The open toxinology journal最新文献

{"title":"Toxinology","authors":"J. Duffus, Monica Nordberg, Douglas M. Templeton","doi":"10.1351/goldbook.t06419","DOIUrl":"https://doi.org/10.1351/goldbook.t06419","url":null,"abstract":"In recent years, the field of toxinology has expanded substantially. On the one hand it studies venomous animals, plants and micro organisms in detail to understand their mode of action on targets. While on the other, it explores the biochemical composition, genomics and proteomics of toxins and venoms to understand their three interaction with life forms (especially humans), development of antidotes and exploring their pharmacological potential. Therefore, toxinology has deep linkages with biochemistry, molecular biology, anatomy and pharmacology. In addition, there is a fast-developing applied subfield, clinical toxinology, which deals with understanding and managing medical effects of toxins on human body. Given the huge impact of toxin-based deaths globally, and the potential of venom in generation of drugs for so-far incurable diseases (for example, diabetes, chronic pain), the continued research and growth of the field is imminent. This has led to the growth of research in the area and the consequent scholarly output by way of publications in journals and books. Despite this ever-growing body of literature within biomedical sciences, there is still no all-inclusive reference work available that collects all of the important biochemical, biomedical and clinical insights relating to toxinology. Composed of 12 volumes, Toxinology provides comprehensive and authoritative coverage of the main areas in toxinology, from fundamental concepts to new developments and applications in the field. Each volume comprises a focused and carefully chosen collection of contributions from leading names in the subject. Series Titles 1. Biological Toxins and Bioterrorism 2. Clinical Toxinology in Asia Pacific and Africa 3. Spider Venoms 4. Scorpion Venoms 5. Marine and Freshwater Toxins 6. Venom Genomics and Proteomics 7. Snake Venoms 8. Evolution of Venomous Animals and Their Venoms 9. Microbial Toxins 10. Plant Toxins 11. Toxins and Drug Discovery 12. Clinical Toxinology in Australia, America, and Europe","PeriodicalId":90367,"journal":{"name":"The open toxinology journal","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76363170","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural Basis of Pore Formation by Mosquito-larvicidal Proteins from Bacillus thuringiensis","authors":"C. Angsuthanasombat","doi":"10.2174/1875414701003010119","DOIUrl":"https://doi.org/10.2174/1875414701003010119","url":null,"abstract":"The insecticidal character of the three-domain Cry  -endotoxins produced by Bacillus thuringiensis during sporulation is believed to be caused by their capability to generate lytic pores in the target larval midgut cell membranes. This review describes toxic mechanisms with emphasis on the structural basis of pore formation by two closely related dipteran-specific toxins, Cry4Aa and Cry4Ba, which are highly toxic to mosquito larvae. One proposed toxic mechanism via an \"umbrella-like\" structure involves membrane penetration and pore formation by the � 4-� 5 transmembrane hairpin. The lipid-induced  -conformation of  7 could possibly serve as a lipid anchor required for an efficient insertion of the pore-forming hairpin into the bilayer membrane. Though current electron crystallographic data are still inadequate to provide such critical insights into the structural details of the Cry toxin-induced pore architecture, this pivotal evidence clearly reveals that the 65-kDa active toxin in association with the lipid membrane could exist in at least two different trimeric conformations, implying the closed and open states of a functional pore.","PeriodicalId":90367,"journal":{"name":"The open toxinology journal","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68119132","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Insecticidal Toxins from the Photorhabdus and Xenorhabdus Bacteria","authors":"S. Hinchliffe, Michelle C. Hares, Andrea Dowling, R. ffrench-Constant","doi":"10.2174/1875414701003010101","DOIUrl":"https://doi.org/10.2174/1875414701003010101","url":null,"abstract":"Insect pathogens are an excellent source of novel insecticidal agents with proven toxicity. In particular, bacteria from the genera Photorhabdus and Xenorhabdus are proving to be a genomic goldmine, encoding a multitude of insecticidal toxins. Some are highly specific in their target species, whilst others are more generalist, but all are of potential use in crop protection against insect pests. These astounding bacterial species are also turning out to be equipped to produce a vast range of anti-microbial compounds which could be of use to medical science. This review will cover the current knowledge of the lifecycles of the two genera and the potential role of the toxins in their biology, before a more in depth exploration of some of the best studied toxins and their potential use in agriculture.","PeriodicalId":90367,"journal":{"name":"The open toxinology journal","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68119645","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Staphylococcal and Streptococcal Superantigens: Basic Biology of Conserved Protein Toxins","authors":"Eileen A. Larkin, T. Krakauer, R. Ulrich, B. Stiles","doi":"10.2174/1875414701003010069","DOIUrl":"https://doi.org/10.2174/1875414701003010069","url":null,"abstract":"Staphylococcus aureus and Streptococcus pyogenes are gram-positive bacteria that possess great pathogenic potential in humans, causing numerous maladies such as arthritis, cutaneous infections, endocarditis, enterocolitis, food poisoning, pharyngitis, pneumonia, rheumatic fever, surgical site infections, and toxic shock. These prevalent pathogens produce various virulence factors that include the staphylococcal enterotoxins (SEs), toxic shock syndrome toxin-1 (TSST-1), and streptococcal pyrogenic exotoxins (SPEs). Minute (picomolar) amounts of these structurally-similar \"superantigens\" (SAgs) elicit high levels of proinflammatory cytokines and chemokines that can induce fever, hypotension, and lethal shock. In vitro and in vivo models have provided important tools for studying the biological effects of, and potential vaccines plus therapeutics against, these related protein toxins. This review will delve into the known physical and biological properties of the SEs, TSST-1, and SPEs. The reader will hopefully derive a general appreciation of these wonderfully-complex, structurally-similar toxins produced by S. aureus and S. pyogenes.","PeriodicalId":90367,"journal":{"name":"The open toxinology journal","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68119556","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mosquito Resistance to Bacterial Larvicidal Toxins","authors":"M. Wirth","doi":"10.2174/1875414701003010126","DOIUrl":"https://doi.org/10.2174/1875414701003010126","url":null,"abstract":"Insecticide resistance to the microbial insecticides Bacillus thuringiensis subsp. israelensis (Bti) and Bacillus sphaericus (Bs) represents a serious threat to their success. Available evidence indicates that the risk for resistance to Bti is low due to the makeup of its parasporal crystal, which contains Cyt1A, Cry4A, Cry4B, and Cry11A toxic proteins. Disrupting the toxin complex in Bti enables resistance to evolve, especially in the absence of the key factor, the cytolytic toxin, Cyt1A. Cross-resistance is widespread among mosquitocidal Bacillus thuringiensis Cry toxins and the mechanisms of Cry resistance in mosquitoes are not known. Bacillus sphaericus (Bs) is at higher risk for resistance due to its single- site action and field cases have been reported from a number of locations worldwide. Cross-resistance is reported among the various Bs isolates, although some isolates produce additional toxic proteins that can reduce cross-resistance and slow resistance evolution. Field and lab evolved resistant populations consistently show recessive and monofactorial inheritance of resistance. Resistant populations, however, have evolved a variety of molecular mechanisms causing that resistance. Traditional resistance management strategies with promise include rotations and mixtures of Bti and Bs, as well as untreated areas that provide natural refuges for susceptible alleles. Promising new strategies include genetic engineering to increase the toxin complexity targeted toward mosquito larvae, to enhance the host range of the mosquito control product, and to avoid the evolution of insecticide resistance. Regardless of the control strategy, a resistance- monitoring program alongside an integrative pest management approach is the best strategy to delay insecticide resistance.","PeriodicalId":90367,"journal":{"name":"The open toxinology journal","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68119143","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The Aerolysin-Like Toxin Family of Cytolytic, Pore-Forming Toxins","authors":"O. Knapp, B. Stiles, M. Popoff","doi":"10.2174/1875414701003010053","DOIUrl":"https://doi.org/10.2174/1875414701003010053","url":null,"abstract":"Pore-forming toxins (PFTs) represent the largest known group of bacterial protein toxins to date. Membrane insertion and subsequent pore-formation occurs after initial binding to cell-surface receptor and oligomerization. Aerolysin, a toxin produced by the Gram-negative bacterium Aeromonas hydrophila and related species, belongs to the PFT group and shares a common mechanism of action involving  -barrel structures resulting from the assembly of  - hairpins from individual toxin monomers into a heptamer. Aerolysin is also the name given to structurally and mechanistically related toxins called the aerolysin-like toxin family. A universal characteristic of this toxin family involves the diverse life forms that synthesize these proteins throughout Nature. Examples include: 1) epsilon-toxin and septicum-alpha-toxin produced by anaerobic, Gram-positive Clostridium species; 2) enterolobin by the Brazilian tree Enterolobium contortisiliquum; 3) a mushroom toxin Laetiporus sulphureus lectin (LSL); 4) mosquitocidal toxins (Mtxs) from the Gram-positive bacteria Bacillus sphaericus and parasporine-2 from Bacillus thuringiensis; and 6) hydralysins from the tiny aquatic animal Chlorohydra viridis. The following review provides an overview of the different members within the aerolysin-like toxin family.","PeriodicalId":90367,"journal":{"name":"The open toxinology journal","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68118570","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Glucosylation of Rho/Ras Proteins by Lethal Toxin – Implications of Actin Re-Organization and Apoptosis in C. Sordellii-Associated Disease","authors":"H. Genth, F. Schulz, I. Just","doi":"10.2174/1875414701003010013","DOIUrl":"https://doi.org/10.2174/1875414701003010013","url":null,"abstract":"Clostridium sordellii causes disease in livestock and life-threatening illnesses in humans. Pathogenic C. sordellii strains produce up to seven virulence factors, including lethal toxin (TcsL), hemorrhagic toxin, a hemolysin, a DNAse, a collagenase, and a lysolecithinase cell. TcsL exhibits an A-B toxin-like structure and enters its target cells by receptor-mediated endocytosis. Inside the, TcsL mono-glucosylates low molecular weight GTP-binding proteins of the Ras and Rho families. This article reviews recent progress for (i) re-enforcing (H/K/N)Ras glucosylation and subsequent inhibition of the phosphoinositide 3-kinase (PI3K) / Akt survival signalling pathway as the cause of TcsL-induced apoptotic cell death, and (ii) showing the critical nature of Rac1 glucosylation in the loss of epithelial and endothelial barrier function. Finally, the detection of TcsL-induced glucosylation of Rac1 and (H/K/N)Ras using glucosylation- sensitive antibodies is presented as a new method to track TcsL activity.","PeriodicalId":90367,"journal":{"name":"The open toxinology journal","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68118391","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Clostridium Perfringens Toxins Involved in Mammalian Veterinary Diseases","authors":"F. Uzal, J. Vidal, B. McClane, A. Gurjar","doi":"10.2174/1875414701003010024","DOIUrl":"https://doi.org/10.2174/1875414701003010024","url":null,"abstract":"Clostridium perfringens is a gram-positive anaerobic rod that is classified into 5 toxinotypes (A, B, C, D, and E) according to the production of 4 major toxins, namely alpha (CPA), beta (CPB), epsilon (ETX) and iota (ITX). However, this microorganism can produce up to 16 toxins in various combinations, including lethal toxins such as perfringolysin O (PFO), enterotoxin (CPE), and beta2 toxin (CPB2). Most diseases caused by this microorganism are mediated by one or more of these toxins. The role of CPA in intestinal disease of mammals is controversial and poorly documented, but there is no doubt that this toxin is essential in the production of gas gangrene of humans and several animal species. CPB produced by C. perfringens types B and C is responsible for necrotizing enteritis and enterotoxemia mainly in neonatal individuals of several animal species. ETX produced by C. perfringens type D is responsible for clinical signs and lesions of enterotoxemia, a predominantly neurological disease of sheep and goats. The role of ITX in disease of animals is poorly understood, although it is usually assumed that the pathogenesis of intestinal diseases produced by C. perfringens type E is mediated by this toxin. CPB2, a necrotizing and lethal toxin that can be produced by all types of C. perfringens, has been blamed for disease in many animal species, but little information is currently available to sustain or rule out this claim. CPE is an important virulence factor for C. perfringens type A gastrointestinal disease in humans and dogs; however, the data implicating CPE in other animal diseases remains ambiguous. PFO does not seem to play a direct role as the main virulence factor for animal diseases, but it may have a synergistic role with CPA-mediated gangrene and ETX-mediated enterotoxemia. The recent improvement of animal models for C. perfringens infection and the use of toxin gene knock-out mutants have demonstrated the specific pathogenic role of several toxins of C. perfringens in animal disease. These research tools are helping us to establish the role of each C. perfringens toxin in animal disease, to investigate the in vivo mechanism of action of these toxins, and to develop more effective vaccines against diseases produced by these microorganisms.","PeriodicalId":90367,"journal":{"name":"The open toxinology journal","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68118408","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Clostridium Botulinum C3 Exoenzyme: Rho-Inactivating Tool in Cell Biology and a Neurotrophic Agent","authors":"I. Just, Stefanie C. Huelsenbeck, H. Genth","doi":"10.2174/1875414701003010019","DOIUrl":"https://doi.org/10.2174/1875414701003010019","url":null,"abstract":"C3 exoenzyme from Clostridium botulinum is the prototype of bacterial ADP-ribosyltransferases, which selectively modifies the Rho isoforms RhoA, RhoB and RhoC by covalent attachment of an ADP-ribose moiety. ADP- ribosylation results in inactivation of cellular functions of Rho. Because of its highly restricted substrate specificity, C3 is an established tool in cell biology; to this end C3 is applied as a cell-permeable chimeric toxin. C3 is superior to other molecular biology techniques such as siRNA or knock down approaches as RhoA inactivation or knock down is intrinsically associated with RhoB activation except after C3 treatment. RhoA plays an essential role in axonal growth and repair after neuronal injury. For therapeutic purposes cell- permeable C3 is now locally administered to treat spinal cord injury. Recently, it was reported that ADP-ribosyltransferase activity is not essential for the neurotrophic effect of C3 and that a peptidic fragment of C3 acts neurotrophic.","PeriodicalId":90367,"journal":{"name":"The open toxinology journal","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68118398","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Iota Toxin, S Toxin and CDT: Members of the Same Class of Clostridial Binary Toxins in Feces of Humans and Other Animals","authors":"R. Carman, A. Stevens, C. Genheimer, T. Wilkins","doi":"10.2174/1875414701003010043","DOIUrl":"https://doi.org/10.2174/1875414701003010043","url":null,"abstract":"Some strains of Clostridium perfringens, Clostridium spiroforme and Clostridium difficile produce binary toxins known respectively as iota toxin, S toxin and CDT. Each toxin consists of two unlinked polypeptides (e.g. CDTa and CDTb) that only together have biological activity. Taking an historical perspective, we review the development and early use of assays employing the specific neutralization of a biological activity for the detection and quantification of binary toxin. The survey moves on to more recent immunological assays and culminates with a discussion of the relevance of binary toxin, especially CDT, in feces.","PeriodicalId":90367,"journal":{"name":"The open toxinology journal","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68118459","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}