, contendo muco, sais inorgânicos, moléculas orgânicas de baixa massa molecular, muitos peptídeos neurotóxicos e proteínas. O envenenamento humano por picada de escorpião é um importante problema de saúde pública em vários países tropicais e subtropicais. No Brasil, Tityus serrulatus é uma das espécies mais perigosas, que causam grave envenenamento, podendo levar ao óbito. Em geral, o envenenamento pode causar sintomas de dor, febre, agitação psicomotora, salivação, lacrimejamento, aumento da mobilidade do trato gastrointestinal, insuficiência respiratória e arritmia cardíaca, hipertensão arterial seguida de hipotensão, insuficiência cardíaca, edema pulmonar e choque anafilático. O veneno dos escorpiões tem sido estudado ao longo dos anos, a fim de elucidar seus compostos juntamente com suas sequências e suas funções biológicas. Algumas espécies de escorpiões possuem em seu veneno compostos antimicrobianos, mediadores que ativam os processos inflamatórios, causam a desgranulação de mastócitos, como também, podem ser capazes de induzir quimiotaxia de neutrófilos. Até o presente momento a toxinologia de escorpiões tem concentrado o foco nas neurotoxinas, que são peptídeos contendo entre 30 e 70 resíduos de aminoácidos em suas sequências, com quatro ou cinco pontes dissulfeto em suas estruturas. A despeito de existir muitos pequenos peptídeos (apresentando entre 5 e 20 resíduos de aminoácidos em suas sequências), que apresentam conformações lineares, por não apresentarem pontes dissulfeto em suas estruturas, este grupo de toxinas tem sido negligenciado pela literatura, devido à dificuldade em isolar e determinar suas estruturas moleculares. O presente trabalho teve como objetivo sintetizar alguns destes peptídeos (Typep-14, -15, -16, -17, and -18), previamente isolados e sequenciados a partir do veneno do escorpião T. serrulatus, por nosso grupo de pesquisas, e caracterizá-los de acordo com suas possíveis funções biológicas através de ensaios de desgranulação de mastócitos e liberação de lactato desidrogenase, hemólise, antibiose, efeitos hiperalgésicos e edematogênicos, e teste de campo aberto. Nenhum peptídeo apresentou atividade hemolítica, antibiótica; ou apresentou atividade desgranuladora de mastócito e liberação de LDH em ratos. Apenas o TyPep 18 apresentou alterações na locomoção de camundongos. Em geral, todos apresentaram ações de hiperalgesia ou formação de edemas localizados. Conclui-se portanto, que os peptídeos ensaiados no presente trabalho estão relacionados à produção de dor e inflamação.
Scorpions are arthropods of the class Arachnida, order Scorpiones. They are venonous animals, i. e, they have secretory organ or gland connected to an injection apparatus, which can inoculate the venom produced by specialized cells. The venom can be described as a complex mixture containing mucus, inorganic salts, organic molecules of low molecular mass, many neurotoxic peptides and proteins. The human enenvenoming by scorpion sting is an important problem of public health in many tropical and subtropical countries. In Brazil, Tityus serrulatus is one of the most dangerous species, which cause severe enenvenoming, that can lead to death. In general, the envenoming can cause symptoms of pain, fever, agitation, salivation, lacrimation, increasing motility of the gastrointestinal tract, respiratory failure and cardiac arrhythmia, hypertension followed by hypotension, heart failure, pulmonary edema and anaphylaxis. The venom of scorpions has been studied over the years in order to elucidate their biochemical composition, along with their sequences and biological functions. Some species of scorpions have antimicrobial compounds in their venom, mediators that trigger inflammatory processes, causing mast cell degranulation, and also may be capable of inducing neutrophil chemotaxis. To date, the toxinology of scorpions has concentrated the focus on neurotoxins, which are peptides containing between 30 and 70 amino acid residues in their sequences, with four or five disulfide bonds in their structures. Despite the existence of many small peptides (having between 5 and 20 amino acid residues in their sequences), that have linear conformations for not having disulfide bonds in their structures, this group of toxins has been neglected in the literature, due to the difficulty in isolating and determine molecular structures of these toxins. This study aimed to synthesize some of these peptides (Typep-14, -15, -16, -17, and -18) previously isolated and sequenced from T. serrulatus scorpion venom, by our research group, and characterize them according to their possible biological functions through mast cell degranulation and lactate dehydrogenase release test, hemolysis, antibiosis, hyperalgesic and edematogênics effects and open field test. None of the peptides presented hemolytic, antibiotic activity, mast cell degranulation or LDH release in rats. Only TyPep 18 influenced the pattern of locomotion in mice. In general, all peptides had presented hyperalgesic and edematogenic effects. It may be concluded that the peptides tested in this study are related to the production of pain and inflammation.
CAPES: 1208/2011

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Silva, Delano Aníbal da. "Atividades biológicas de peçonhas de vespa (Polistes lanio lanio) e formiga (Paraponera clavata)." [s.n.], 2011. http://repositorio.unicamp.br/jspui/handle/REPOSIP/312158.

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Orientador: Stephen Hyslop
Tese (doutorado) - Universidade Estadual de Campinas, Faculdade de Ciências Médicas
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Resumo: As peçonhas de himenópteros contêm diversas toxinas que podem causar hemólise, cardiotoxicidade e insuficiência renal, além de reação de hipersensibilidade. Adicionalmente, algumas vespas e formigas utilizam sua peçonha para imobilizar ou matar a presa. Neste estudo analisamos as atividades fosfolipásica (PLA2) e hemolítica bem como a atividade biológica sobre íleo e átrio isolados de rato, e sobre coração semi-isolado de barata, das peçonhas de formiga (Paraponera clavata) e vespa (Polistes lanio lanio). A eletroforese das peçonhas (SDS-PAGE) revelou a presença de componentes com massas moleculares de ~22 kDa a 100 kDa em P. clavata e de 19 a 119 kDa em P. l. lanio. Já a cromatografia por gel filtração resultou em cinco picos principais para a peçonha de P. clavata e seis para a de P. l. lanio. A peçonha de P. clavata possuiu atividades PLA2 e hemolítica moderadas, que foram abolidas pelo aquecimento (100ºC, 20 min). A peçonha de P. clavata (0,1-3 ?g/ml) contraiu íleo isolado de rato, cujo efeito foi dessensibilizante e resistente ao aquecimento da peçonha. Esta atividade contraturante foi localizada no primeiro pico do perfil de eluição da cromatografia por gel filtração. Em átrio isolado de rato a peçonha de P. clavata (0,125-10 ?g/ml) causou contratura, resultando em diminuição da força contrátil e redução na freqüência atrial com aumento na liberação de creatinoquinase-MB (CK-MB) tecidual. O aquecimento da peçonha não aboliu esta ação atrial. A análise histopatológica mostrou necrose dos cardiomiócitos que não foi afetada pelo aquecimento. Dos picos obtidos por gel filtração, o pico 1 reproduziu a contratura causada pela peçonha enquanto o pico 3 aumentou a contratilidade atrial. Em coração semi-isolado de barata, a peçonha de P. clavata (1-100 ?g) causou bradicardia. Conclui-se que a peçonha de P. clavata: (1) possui atividades PLA2 e hemolítica que são termolábeis, (2) causa bradicardia em coração semi-isolado de barata, e (3) provoca contração em íleo isolado e contratura em átrio direito de rato. Ao contrário de P. clavata, a peçonha de P. l. lanio (0,3-100 ?g/ml) mostrou altas atividades PLA2 e hemolítica que também foram abolidas pelo aquecimento (100ºC, 20 min). A peçonha contraiu íleo isolado de rato, e causou inotropismo negativo em átrio direito isolado de rato, sem afetar o cronotropismo; não houve contratura da linha basal. A peçonha causou forte bradicardia em coração semi-isolado de barata que não foi abolido pelo aquecimento (100ºC, 20 min). Este cronotropismo negativo foi mediado por uma fração da peçonha de P. l. lanio enriquecida em componentes de baixa massa molecular (<5 kDa, obtida através da ultrafiltração). A cromatografia desta fração em HPLC de fase reversa resultou em seis picos, dos quais apenas o pico 4 causou bradicardia em coração semi-isolado de barata. A bradicardia foi bloqueada pela glibenclamida, sugerindo o envolvimento de canais de K+ dependentes de ATP neste fenômeno. A análise do pico ativo por espectrometria de massas indicou a presença de peptídeos. Conclui-se que a peçonha de P. l. lanio: (1) tem alta atividade fosfolipásica e hemolítica (ambas termolábeis), (2) provoca contração de íleo e inotropismo negativo em átrio direito de rato e (3) exerce forte cronotropismo negativo em coração semi-isolado de barata mediado pela ativação de canais de potássio dependentes de ATP
Abstract: Hymenoptera venoms contain toxins that can cause hemolysis, renal failure, cardiotoxicity and hypersensitivity in humans. Additionally, some wasps and ants use their venom to immobilize or kill prey. In this study, we analyzed the phospholipase (PLA2) and hemolytic activities of ant (Paraponera clavata) and wasp (Polistes lanio lanio) venoms, and their action on rat isolated ileum and right atrium and cockroach semi-isolated heart. Electrophoresis (SDS-PAGE) showed that the venoms of P. clavata and P. l. lanio contained components with molecular masses of ~20-100 kDa and 19-119 kDa, respectively. Gel filtration chromatography resulted in five major peaks for P. clavata venom and six for P. l. lanio. Paraponera clavata venom had moderate phospholipase and hemolytic activities that were abolished by heating (100ºC, 20 min). This venom (0.1-3 ?g/ml) contracted rat isolated ileum, with a desensitizing effect, and heating the venom did not abolish this activity, which was located in the first peak of the gel filtration elution profile. In isolated atria, the venom (0.125-10 ?g/ml) caused muscle contraction that resulted in decreased contractile force and a reduction in atrial rate, with an increase in creatine kinase-MB (CK-MB) release; this atrial action was not abolished by heating. Histopathological analysis revealed myonecrosis that was also unaffected by heating. Of the peaks obtained by gel filtration, peak 1 reproduced the contraction observed with the venom whereas peak 3 caused a sustained increase in atrial contractility. The venom (1-100 ?g) caused bradycardia in cockroach semi-isolated hearts. These results show that P. clavata venom: (1) has PLA2 and hemolytic activities that are thermolabile, (2) causes bradycardia in cockroach semi-isolated hearts, and (3) contracts rat isolated ileum and causes contracture of rat right atria. In contrast to P. clavata, P. l. lanio venom (0.3-100 ?g/ml) showed high PLA2 and hemolytic activities that were also abolished by heating (100°C, 20 min). Polistes l. lanio venom contracted rat isolated ileum and produced negative inotropism in isolated rat right atria; there was no effect on the chronotropic response or on the baseline tension, i.e., no muscle contracture. The venom caused marked bradycardia in coackroach semi-isolated hearts that was unaffected by heating. This bradycardia was mediated by a low-molecular mass fraction of the venom (<5 kDa, obtained by ultrafiltration). RP-HPLC of this fraction resulted in six peaks, of which only the fourth caused bradycardia in cockroach semi-isolated hearts. This bradycardia was blocked by glibenclamide, suggesting the involvement of ATP-dependent K+ channel activation. Mass spectrometry of the active peak indicated the presence of peptides. These results indicate that P. l. lanio venom: (1) has high PLA2 and hemolytic activities that are thermolabile, (2) contracts rat isolated ileum and reduces the contractile force of isolated right atria, and (3) causes marked bradycardia in cockroach semi-isolated heart via the activation of ATP-dependent K+ channels
Doutorado
Farmacologia
Doutor em Farmacologia

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Inceoglu, A. Bora. "Identification of novel toxins from the venom of South African scorpion Parabuthus transvaalicus and characterization of a unique step of venom use in scorpions /." For electronic version search Digital dissertations database. Restricted to UC campuses. Access is free to UC campus dissertations, 2002. http://uclibs.org/PID/11984.

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Wickramaratna, Janith C. "A pharmacological characterisation of death adder (Acanthophis Spp.) venoms and toxins." Monash University, Dept. of Pharmacology, 2003. http://arrow.monash.edu.au/hdl/1959.1/5514.

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Thompson, Christopher Hal. "Identification and characterization of a peptide toxin inhibitor of ClC-2 chloride channels." Diss., Atlanta, Ga. : Georgia Institute of Technology, 2008. http://hdl.handle.net/1853/26604.

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Abstract:

Thesis (Ph.D)--Biology, Georgia Institute of Technology, 2009.
Committee Chair: McCarty, Nael; Committee Co-Chair: Harvey, Stephen; Committee Member: Hartzell, Criss; Committee Member: Kubanek, Julia; Committee Member: Lee, Robert. Part of the SMARTech Electronic Thesis and Dissertation Collection.

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Du, Plessis Lissinda Hester. "Electrophysiological effects of fractions isolated from the venom of Parabuthus granulatus on calcium channels in cardiac myocytes / L.H. du Plessis." Thesis, North-West University, 2004. http://hdl.handle.net/10394/577.

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Scorpion toxins specific for Na+ and K+ channels, have been studied extensively but relatively little has been done on Ca2+ channel toxins. Toxins in the venom of only two South African scorpions P. transvaalicus and P. granulatus have been found to interact with Ca2+ channels. Kurtoxin isolated from the venom of P. transvaalicus inhibits the T and L-type neuronal Ca2+ channels, whereas KLI and KLII (Kurtoxin-like peptide I and II), isolated from P. granulatus, inhibits T-type Ca2+ channel activity in mouse male germ cells. In this study the effects of fractions isolated from the venom of P. granularus on Cca2+ channels in rat ventricular myocytes were investigated by means of the whole-cell patch clamp technique. Fractions of P. granulatus crude venom were isolated with Sephadex G50 columns (fraction I-IV). Fraction III (PgIII) showed a voltage dependent increase of the inward Ca2+ current and influenced the channel kinetics by shifting the voltage dependence of activation towards more hyperpolarizing membrane potentials and decreased the rate of inactivation and deactivation. The time of the current to reach peak was also delayed. PgIII was further separated by HPLC in an attempt to identify the subfraction/s responsible for the agonistic effect. Subfraction I had an agonistic effect similar to PgIII, whereas subfraction II and III, decreased the Ca2+ current. The observed agonistic effect has not been described in the literature. The identification of new peptide structures with unique functions are important in the field of toxin research. Peptides that target Ca2+ channels can be valuable tools to characterize Ca2+ channels. Ca2+ channels in the heart are implicated in a number of pathological disorders like angina, ischemia, some arrhythmias and hypertension.
Thesis (M.Sc. (Physiology))--North-West University, Potchefstroom Campus, 2005.

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Books on the topic "Venom toxins"

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Snake venoms and envenomations. Malabar, Fla: Krieger Pub., 2006.

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Sutherland, Struan K. Australian animal toxins: The creatures, their toxins, and care of the poisoned patient. 2nd ed. South Melbourne: Oxford University Press, 2001.

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Simpósio, da ACIESP (12th 1988 São Paulo Brazil). Anais do XII Simpósio Anual da ACIESP sobre toxinas protéicas. [São Paulo]: Academia de Ciências do Estado de São Paulo, 1988.

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Nellis, David W. Poisonous Plants and Animals of Florida and the Caribbean. Sarasota, Florida: Pineapple Press, Inc., 1997.

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Gopalakrishnakone, P. Progress in venom and toxin research: Proceedings of the first Asia-Pacific congress on animal, plant andmicrobial toxins, held in Singapore, 24-27 June 1987. Singapore: National University of Singapore, 1987.

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P, Gopalakrishnakone, Tan C. K, International Society on Toxinology, and National University of Singapore. Venom and Toxin Research Group., eds. Progress in venom and toxin research: Proceedings of the First Asia-Pacific Congress on Animal, Plant and Microbial Toxins, held in Singapore, June 24-27, 1987. Singapore: National University of Singapore, 1987.

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ill, Shalvey Declan, ed. Venom: Toxin with a vengeance! New York: Marvel Worldwide, Inc., 2013.

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Gopalakrishnakone, P. Progress in venom and toxin research. Singapore: University of Singapore, 1987.

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Mackessy, Stephen P. Handbook of Venoms and Toxins of Reptiles. Edited by Stephen P. Mackessy. 2nd ed. Second edition. | Boca Raton : CRC Press, 2021.: CRC Press, 2021. http://dx.doi.org/10.1201/9780429054204.

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Marcussi, Silvana, Eliane Candiani Arantes, and Andreimar Martins Soares. Escorpiões: Biologia, envenenamento e mecanismos de ação de sua toxinas. São Paulo: FUNPEC Editora, 2011.

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Book chapters on the topic "Venom toxins"

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Chen, Jun, and Su-Min Guan. "Bee Venom and Pain." In Toxins and Drug Discovery, 1–34. Dordrecht: Springer Netherlands, 2015. http://dx.doi.org/10.1007/978-94-007-6726-3_1-1.

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Chen, Jun, and Su-Min Guan. "Bee Venom and Pain." In Toxins and Drug Discovery, 253–94. Dordrecht: Springer Netherlands, 2017. http://dx.doi.org/10.1007/978-94-007-6452-1_1.

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Rosing, Jan, and Guido Tans. "Snake Venom Prothrombin Activators – The History." In Toxins and Hemostasis, 485–99. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-9295-3_28.

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Bdolah, Avner. "Hypertensive and Hypotensive Snake Venom Components." In Toxins and Hemostasis, 655–72. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-9295-3_37.

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Fox, Eduardo Gonçalves Paterson. "Venom Toxins of Fire Ants." In Venom Genomics and Proteomics, 149–67. Dordrecht: Springer Netherlands, 2016. http://dx.doi.org/10.1007/978-94-007-6416-3_38.

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Strong, Peter N., and Jonathan D. F. Wadsworth. "Pharmacologically Active Peptides and Proteins from Bee Venom." In Animal Toxins, 127–51. Basel: Birkhäuser Basel, 2000. http://dx.doi.org/10.1007/978-3-0348-8466-2_9.

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Kini, R. Manjunatha. "Snake Venom Phospholipase A2 Enzymes in Cell Biology." In Animal Toxins, 304–18. Basel: Birkhäuser Basel, 2000. http://dx.doi.org/10.1007/978-3-0348-8466-2_19.

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Saviola, Anthony J., and Juan J. Calvete. "Reptile Venom Disintegrins." In Handbook of Venoms and Toxins of Reptiles, 211–24. 2nd ed. Second edition. | Boca Raton : CRC Press, 2021.: CRC Press, 2021. http://dx.doi.org/10.1201/9780429054204-17.

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Vogel, Carl-Wilhelm, Brian E. Hew, and David C. Fritzinger. "Cobra Venom Factor." In Handbook of Venoms and Toxins of Reptiles, 323–38. 2nd ed. Second edition. | Boca Raton : CRC Press, 2021.: CRC Press, 2021. http://dx.doi.org/10.1201/9780429054204-24.

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Ahmed, Mushtaq, Wasim Ahmad, Nadia Mushtaq, Rehmat Ali Khan, and Maria Rosa Chitolina Schetinger. "Reptile Venom Acetylcholinesterases." In Handbook of Venoms and Toxins of Reptiles, 445–52. 2nd ed. Second edition. | Boca Raton : CRC Press, 2021.: CRC Press, 2021. http://dx.doi.org/10.1201/9780429054204-33.

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Conference papers on the topic "Venom toxins"

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Hapeshi, Evroula, Sotirios Kyriacou, Michail Panagiotidis, Alexandra Primikyri, Eleftheria Galatou, Vicky Nicolaidou, Lefteris Zacharia, Constantina Eleftheriou, Socrates Tsinoglou, and Yiannis Sarigiannis. "First Exploration of the<em> Mesobuthus Cyprius</em> Venom." In 1st International Electronic Conference on Toxins. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/iect2021-09125.

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Ascoët, Steven, Michel Treilhou, Nathan Tene, Axel Touchard, Valentine Barasse, Jérôme Leprince, Arnaud Billet, and Elsa Bonnafe. "Analogous venom peptides acting on different pathways: a study of Bicarinalin and U<sub>9</sub>-MYRTX-Tb1a from <em>T. bicarinatum</em> venom." In 1st International Electronic Conference on Toxins. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/iect2021-09121.

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Fusco, Luciano, Laura Leiva, David Hernández, and Stephen Hyslop. "Biological activities of phosphodiesterase from <em>Crotalus durissus terrificus</em> venom." In 1st International Electronic Conference on Toxins. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/iect2021-09122.

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de Roodt, Adolfo, Daniel Dozoretz, Fernando Morón Goñi, Marcela Desio, Laura Lanari, and Carlos Damin. "Use of neostigmine - atropine plus antivenom in the experimental envenomation by Micrurus venom. Preliminary results." In 1st International Electronic Conference on Toxins. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/iect2021-09119.

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D'Amélio, Fernanda, Irina Kerkis, Hugo Barros, Álvaro Silva, Eduardo Frare, Isabel Batista, and Daniel Pimenta. "<em>Bothrops moojeni</em> venom: a new tool to investigate osteoclasts differentiation." In 1st International Electronic Conference on Toxins. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/iect2021-09136.

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Tonello, Fiorella, and Caterina Peggion. "<em>In silico</em> analysis of short linear motifs present in snake venom phospholipases A2." In 1st International Electronic Conference on Toxins. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/iect2021-09137.

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Arantes, Eliane, Beatriz Jacob, Francielle Cordeiro, Iara Cardoso, and Gisele Wiezel. "Expression and purification of rTs7, a recombinant toxin from <em>Tityus serrulatus</em> scorpion venom." In 1st International Electronic Conference on Toxins. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/iect2021-09128.

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Sanchez, Elda, Emelyn Salazar, Kassandra Rodriguez, and Montamas Suntravat. "Biological characterization of a Kunitz-type inhibitor from the Malaysian King cobra (<em>Ophiophagus hannah</em>) venom." In 1st International Electronic Conference on Toxins. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/iect2021-09144.

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Harvey, Merideth, Elda Sánchez, Emelyn Salazar, Oscar Sanchez, and Montamas Suntravat. "Exploration of the biological effects of a basic Phospholipase A2 from <em>Agkistrodon piscivorus piscivorus </em>venom." In 1st International Electronic Conference on Toxins. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/iect2021-09118.

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Fitches, Elaine C. "Beyond Bt: Exploiting arachnid venom peptide toxins to control crop pests." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.107005.

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Reports on the topic "Venom toxins"

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Krishnamurthy, Thaiya. Investigation on Toxins and Venoms by Novel MS Techniques. Mass Spectral Investigations on Blue-Green Algal Toxic Peptides and Other Toxins. Fort Belvoir, VA: Defense Technical Information Center, August 1990. http://dx.doi.org/10.21236/ada246914.

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