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3 pages, 242 KiB

Open AccessEditorial

Toxinologic and Pharmacological Investigation of Venomous Arthropods

by Gandhi Rádis-Baptista and Katsuhiro Konno

Toxins 2022, 14(4), 283; https://doi.org/10.3390/toxins14040283 - 15 Apr 2022

Cited by 1 | Viewed by 1906

Abstract

Arthropods comprise the largest group of living animals, including thousands of species that inhabit marine and terrestrial niches in the biosphere [...] Full article

(This article belongs to the Special Issue Toxinologic and Pharmacological Investigation of Venomous Arthropods)

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12 pages, 2661 KiB

Open AccessArticle

Antimicrobial, Insecticidal and Cytotoxic Activity of Linear Venom Peptides from the Pseudoscorpion Chelifer cancroides

by Jonas Krämer, Tim Lüddecke, Michael Marner, Elena Maiworm, Johanna Eichberg, Kornelia Hardes, Till F. Schäberle, Andreas Vilcinskas and Reinhard Predel

Toxins 2022, 14(1), 58; https://doi.org/10.3390/toxins14010058 - 14 Jan 2022

Cited by 14 | Viewed by 3592

Abstract

Linear cationic venom peptides are antimicrobial peptides (AMPs) that exert their effects by damaging cell membranes. These peptides can be highly specific, and for some, a significant therapeutic value was proposed, in particular for treatment of bacterial infections. A prolific source of novel [...] Read more.

Linear cationic venom peptides are antimicrobial peptides (AMPs) that exert their effects by damaging cell membranes. These peptides can be highly specific, and for some, a significant therapeutic value was proposed, in particular for treatment of bacterial infections. A prolific source of novel AMPs are arthropod venoms, especially those of hitherto neglected groups such as pseudoscorpions. In this study, we describe for the first time pharmacological effects of AMPs discovered in pseudoscorpion venom. We examined the antimicrobial, cytotoxic, and insecticidal activity of full-length Checacin1, a major component of the Chelifer cancroides venom, and three truncated forms of this peptide. The antimicrobial tests revealed a potent inhibitory activity of Checacin1 against several bacteria and fungi, including methicillin resistant Staphylococcus aureus (MRSA) and even Gram-negative pathogens. All peptides reduced survival rates of aphids, with Checacin1 and the C-terminally truncated Checacin1¹⁻²¹ exhibiting effects comparable to Spinosad, a commercially used pesticide. Cytotoxic effects on mammalian cells were observed mainly for the full-length Checacin1. All tested peptides might be potential candidates for developing lead structures for aphid pest treatment. However, as these peptides were not yet tested on other insects, aphid specificity has not been proven. The N- and C-terminal fragments of Checacin1 are less potent against aphids but exhibit no cytotoxicity on mammalian cells at the tested concentration of 100 µM. Full article

(This article belongs to the Special Issue Toxinologic and Pharmacological Investigation of Venomous Arthropods)

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22 pages, 3365 KiB

Open AccessArticle

Shedding Lights on Crude Venom from Solitary Foraging Predatory Ant Ectatomma opaciventre: Initial Toxinological Investigation

by Lucas Ian Veloso Correia, Fernanda Van Petten de Vasconcelos Azevedo, Fernanda Gobbi Amorim, Sarah Natalie Cirilo Gimenes, Lorena Polloni, Mariana Alves Pereira Zoia, Mônica Soares Costa, Jéssica Peixoto Rodrigues, Kelly A. Geraldo Yoneyama, Jean Carlos Santos, Eliane Candiani Arantes, Veridiana de Melo Rodrigues, Luiz Ricardo Goulart and Renata Santos Rodrigues

Toxins 2022, 14(1), 37; https://doi.org/10.3390/toxins14010037 - 04 Jan 2022

Cited by 2 | Viewed by 2993

Abstract

Some species of primitive predatory ants, despite living in a colony, exercise their hunting collection strategy individually; their venom is painful, paralyzing, digestive, and lethal for their prey, yet the toxins responsible for these effects are poorly known. Ectatomma opaciventre is a previously [...] Read more.

Some species of primitive predatory ants, despite living in a colony, exercise their hunting collection strategy individually; their venom is painful, paralyzing, digestive, and lethal for their prey, yet the toxins responsible for these effects are poorly known. Ectatomma opaciventre is a previously unrecorded solitary hunting ant from the Brazilian Cerrado. To overcome this hindrance, the present study performed the in vitro enzymatic, biochemical, and biological activities of E. opaciventre to better understand the properties of this venom. Its venom showed several proteins with masses ranging from 1–116 kDa, highlighting the complexity of this venom. Compounds with high enzymatic activity were described, elucidating different enzyme classes present in the venom, with the presence of the first L-amino acid oxidase in Hymenoptera venoms being reported. Its crude venom contributes to a state of blood incoagulability, acting on primary hemostasis, inhibiting collagen-induced platelet aggregation, and operating on the fibrinolysis of loose red clots. Furthermore, the E. opaciventre venom preferentially induced cytotoxic effects on lung cancer cell lines and three different species of Leishmania. These data shed a comprehensive portrait of enzymatic components, biochemical and biological effects in vitro, opening perspectives for bio-pharmacological application of E. opaciventre venom molecules. Full article

(This article belongs to the Special Issue Toxinologic and Pharmacological Investigation of Venomous Arthropods)

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13 pages, 2659 KiB

Open AccessArticle

Effect of Lonomia obliqua Venom on Human Neutrophils

by João Alfredo Moraes, Genilson Rodrigues, Daniel Guimarães-Bastos, Vany Nascimento-Silva, Erik Svensjö, Mariana Renovato-Martins, Markus Berger, Jorge Guimarães and Christina Barja-Fidalgo

Toxins 2021, 13(12), 908; https://doi.org/10.3390/toxins13120908 - 18 Dec 2021

Cited by 1 | Viewed by 2073

Abstract

The significant incidence of deforestation in South America culminates in the contact of humans with typical forests species. Among these species, one may highlight Lonomia obliqua caterpillar, which, when touched by humans, can poison them through their bristles. Therefore, better acknowledging the mechanisms [...] Read more.

The significant incidence of deforestation in South America culminates in the contact of humans with typical forests species. Among these species, one may highlight Lonomia obliqua caterpillar, which, when touched by humans, can poison them through their bristles. Therefore, better acknowledging the mechanisms involved in envenomation caused by Lonomia obliqua caterpillar bristle extract (LOCBE) may contribute to further treatments. Recently, we demonstrated that LOCBE induces a pro-inflammatory profile in endothelial cells; thus, we decided to investigate the effects of LOCBE on human polymorphonuclear neutrophils (PMN), which are the first leukocytes that migrate to the inflammatory focus. Our results showed that treatment with LOCBE induced PMN chemotaxis together with alterations in actin cytoskeleton and focal adhesion kinase (FAK) activation, favoring migration. Concurrently, LOCBE induced PMN adhesion to matrix proteins, such as collagen IV, fibronectin, and fibrinogen. Moreover, we observed that LOCBE attenuated PMN apoptosis and increased reactive oxygen species (ROS) production together with nuclear factor kB (NF-κB) activation—a redox-sensitive transcription factor—as well as interleukin (IL)-1β and IL-8 release. We call attention to the ROS-dependent effect of LOCBE on increased cell migration once an antioxidant treatment reverted it. In summary, we report that LOCBE activates PMN, inducing pro-inflammatory responses modulated by ROS. Full article

(This article belongs to the Special Issue Toxinologic and Pharmacological Investigation of Venomous Arthropods)

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20 pages, 2039 KiB

Open AccessEditor’s ChoiceArticle

Comprehensive Analysis and Biological Characterization of Venom Components from Solitary Scoliid Wasp Campsomeriella annulata annulata

by Carlos Alberto-Silva, Fernanda Calheta Vieira Portaro, Roberto Tadashi Kodama, Halyne Queiroz Pantaleão, Hidetoshi Inagaki, Ken-ichi Nihei and Katsuhiro Konno

Toxins 2021, 13(12), 885; https://doi.org/10.3390/toxins13120885 - 10 Dec 2021

Cited by 5 | Viewed by 2383

Abstract

Venoms of solitary wasps are utilized for prey capture (insects and spiders), paralyzing them with a stinger injection to be offered as food for their larvae. Thus, the identification and characterization of the components of solitary wasp venoms can have biotechnological application. In [...] Read more.

Venoms of solitary wasps are utilized for prey capture (insects and spiders), paralyzing them with a stinger injection to be offered as food for their larvae. Thus, the identification and characterization of the components of solitary wasp venoms can have biotechnological application. In the present study, the venom components profile of a solitary scoliid wasp, Campsomeriella annulata annulata, was investigated through a comprehensive analysis using LC-MS and -MS/MS. Online mass fingerprinting revealed that the venom extract contains 138 components, and MS/MS analysis identified 44 complete sequences of the peptide components. The peptides are broadly divided into two classes: bradykinin-related peptides, and linear α-helical peptides. Among the components of the first class, the two main peptides, α-campsomerin (PRLRRLTGLSPLR) and β-campsomerin (PRLRRLTGLSPLRAP), had their biological activities evaluated. Both peptides had no effects on metallopeptidases [human neprilysin (NEP) and angiotensin-converting enzyme (ACE)] and acetylcholinesterase (AChE), and had no cytotoxic effects. Studies with PC12 neuronal cells showed that only α-campsomerin was able to enhance cell viability, while β-campsomerin had no effect. It is noteworthy that the only difference between the primary structures from these peptides is the presence of the AP extension at the C-terminus of β-campsomerin, compared to α-campsomerin. Among the linear α-helical peptides, annulatin (ISEALKSIIVG-NH₂) was evaluated for its biological activities. Annulatin showed histamine releasing activity from mast cells and low hemolytic activity, but no antimicrobial activities against all microbes tested were observed. Thus, in addition to providing unprecedented information on the whole components, the three peptides selected for the study suggest that molecules present in solitary scoliid wasp venoms may have interesting biological activities. Full article

(This article belongs to the Special Issue Toxinologic and Pharmacological Investigation of Venomous Arthropods)

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13 pages, 2751 KiB

Open AccessEditor’s ChoiceArticle

Stability and Safety of Inhibitor Cystine Knot Peptide, GTx1-15, from the Tarantula Spider Grammostola rosea

by Tadashi Kimura

Toxins 2021, 13(9), 621; https://doi.org/10.3390/toxins13090621 - 03 Sep 2021

Cited by 5 | Viewed by 2882

Abstract

Inhibitor cystine knot (ICK) peptides are knotted peptides with three intramolecular disulfide bonds that affect several types of ion channels. Some are proteolytically stable and are promising scaffolds for drug development. GTx1-15 is an ICK peptide that inhibits the voltage-dependent calcium channel Ca [...] Read more.

Inhibitor cystine knot (ICK) peptides are knotted peptides with three intramolecular disulfide bonds that affect several types of ion channels. Some are proteolytically stable and are promising scaffolds for drug development. GTx1-15 is an ICK peptide that inhibits the voltage-dependent calcium channel Ca_v3.1 and the voltage-dependent sodium channels Na_v1.3 and Na_v1.7. As a model molecule to develop an ICK peptide drug, we investigated several important pharmaceutical characteristics of GTx1-15. The stability of GTx1-15 in rat and human blood plasma was examined, and no GTx1-15 degradation was observed in either rat or human blood plasma for 24 h in vitro. GTx1-15 in blood circulation was detected for several hours after intravenous and intramuscular administration, indicating high stability in plasma. The thermal stability of GTx1-15 as examined by high thermal incubation and protein thermal shift assays indicated that GTx1-15 possesses high heat stability. The cytotoxicity and immunogenicity of GTx1-15 were examined using the human monocytic leukemia cell line THP-1. GTx1-15 showed no cytotoxicity or immunogenicity even at high concentrations. These results indicate that GTx1-15 itself is suitable for peptide drug development and as a peptide library scaffold. Full article

(This article belongs to the Special Issue Toxinologic and Pharmacological Investigation of Venomous Arthropods)

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13 pages, 644 KiB

Open AccessArticle

Antiparasitic Effects of Potentially Toxic Beetles (Tenebrionidae and Meloidae) from Steppe Zones

by Marta Díaz-Navarro, Paula Bolívar, María Fe Andrés, María Teresa Gómez-Muñoz, Rafael A. Martínez-Díaz, Félix Valcárcel, Mario García-París, Luis M. Bautista and Azucena González-Coloma

Toxins 2021, 13(7), 489; https://doi.org/10.3390/toxins13070489 - 14 Jul 2021

Cited by 3 | Viewed by 3101

Abstract

Arthropods and specifically beetles can synthesize and/or sequester metabolites from dietary sources. In beetle families such as Tenebrionidae and Meloidae, a few studies have reported species with toxic defensive substances and antiparasitic properties that are consumed by birds. Here we have studied the [...] Read more.

Arthropods and specifically beetles can synthesize and/or sequester metabolites from dietary sources. In beetle families such as Tenebrionidae and Meloidae, a few studies have reported species with toxic defensive substances and antiparasitic properties that are consumed by birds. Here we have studied the antiparasitic activity of extracts from beetle species present in the habitat of the Great Bustard (Otis tarda) against four pathogen models (Aspergillus niger, Meloidogyne javanica, Hyalomma lusitanicum, and Trichomonas gallinae). The insect species extracted were Tentyria peiroleri, Scaurus uncinus, Blaps lethifera (Tenebrionidae), and Mylabris quadripunctata (Meloidae). M. quadripunctata exhibited potent activity against M. javanica and T. gallinae, while T. peiroleri exhibited moderate antiprotozoal activity. The chemical composition of the insect extracts was studied by gas chromatography coupled with mass spectrometry (GC-MS) analysis. The most abundant compounds in the four beetle extracts were hydrocarbons and fatty acids such as palmitic acid, myristic acid and methyl linoleate, which are characteristic of insect cuticles. The presence of cantharidin (CTD) in the M. quadripunctata meloid and ethyl oleate (EO) in T. peiroleri accounted for the bioactivity of their extracts. Full article

(This article belongs to the Special Issue Toxinologic and Pharmacological Investigation of Venomous Arthropods)

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16 pages, 2264 KiB

Open AccessEditor’s ChoiceArticle

Sphingomyelinase D Activity in Sicarius tropicus Venom: Toxic Potential and Clues to the Evolution of SMases D in the Sicariidae Family

by Priscila Hess Lopes, Caroline Sayuri Fukushima, Rosana Shoji, Rogério Bertani and Denise V. Tambourgi

Toxins 2021, 13(4), 256; https://doi.org/10.3390/toxins13040256 - 01 Apr 2021

Cited by 3 | Viewed by 3434

Abstract

The spider family Sicariidae includes three genera, Hexophthalma, Sicarius and Loxosceles. The three genera share a common characteristic in their venoms: the presence of Sphingomyelinases D (SMase D). SMases D are considered the toxins that cause the main pathological effects of [...] Read more.

The spider family Sicariidae includes three genera, Hexophthalma, Sicarius and Loxosceles. The three genera share a common characteristic in their venoms: the presence of Sphingomyelinases D (SMase D). SMases D are considered the toxins that cause the main pathological effects of the Loxosceles venom, that is, those responsible for the development of loxoscelism. Some studies have shown that Sicarius spiders have less or undetectable SMase D activity in their venoms, when compared to Hexophthalma. In contrast, our group has shown that Sicarius ornatus, a Brazilian species, has active SMase D and toxic potential to envenomation. However, few species of Sicarius have been characterized for their toxic potential. In order to contribute to a better understanding about the toxicity of Sicarius venoms, the aim of this study was to characterize the toxic properties of male and female venoms from Sicarius tropicus and compare them with that from Loxosceles laeta, one of the most toxic Loxosceles venoms. We show here that S. tropicus venom presents active SMases D. However, regarding hemolysis development, it seems that these toxins in this species present different molecular mechanisms of action than that described for Loxosceles venoms, whereas it is similar to those present in bacteria containing SMase D. Besides, our results also suggest that, in addition to the interspecific differences, intraspecific variations in the venoms’ composition may play a role in the toxic potential of venoms from Sicarius species. Full article

(This article belongs to the Special Issue Toxinologic and Pharmacological Investigation of Venomous Arthropods)

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