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Arthropod Venom Components and Their Potential Usage
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Arthropod Venom Components and Their Potential Usage

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Animal Venoms".

Deadline for manuscript submissions: closed (31 July 2019) | Viewed by 128884

Printed Edition Available!
A printed edition of this Special Issue is available here.

Special Issue Editors

Prof. Dr. Katsuhiro Konno

E-Mail Website
Guest Editor
Institute of Natural Medicine, University of Toyama, Toyama 930-0194, Japan
Interests: chemistry (isolation, structure and synthesis) of natural products; solitary wasp and ant venom peptides; sea anemone toxins; spider toxins
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Gandhi Rádis-Baptista

E-Mail Website
Guest Editor
Laboratory of Biochemistry and Biotechnology, Institute for Marine Sciences, Federal University of Ceara, Fortaleza 60165-081, CE, Brazil
Interests: transcriptome of arthropods, cnidarians and other venomous animals; peptide engineering; anti-proliferative peptides; membranolytic peptides; regulatory peptides; molecular biology; pharmaceutical biotechnology
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Thousands of arthropod species, ranging from arachnids (spiders and scorpions) to hymenopterans (ants, bees, and wasps) and myriapods (centipedes), are venomous and utilize their venoms for both defending themselves and predating preys. These venoms are invariably harmful to humans, and some may cause serious injuries, e.g., those from scorpions, spiders, and wasps. On the other hand, arthropods’ venoms have been known as rich sources of biologically active compounds and have attracted the attention of toxin researchers for years. Especially in this century, venom component analysis has progressed much more than ever because of the great advances of analytical techniques, in particular, mass spectrometry and next-generation deep (DNA and RNA) sequencing. As such, proteomic and peptidomic analyses utilizing LC–MS, as well as transcriptomics - alone or in combination with proteomics, have made it possible to fully analyze venoms’ components, revealing a variety of novel peptide and protein toxins sequences and scaffolds, potentially useful as pharmacological research tools and for the development of highly selective peptide ligands and therapeutic leads. Because of their specificity for numerous ion-channel subtypes, including voltage- and ligand-gated ion channels, arthropod neurotoxins have been investigated to dissect and treat neurodegenerative diseases and control epileptic syndromes. This Special Issue will collect information on such progress, encouraging contributions on the chemical and biological characterization of venom components, not only peptides and proteins but also small molecules, their mechanisms of action, and the development of venom-derived peptide leads.

Prof. Dr. Katsuhiro Konno
Prof. Dr. Gandhi Rádis-Baptista
Guest Editors

Manuscript Submission Information

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Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • venom components
  • peptide toxins
  • protein toxins
  • proteomics
  • peptidomics
  • transcriptome
  • venomics
  • peptide ligand
  • peptide engineering
  • venom-derived peptide leads

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Published Papers (21 papers)

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Editorial

Jump to: Research, Review

4 pages, 240 KiB  
Editorial
Arthropod Venom Components and Their Potential Usage
by Gandhi Rádis-Baptista and Katsuhiro Konno
Toxins 2020, 12(2), 82; https://doi.org/10.3390/toxins12020082 - 25 Jan 2020
Cited by 14 | Viewed by 2805
Abstract
Arthropods comprise a predominant and well-succeeded phylum of the animal kingdom that evolved and diversified in millions of species grouped in four subphyla, namely, Chelicerata (arachnids), Crustacea, Myriapoda (centipedes), and Hexapoda (insects) [...] Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)

Research

Jump to: Editorial, Review

15 pages, 1796 KiB  
Article
Sa12b Peptide from Solitary Wasp Inhibits ASIC Currents in Rat Dorsal Root Ganglion Neurons
by Carmen Hernández, Katsuhiro Konno, Emilio Salceda, Rosario Vega, André Junqueira Zaharenko and Enrique Soto
Toxins 2019, 11(10), 585; https://doi.org/10.3390/toxins11100585 - 10 Oct 2019
Cited by 11 | Viewed by 3563
Abstract
In this work, we evaluate the effect of two peptides Sa12b (EDVDHVFLRF) and Sh5b (DVDHVFLRF-NH2) on Acid-Sensing Ion Channels (ASIC). These peptides were purified from the venom of solitary wasps Sphex argentatus argentatus and Isodontia harmandi, respectively. Voltage clamp recordings [...] Read more.
In this work, we evaluate the effect of two peptides Sa12b (EDVDHVFLRF) and Sh5b (DVDHVFLRF-NH2) on Acid-Sensing Ion Channels (ASIC). These peptides were purified from the venom of solitary wasps Sphex argentatus argentatus and Isodontia harmandi, respectively. Voltage clamp recordings of ASIC currents were performed in whole cell configuration in primary culture of dorsal root ganglion (DRG) neurons from (P7-P10) CII Long-Evans rats. The peptides were applied by preincubation for 25 s (20 s in pH 7.4 solution and 5 s in pH 6.1 solution) or by co-application (5 s in pH 6.1 solution). Sa12b inhibits ASIC current with an IC50 of 81 nM, in a concentration-dependent manner when preincubation application was used. While Sh5b did not show consistent results having both excitatory and inhibitory effects on the maximum ASIC currents, its complex effect suggests that it presents a selective action on some ASIC subunits. Despite the similarity in their sequences, the action of these peptides differs significantly. Sa12b is the first discovered wasp peptide with a significant ASIC inhibitory effect. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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17 pages, 5992 KiB  
Article
Identification of Aethina tumida Kir Channels as Putative Targets of the Bee Venom Peptide Tertiapin Using Structure-Based Virtual Screening Methods
by Craig A. Doupnik
Toxins 2019, 11(9), 546; https://doi.org/10.3390/toxins11090546 - 19 Sep 2019
Cited by 3 | Viewed by 3453
Abstract
Venoms are comprised of diverse mixtures of proteins, peptides, and small molecules. Identifying individual venom components and their target(s) with mechanism of action is now attainable to understand comprehensively the effectiveness of venom cocktails and how they collectively function in the defense and [...] Read more.
Venoms are comprised of diverse mixtures of proteins, peptides, and small molecules. Identifying individual venom components and their target(s) with mechanism of action is now attainable to understand comprehensively the effectiveness of venom cocktails and how they collectively function in the defense and predation of an organism. Here, structure-based computational methods were used with bioinformatics tools to screen and identify potential biological targets of tertiapin (TPN), a venom peptide from Apis mellifera (European honey bee). The small hive beetle (Aethina tumida (A. tumida)) is a natural predator of the honey bee colony and was found to possess multiple inwardly rectifying K+ (Kir) channel subunit genes from a genomic BLAST search analysis. Structure-based virtual screening of homology modelled A. tumida Kir (atKir) channels found TPN to interact with a docking profile and interface “footprint” equivalent to known TPN-sensitive mammalian Kir channels. The results support the hypothesis that atKir channels, and perhaps other insect Kir channels, are natural biological targets of TPN that help defend the bee colony from infestations by blocking K+ transport via atKir channels. From these in silico findings, this hypothesis can now be subsequently tested in vitro by validating atKir channel block as well as in vivo TPN toxicity towards A. tumida. This study highlights the utility and potential benefits of screening in virtual space for venom peptide interactions and their biological targets, which otherwise would not be feasible. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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12 pages, 1573 KiB  
Communication
The Influence of Bee Venom Melittin on the Functioning of the Immune System and the Contractile Activity of the Insect Heart—A Preliminary Study
by Jan Lubawy, Arkadiusz Urbański, Lucyna Mrówczyńska, Eliza Matuszewska, Agata Światły-Błaszkiewicz, Jan Matysiak and Grzegorz Rosiński
Toxins 2019, 11(9), 494; https://doi.org/10.3390/toxins11090494 - 27 Aug 2019
Cited by 16 | Viewed by 4042
Abstract
Melittin (MEL) is a basic polypeptide originally purified from honeybee venom. MEL exhibits a broad spectrum of biological activity. However, almost all studies on MEL activity have been carried out on vertebrate models or cell lines. Recently, due to cheap breeding and the [...] Read more.
Melittin (MEL) is a basic polypeptide originally purified from honeybee venom. MEL exhibits a broad spectrum of biological activity. However, almost all studies on MEL activity have been carried out on vertebrate models or cell lines. Recently, due to cheap breeding and the possibility of extrapolating the results of the research to vertebrates, insects have been used for various bioassays and comparative physiological studies. For these reasons, it is valuable to examine the influence of melittin on insect physiology. Here, for the first time, we report the immunotropic and cardiotropic effects of melittin on the beetle Tenebrio molitor as a model insect. After melittin injection at 10−7 M and 10−3 M, the number of apoptotic cells in the haemolymph increased in a dose-dependent manner. The pro-apoptotic action of MEL was likely compensated by increasing the total number of haemocytes. However, the injection of MEL did not cause any changes in the percent of phagocytic haemocytes or in the phenoloxidase activity. In an in vitro bioassay with a semi-isolated Tenebrio heart, MEL induced a slight chronotropic-positive effect only at a higher concentration (10−4 M). Preliminary results indicated that melittin exerts pleiotropic effects on the functioning of the immune system and the endogenous contractile activity of the heart. Some of the induced responses in T. molitor resemble the reactions observed in vertebrate models. Therefore, the T. molitor beetle may be a convenient invertebrate model organism for comparative physiological studies and for the identification of new properties and mechanisms of action of melittin and related compounds. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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27 pages, 18163 KiB  
Article
Bottom-Up Proteomic Analysis of Polypeptide Venom Components of the Giant Ant Dinoponera Quadriceps
by Douglas Oscar Ceolin Mariano, Úrsula Castro de Oliveira, André Junqueira Zaharenko, Daniel Carvalho Pimenta, Gandhi Rádis-Baptista and Álvaro Rossan de Brandão Prieto-da-Silva
Toxins 2019, 11(8), 448; https://doi.org/10.3390/toxins11080448 - 29 Jul 2019
Cited by 15 | Viewed by 4778
Abstract
Ant species have specialized venom systems developed to sting and inoculate a biological cocktail of organic compounds, including peptide and polypeptide toxins, for the purpose of predation and defense. The genus Dinoponera comprises predatory giant ants that inoculate venom capable of causing long-lasting [...] Read more.
Ant species have specialized venom systems developed to sting and inoculate a biological cocktail of organic compounds, including peptide and polypeptide toxins, for the purpose of predation and defense. The genus Dinoponera comprises predatory giant ants that inoculate venom capable of causing long-lasting local pain, involuntary shaking, lymphadenopathy, and cardiac arrhythmias, among other symptoms. To deepen our knowledge about venom composition with regard to protein toxins and their roles in the chemical–ecological relationship and human health, we performed a bottom-up proteomics analysis of the crude venom of the giant ant D. quadriceps, popularly known as the “false” tocandiras. For this purpose, we used two different analytical approaches: (i) gel-based proteomics approach, wherein the crude venom was resolved by denaturing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and all protein bands were excised for analysis; (ii) solution-based proteomics approach, wherein the crude venom protein components were directly fragmented into tryptic peptides in solution for analysis. The proteomic data that resulted from these two methodologies were compared against a previously annotated transcriptomic database of D. quadriceps, and subsequently, a homology search was performed for all identified transcript products. The gel-based proteomics approach unequivocally identified nine toxins of high molecular mass in the venom, as for example, enzymes [hyaluronidase, phospholipase A1, dipeptidyl peptidase and glucose dehydrogenase/flavin adenine dinucleotide (FAD) quinone] and diverse venom allergens (homologous of the red fire ant Selenopsis invicta) and venom-related proteins (major royal jelly-like). Moreover, the solution-based proteomics revealed and confirmed the presence of several hydrolases, oxidoreductases, proteases, Kunitz-like polypeptides, and the less abundant inhibitor cysteine knot (ICK)-like (knottin) neurotoxins and insect defensin. Our results showed that the major components of the D. quadriceps venom are toxins that are highly likely to damage cell membranes and tissue, to cause neurotoxicity, and to induce allergic reactions, thus, expanding the knowledge about D. quadriceps venom composition and its potential biological effects on prey and victims. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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14 pages, 1233 KiB  
Article
Pain and Lethality Induced by Insect Stings: An Exploratory and Correlational Study
by Justin O. Schmidt
Toxins 2019, 11(7), 427; https://doi.org/10.3390/toxins11070427 - 21 Jul 2019
Cited by 12 | Viewed by 11125
Abstract
Pain is a natural bioassay for detecting and quantifying biological activities of venoms. The painfulness of stings delivered by ants, wasps, and bees can be easily measured in the field or lab using the stinging insect pain scale that rates the pain intensity [...] Read more.
Pain is a natural bioassay for detecting and quantifying biological activities of venoms. The painfulness of stings delivered by ants, wasps, and bees can be easily measured in the field or lab using the stinging insect pain scale that rates the pain intensity from 1 to 4, with 1 being minor pain, and 4 being extreme, debilitating, excruciating pain. The painfulness of stings of 96 species of stinging insects and the lethalities of the venoms of 90 species was determined and utilized for pinpointing future directions for investigating venoms having pharmaceutically active principles that could benefit humanity. The findings suggest several under- or unexplored insect venoms worthy of future investigations, including: those that have exceedingly painful venoms, yet with extremely low lethality—tarantula hawk wasps (Pepsis) and velvet ants (Mutillidae); those that have extremely lethal venoms, yet induce very little pain—the ants, Daceton and Tetraponera; and those that have venomous stings and are both painful and lethal—the ants Pogonomyrmex, Paraponera, Myrmecia, Neoponera, and the social wasps Synoeca, Agelaia, and Brachygastra. Taken together, and separately, sting pain and venom lethality point to promising directions for mining of pharmaceutically active components derived from insect venoms. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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14 pages, 4664 KiB  
Article
Fire Ant Venom Alkaloids Inhibit Biofilm Formation
by Danielle Bruno de Carvalho, Eduardo Gonçalves Paterson Fox, Diogo Gama dos Santos, Joab Sampaio de Sousa, Denise Maria Guimarães Freire, Fabio C. S. Nogueira, Gilberto B. Domont, Livia Vieira Araujo de Castilho and Ednildo de Alcântara Machado
Toxins 2019, 11(7), 420; https://doi.org/10.3390/toxins11070420 - 18 Jul 2019
Cited by 15 | Viewed by 9444
Abstract
Biofilm formation on exposed surfaces is a serious issue for the food industry and medical health facilities. There are many proposed strategies to delay, reduce, or even eliminate biofilm formation on surfaces. The present study focuses on the applicability of fire ant venom [...] Read more.
Biofilm formation on exposed surfaces is a serious issue for the food industry and medical health facilities. There are many proposed strategies to delay, reduce, or even eliminate biofilm formation on surfaces. The present study focuses on the applicability of fire ant venom alkaloids (aka ‘solenopsins’, from Solenopsis invicta) tested on polystyrene and stainless steel surfaces relative to the adhesion and biofilm-formation by the bacterium Pseudomonas fluorescens. Conditioning with solenopsins demonstrates significant reduction of bacterial adhesion. Inhibition rates were 62.7% on polystyrene and 59.0% on stainless steel surfaces. In addition, solenopsins drastically reduced cell populations already growing on conditioned surfaces. Contrary to assumptions by previous authors, solenopsins tested negative for amphipathic properties, thus understanding the mechanisms behind the observed effects still relies on further investigation. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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10 pages, 2061 KiB  
Article
Analgesic Effect of Melittin on Oxaliplatin-Induced Peripheral Neuropathy in Rats
by Seunghwan Choi, Hyeon Kyeong Chae, Ho Heo, Dae-Hyun Hahm, Woojin Kim and Sun Kwang Kim
Toxins 2019, 11(7), 396; https://doi.org/10.3390/toxins11070396 - 08 Jul 2019
Cited by 23 | Viewed by 3955
Abstract
Oxaliplatin is a chemotherapeutic agent used for metastatic colon and other advanced cancers. Most common side effect of oxaliplatin is peripheral neuropathy, manifested in mechanical and cold allodynia. Although the analgesic effect of bee venom has been proven to be effective against oxaliplatin-induced [...] Read more.
Oxaliplatin is a chemotherapeutic agent used for metastatic colon and other advanced cancers. Most common side effect of oxaliplatin is peripheral neuropathy, manifested in mechanical and cold allodynia. Although the analgesic effect of bee venom has been proven to be effective against oxaliplatin-induced peripheral neuropathy, the effect of its major component; melittin has not been studied yet. Thus, in this study, we investigated whether melittin has an analgesic effect on oxaliplatin-induced allodynia. Intraperitoneal single injection of oxaliplatin (6 mg/kg) induced mechanical and cold allodynia, resulting in increased withdrawal behavior in response to von Frey filaments and acetone drop on hind paw. Subcutaneous melittin injection on acupoint ST36 (0.5 mg/kg) alleviated oxaliplatin-induced mechanical and cold allodynia. In electrophysiological study, using spinal in vivo extracellular recording, it was shown that oxaliplatin-induced hyperexcitation of spinal wide dynamic range neurons in response to peripheral stimuli, and melittin administration inhibited this neuronal activity. In behavioral assessment, analgesic effect of melittin was blocked by intrathecal α1- and α2- adrenergic receptor antagonists administration. Based on these results, we suggest that melittin could be used as an analgesic on oxaliplatin-induced peripheral neuropathy, and that its effect is mediated by activating the spinal α1- and α2-adrenergic receptors. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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21 pages, 2502 KiB  
Article
Chemical Synthesis, Proper Folding, Nav Channel Selectivity Profile and Analgesic Properties of the Spider Peptide Phlotoxin 1
by Sébastien Nicolas, Claude Zoukimian, Frank Bosmans, Jérôme Montnach, Sylvie Diochot, Eva Cuypers, Stephan De Waard, Rémy Béroud, Dietrich Mebs, David Craik, Didier Boturyn, Michel Lazdunski, Jan Tytgat and Michel De Waard
Toxins 2019, 11(6), 367; https://doi.org/10.3390/toxins11060367 - 21 Jun 2019
Cited by 18 | Viewed by 4750
Abstract
Phlotoxin-1 (PhlTx1) is a peptide previously identified in tarantula venom (Phlogius species) that belongs to the inhibitory cysteine-knot (ICK) toxin family. Like many ICK-based spider toxins, the synthesis of PhlTx1 appears particularly challenging, mostly for obtaining appropriate folding and concomitant suitable disulfide [...] Read more.
Phlotoxin-1 (PhlTx1) is a peptide previously identified in tarantula venom (Phlogius species) that belongs to the inhibitory cysteine-knot (ICK) toxin family. Like many ICK-based spider toxins, the synthesis of PhlTx1 appears particularly challenging, mostly for obtaining appropriate folding and concomitant suitable disulfide bridge formation. Herein, we describe a procedure for the chemical synthesis and the directed sequential disulfide bridge formation of PhlTx1 that allows for a straightforward production of this challenging peptide. We also performed extensive functional testing of PhlTx1 on 31 ion channel types and identified the voltage-gated sodium (Nav) channel Nav1.7 as the main target of this toxin. Moreover, we compared PhlTx1 activity to 10 other spider toxin activities on an automated patch-clamp system with Chinese Hamster Ovary (CHO) cells expressing human Nav1.7. Performing these analyses in reproducible conditions allowed for classification according to the potency of the best natural Nav1.7 peptide blockers. Finally, subsequent in vivo testing revealed that intrathecal injection of PhlTx1 reduces the response of mice to formalin in both the acute pain and inflammation phase without signs of neurotoxicity. PhlTx1 is thus an interesting toxin to investigate Nav1.7 involvement in cellular excitability and pain. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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21 pages, 3309 KiB  
Article
Dissecting Toxicity: The Venom Gland Transcriptome and the Venom Proteome of the Highly Venomous Scorpion Centruroides limpidus (Karsch, 1879)
by Jimena I. Cid-Uribe, Erika P. Meneses, Cesar V. F. Batista, Ernesto Ortiz and Lourival D. Possani
Toxins 2019, 11(5), 247; https://doi.org/10.3390/toxins11050247 - 30 Apr 2019
Cited by 23 | Viewed by 5815
Abstract
Venom glands and soluble venom from the Mexican scorpion Centruroides limpidus (Karsch, 1879) were used for transcriptomic and proteomic analyses, respectively. An RNA-seq was performed by high-throughput sequencing with the Illumina platform. Approximately 80 million reads were obtained and assembled into 198,662 putative [...] Read more.
Venom glands and soluble venom from the Mexican scorpion Centruroides limpidus (Karsch, 1879) were used for transcriptomic and proteomic analyses, respectively. An RNA-seq was performed by high-throughput sequencing with the Illumina platform. Approximately 80 million reads were obtained and assembled into 198,662 putative transcripts, of which 11,058 were annotated by similarity to sequences from available databases. A total of 192 venom-related sequences were identified, including Na+ and K+ channel-acting toxins, enzymes, host defense peptides, and other venom components. The most diverse transcripts were those potentially coding for ion channel-acting toxins, mainly those active on Na+ channels (NaScTx). Sequences corresponding to β- scorpion toxins active of K+ channels (KScTx) and λ-KScTx are here reported for the first time for a scorpion of the genus Centruroides. Mass fingerprint corroborated that NaScTx are the most abundant components in this venom. Liquid chromatography coupled to mass spectometry (LC-MS/MS) allowed the identification of 46 peptides matching sequences encoded in the transcriptome, confirming their expression in the venom. This study corroborates that, in the venom of toxic buthid scorpions, the more abundant and diverse components are ion channel-acting toxins, mainly NaScTx, while they lack the HDP diversity previously demonstrated for the non-buthid scorpions. The highly abundant and diverse antareases explain the pancreatitis observed after envenomation by this species. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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11 pages, 2092 KiB  
Article
Isolation and Characterization of Insecticidal Toxins from the Venom of the North African Scorpion, Buthacus leptochelys
by Yusuke Yoshimoto, Masahiro Miyashita, Mohammed Abdel-Wahab, Moustafa Sarhan, Yoshiaki Nakagawa and Hisashi Miyagawa
Toxins 2019, 11(4), 236; https://doi.org/10.3390/toxins11040236 - 25 Apr 2019
Cited by 8 | Viewed by 4410
Abstract
Various bioactive peptides have been identified in scorpion venom, but there are many scorpion species whose venom has not been investigated. In this study, we characterized venom components of the North African scorpion, Buthacus leptochelys, by mass spectrometric analysis and evaluated their [...] Read more.
Various bioactive peptides have been identified in scorpion venom, but there are many scorpion species whose venom has not been investigated. In this study, we characterized venom components of the North African scorpion, Buthacus leptochelys, by mass spectrometric analysis and evaluated their insect toxicity. This is the first report of chemical and biological characterization of the B. leptochelys venom. LC/MS analysis detected at least 148 components in the venom. We isolated four peptides that show insect toxicity (Bl-1, Bl-2, Bl-3, and Bl-4) through bioassay-guided HPLC fractionation. These toxins were found to be similar to scorpion α- and β-toxins based on their N-terminal sequences. Among them, the complete primary structure of Bl-1 was determined by combination of Edman degradation and MS/MS analysis. Bl-1 is composed of 67 amino acid residues and crosslinked with four disulfide bonds. Since Bl-1 shares high sequence similarity with α-like toxins, it is likely that it acts on Na+ channels of both insects and mammals. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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9 pages, 741 KiB  
Article
Antiparasitic Properties of Cantharidin and the Blister Beetle Berberomeloe majalis (Coleoptera: Meloidae)
by Douglas W. Whitman, Maria Fe Andrés, Rafael A. Martínez-Díaz, Alexandra Ibáñez-Escribano, A. Sonia Olmeda and Azucena González-Coloma
Toxins 2019, 11(4), 234; https://doi.org/10.3390/toxins11040234 - 22 Apr 2019
Cited by 19 | Viewed by 7536
Abstract
Cantharidin (CTD) is a toxic monoterpene produced by blister beetles (Fam. Meloidae) as a chemical defense against predators. Although CTD is highly poisonous to many predator species, some have evolved the ability to feed on poisonous Meloidae, or otherwise beneficially use blister beetles. [...] Read more.
Cantharidin (CTD) is a toxic monoterpene produced by blister beetles (Fam. Meloidae) as a chemical defense against predators. Although CTD is highly poisonous to many predator species, some have evolved the ability to feed on poisonous Meloidae, or otherwise beneficially use blister beetles. Great Bustards, Otis tarda, eat CTD-containing Berberomeloe majalis blister beetles, and it has been hypothesized that beetle consumption by these birds reduces parasite load (a case of self-medication). We examined this hypothesis by testing diverse organisms against CTD and extracts of B. majalis hemolymph and bodies. Our results show that all three preparations (CTD and extracts of B. majalis) were toxic to a protozoan (Trichomonas vaginalis), a nematode (Meloidogyne javanica), two insects (Myzus persicae and Rhopalosiphum padi) and a tick (Hyalomma lusitanicum). This not only supports the anti-parasitic hypothesis for beetle consumption, but suggests potential new roles for CTD, under certain conditions. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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18 pages, 3884 KiB  
Article
Antimicrobial and Antibiofilm Effects of Peptides from Venom of Social Wasp and Scorpion on Multidrug-Resistant Acinetobacter baumannii
by Rogério Coutinho das Neves, Márcia Renata Mortari, Elisabeth Ferroni Schwartz, André Kipnis and Ana Paula Junqueira-Kipnis
Toxins 2019, 11(4), 216; https://doi.org/10.3390/toxins11040216 - 10 Apr 2019
Cited by 26 | Viewed by 5019
Abstract
Intravascular stent infection is a rare complication with a high morbidity and high mortality; bacteria from the hospital environment form biofilms and are often multidrug-resistant (MDR). Antimicrobial peptides (AMPs) have been considered as alternatives to bacterial infection treatment. We analyzed the formation of [...] Read more.
Intravascular stent infection is a rare complication with a high morbidity and high mortality; bacteria from the hospital environment form biofilms and are often multidrug-resistant (MDR). Antimicrobial peptides (AMPs) have been considered as alternatives to bacterial infection treatment. We analyzed the formation of the bacterial biofilm on the vascular stents and also tested the inhibition of this biofilm by AMPs to be used as treatment or coating. Antimicrobial activity and antibiofilm were tested with wasp (Agelaia-MPI, Polybia-MPII, Polydim-I) and scorpion (Con10 and NDBP5.8) AMPs against Acinetobacter baumannii clinical strains. A. baumannii formed a biofilm on the vascular stent. Agelaia-MPI and Polybia-MPII inhibited biofilm formation with bacterial cell wall degradation. Coating biofilms with polyethylene glycol (PEG 400) and Agelaia-MPI reduced 90% of A. baumannii adhesion on stents. The wasp AMPs Agelaia-MPI and Polybia-MPII had better action against MDR A. baumannii adherence and biofilm formation on vascular stents, preventing its formation and treating mature biofilm when compared to the other tested peptides. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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16 pages, 3749 KiB  
Article
A New Topical Eye Drop Containing LyeTxI-b, A Synthetic Peptide Designed from A Lycosa erithrognata Venom Toxin, Was Effective to Treat Resistant Bacterial Keratitis
by Carolina Nunes da Silva, Flavia Rodrigues da Silva, Lays Fernanda Nunes Dourado, Pablo Victor Mendes dos Reis, Rummenigge Oliveira Silva, Bruna Lopes da Costa, Paula Santos Nunes, Flávio Almeida Amaral, Vera Lúcia dos Santos, Maria Elena de Lima and Armando da Silva Cunha Júnior
Toxins 2019, 11(4), 203; https://doi.org/10.3390/toxins11040203 - 04 Apr 2019
Cited by 22 | Viewed by 5461
Abstract
Bacterial keratitis is an ocular infection that can lead to severe visual disability. Staphylococcus aureus is a major pathogen of the eye. We recently demonstrated the strong antimicrobial activity of LyeTxI-b, a synthetic peptide derived from a Lycosa erithrognatha toxin. Herein, we evaluated [...] Read more.
Bacterial keratitis is an ocular infection that can lead to severe visual disability. Staphylococcus aureus is a major pathogen of the eye. We recently demonstrated the strong antimicrobial activity of LyeTxI-b, a synthetic peptide derived from a Lycosa erithrognatha toxin. Herein, we evaluated a topical formulation (eye drops) containing LyeTxI-b to treat resistant bacterial keratitis. Keratitis was induced with intrastromal injection of 4 × 105 cells (4 µL) in New Zealand female white rabbits. Minimum inhibitory concentration (MIC) and biofilm viability were determined. LyeTxI-b ocular toxicity was evaluated through chorioallantoic membrane and Draize tests. One drop of the formulation (LyeTxI-b 28.9 µmol/L +0.5% CMC in 0.9% NaCl) was instilled into each eye four times a day, for a week. Slit-lamp biomicroscopy analysis, corneal histopathological studies and cellular infiltrate quantification through myeloperoxidase (MPO) and N-acetylglucosaminidase (NAG) detection were performed. LyeTxI-b was very effective in the treatment of keratitis, with no signs of ocular toxicity. Planktonic bacteria MIC was 3.6 µmol/L and LyeTxI-b treatment reduced biofilm viability in 90%. LyeTxI-b eliminated bacteria and reduced inflammatory cellular activity in the eyes. Healthy and treated animals showed similar NAG and MPO levels. LyeTxI-b is a potent new drug to treat resistant bacterial keratitis, showing effective antimicrobial and anti-inflammatory activity. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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21 pages, 2614 KiB  
Article
Design and Production of a Recombinant Hybrid Toxin to Raise Protective Antibodies against Loxosceles Spider Venom
by Paula A. L. Calabria, Lhiri Hanna A. L. Shimokawa-Falcão, Monica Colombini, Ana M. Moura-da-Silva, Katia C. Barbaro, Eliana L. Faquim-Mauro and Geraldo S. Magalhaes
Toxins 2019, 11(2), 108; https://doi.org/10.3390/toxins11020108 - 12 Feb 2019
Cited by 13 | Viewed by 4635
Abstract
Human accidents with spiders of the genus Loxosceles are an important health problem affecting thousands of people worldwide. Patients evolve to severe local injuries and, in many cases, to systemic disturbances as acute renal failure, in which cases antivenoms are considered to be [...] Read more.
Human accidents with spiders of the genus Loxosceles are an important health problem affecting thousands of people worldwide. Patients evolve to severe local injuries and, in many cases, to systemic disturbances as acute renal failure, in which cases antivenoms are considered to be the most effective treatment. However, for antivenom production, the extraction of the venom used in the immunization process is laborious and the yield is very low. Thus, many groups have been exploring the use of recombinant Loxosceles toxins, particularly phospholipases D (PLDs), to produce the antivenom. Nonetheless, some important venom activities are not neutralized by anti-PLD antibodies. Astacin-like metalloproteases (ALMPs) are the second most expressed toxin acting on the extracellular matrix, indicating the importance of its inclusion in the antigen’s formulation to provide a better antivenom. Here we show the construction of a hybrid recombinant immunogen, called LgRec1ALP1, composed of hydrophilic regions of the PLD and the ALMP toxins from Loxosceles gaucho. Although the LgRec1ALP1 was expressed as inclusion bodies, it resulted in good yields and it was effective to produce neutralizing antibodies in mice. The antiserum neutralized fibrinogenolytic, platelet aggregation and dermonecrotic activities elicited by L. gaucho, L. laeta, and L. intermedia venoms, indicating that the hybrid recombinant antigen may be a valuable source for the production of protective antibodies against Loxosceles ssp. venoms. In addition, the hybrid recombinant toxin approach may enrich and expand the alternative antigens for antisera production for other venoms. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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15 pages, 2534 KiB  
Article
Mass Spectrometry Analysis and Biological Characterization of the Predatory Ant Odontomachus monticola Venom and Venom Sac Components
by Naoki Tani, Kohei Kazuma, Yukio Ohtsuka, Yasushi Shigeri, Keiichi Masuko, Katsuhiro Konno and Hidetoshi Inagaki
Toxins 2019, 11(1), 50; https://doi.org/10.3390/toxins11010050 - 17 Jan 2019
Cited by 14 | Viewed by 4058
Abstract
We previously identified 92 toxin-like peptides and proteins, including pilosulin-like peptides 1–6 from the predatory ant Odontomachus monticola, by transcriptome analysis. Here, to further characterize venom components, we analyzed the venom and venom sac extract by ESI-MS/MS with or without trypsin digestion [...] Read more.
We previously identified 92 toxin-like peptides and proteins, including pilosulin-like peptides 1–6 from the predatory ant Odontomachus monticola, by transcriptome analysis. Here, to further characterize venom components, we analyzed the venom and venom sac extract by ESI-MS/MS with or without trypsin digestion and reducing agent. As the low-molecular-mass components, we found amino acids (leucine/isoleucine, phenylalanine, and tryptophan) and biogenic amines (histamine and tyramine) in the venom and venom sac extract. As the higher molecular mass components, we found peptides and proteins such as pilosulin-like peptides, phospholipase A2s, hyaluronidase, venom dipeptidyl peptidases, conotoxin-like peptide, and icarapin-like peptide. In addition to pilosulin-like peptides 1–6, we found three novel pilosulin-like peptides that were overlooked by transcriptome analysis. Moreover, pilosulin-like peptides 1–6 were chemically synthesized, and some of them displayed antimicrobial, hemolytic, and histamine-releasing activities. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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Review

Jump to: Editorial, Research

39 pages, 7294 KiB  
Review
Spider Knottin Pharmacology at Voltage-Gated Sodium Channels and Their Potential to Modulate Pain Pathways
by Yashad Dongol, Fernanda C. Cardoso and Richard J. Lewis
Toxins 2019, 11(11), 626; https://doi.org/10.3390/toxins11110626 - 29 Oct 2019
Cited by 26 | Viewed by 6867
Abstract
Voltage-gated sodium channels (NaVs) are a key determinant of neuronal signalling. Neurotoxins from diverse taxa that selectively activate or inhibit NaV channels have helped unravel the role of NaV channels in diseases, including chronic pain. Spider venoms contain the [...] Read more.
Voltage-gated sodium channels (NaVs) are a key determinant of neuronal signalling. Neurotoxins from diverse taxa that selectively activate or inhibit NaV channels have helped unravel the role of NaV channels in diseases, including chronic pain. Spider venoms contain the most diverse array of inhibitor cystine knot (ICK) toxins (knottins). This review provides an overview on how spider knottins modulate NaV channels and describes the structural features and molecular determinants that influence their affinity and subtype selectivity. Genetic and functional evidence support a major involvement of NaV subtypes in various chronic pain conditions. The exquisite inhibitory properties of spider knottins over key NaV subtypes make them the best lead molecules for the development of novel analgesics to treat chronic pain. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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28 pages, 2809 KiB  
Review
Natural Occurrence in Venomous Arthropods of Antimicrobial Peptides Active against Protozoan Parasites
by Elias Ferreira Sabiá Júnior, Luis Felipe Santos Menezes, Israel Flor Silva de Araújo and Elisabeth Ferroni Schwartz
Toxins 2019, 11(10), 563; https://doi.org/10.3390/toxins11100563 - 25 Sep 2019
Cited by 28 | Viewed by 7041
Abstract
Arthropoda is a phylum of invertebrates that has undergone remarkable evolutionary radiation, with a wide range of venomous animals. Arthropod venom is a complex mixture of molecules and a source of new compounds, including antimicrobial peptides (AMPs). Most AMPs affect membrane integrity and [...] Read more.
Arthropoda is a phylum of invertebrates that has undergone remarkable evolutionary radiation, with a wide range of venomous animals. Arthropod venom is a complex mixture of molecules and a source of new compounds, including antimicrobial peptides (AMPs). Most AMPs affect membrane integrity and produce lethal pores in microorganisms, including protozoan pathogens, whereas others act on internal targets or by modulation of the host immune system. Protozoan parasites cause some serious life-threatening diseases among millions of people worldwide, mostly affecting the poorest in developing tropical regions. Humans can be infected with protozoan parasites belonging to the genera Trypanosoma, Leishmania, Plasmodium, and Toxoplasma, responsible for Chagas disease, human African trypanosomiasis, leishmaniasis, malaria, and toxoplasmosis. There is not yet any cure or vaccine for these illnesses, and the current antiprotozoal chemotherapeutic compounds are inefficient and toxic and have been in clinical use for decades, which increases drug resistance. In this review, we will present an overview of AMPs, the diverse modes of action of AMPs on protozoan targets, and the prospection of novel AMPs isolated from venomous arthropods with the potential to become novel clinical agents to treat protozoan-borne diseases. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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18 pages, 1347 KiB  
Review
Chemical and Biological Characteristics of Antimicrobial α-Helical Peptides Found in Solitary Wasp Venoms and Their Interactions with Model Membranes
by Marcia Perez dos Santos Cabrera, Marisa Rangel, João Ruggiero Neto and Katsuhiro Konno
Toxins 2019, 11(10), 559; https://doi.org/10.3390/toxins11100559 - 24 Sep 2019
Cited by 19 | Viewed by 3880
Abstract
Solitary wasps use their stinging venoms for paralyzing insect or spider prey and feeding them to their larvae. We have surveyed bioactive substances in solitary wasp venoms, and found antimicrobial peptides together with some other bioactive peptides. Eumenine mastoparan-AF (EMP-AF) was the first [...] Read more.
Solitary wasps use their stinging venoms for paralyzing insect or spider prey and feeding them to their larvae. We have surveyed bioactive substances in solitary wasp venoms, and found antimicrobial peptides together with some other bioactive peptides. Eumenine mastoparan-AF (EMP-AF) was the first to be found from the venom of the solitary eumenine wasp Anterhynchium flavomarginatum micado, showing antimicrobial, histamine-releasing, and hemolytic activities, and adopting an α-helical secondary structure under appropriate conditions. Further survey of solitary wasp venom components revealed that eumenine wasp venoms contained such antimicrobial α-helical peptides as the major peptide component. This review summarizes the results obtained from the studies of these peptides in solitary wasp venoms and some analogs from the viewpoint of (1) chemical and biological characterization; (2) physicochemical properties and secondary structure; and (3) channel-like pore-forming properties. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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29 pages, 747 KiB  
Review
Potential Therapeutic Applications of Bee Venom on Skin Disease and Its Mechanisms: A Literature Review
by Haejoong Kim, Soo-Yeon Park and Gihyun Lee
Toxins 2019, 11(7), 374; https://doi.org/10.3390/toxins11070374 - 27 Jun 2019
Cited by 38 | Viewed by 18751
Abstract
Skin is larger than any other organ in humans. Like other organs, various bacterial, viral, and inflammatory diseases, as well as cancer, affect the skin. Skin diseases like acne, atopic dermatitis, and psoriasis often reduce the quality of life seriously. Therefore, effective treatment [...] Read more.
Skin is larger than any other organ in humans. Like other organs, various bacterial, viral, and inflammatory diseases, as well as cancer, affect the skin. Skin diseases like acne, atopic dermatitis, and psoriasis often reduce the quality of life seriously. Therefore, effective treatment of skin disorders is important despite them not being life-threatening. Conventional medicines for skin diseases include corticosteroids and antimicrobial drugs, which are effective in treating many inflammatory and infectious skin diseases; however, there are growing concerns about the side effects of these therapies, especially during long-term use in relapsing or intractable diseases. Hence, many researchers are trying to develop alternative treatments, especially from natural sources, to resolve these limitations. Bee venom (BV) is an attractive candidate because many experimental and clinical reports show that BV exhibits anti-inflammatory, anti-apoptotic, anti-fibrotic, antibacterial, antiviral, antifungal, and anticancer effects. Here, we review the therapeutic applications of BV in skin diseases, including acne, alopecia, atopic dermatitis, melanoma, morphea, photoaging, psoriasis, wounds, wrinkles, and vitiligo. Moreover, we explore the therapeutic mechanisms of BV in the treatment of skin diseases and killing effects of BV on skin disease-causing pathogens, including bacteria, fungi and viruses. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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22 pages, 2162 KiB  
Review
Brown Spider (Loxosceles) Venom Toxins as Potential Biotools for the Development of Novel Therapeutics
by Daniele Chaves-Moreira, Fernando Hitomi Matsubara, Zelinda Schemczssen-Graeff, Elidiana De Bona, Vanessa Ribeiro Heidemann, Clara Guerra-Duarte, Luiza Helena Gremski, Carlos Chávez-Olórtegui, Andrea Senff-Ribeiro, Olga Meiri Chaim, Raghuvir Krishnaswamy Arni and Silvio Sanches Veiga
Toxins 2019, 11(6), 355; https://doi.org/10.3390/toxins11060355 - 19 Jun 2019
Cited by 23 | Viewed by 5652
Abstract
Brown spider envenomation results in dermonecrosis with gravitational spreading characterized by a marked inflammatory reaction and with lower prevalence of systemic manifestations such as renal failure and hematological disturbances. Several toxins make up the venom of these species, and they are mainly peptides [...] Read more.
Brown spider envenomation results in dermonecrosis with gravitational spreading characterized by a marked inflammatory reaction and with lower prevalence of systemic manifestations such as renal failure and hematological disturbances. Several toxins make up the venom of these species, and they are mainly peptides and proteins ranging from 5–40 kDa. The venoms have three major families of toxins: phospholipases-D, astacin-like metalloproteases, and the inhibitor cystine knot (ICK) peptides. Serine proteases, serpins, hyaluronidases, venom allergens, and a translationally controlled tumor protein (TCTP) are also present. Toxins hold essential biological properties that enable interactions with a range of distinct molecular targets. Therefore, the application of toxins as research tools and clinical products motivates repurposing their uses of interest. This review aims to discuss possibilities for brown spider venom toxins as putative models for designing molecules likely for therapeutics based on the status quo of brown spider venoms. Herein, we explore new possibilities for the venom components in the context of their biochemical and biological features, likewise their cellular targets, three-dimensional structures, and mechanisms of action. Full article
(This article belongs to the Special Issue Arthropod Venom Components and Their Potential Usage)
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