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At least 649 records · Page 36Linked to original sources
PubMed2005

The influence of methyl jasmonate (JA-Me) and B-glucosidase on induction of resistance mechanisms of strawberry against two-spotted spider mite (Tetranychus urticae Koch.).

The goal of the research was to study the influence of methyl jasmonate (JA-Me) and beta-glucosidase treatments on fecundity and preference to infestation and oviposition of two-spotted spider mite feeding on strawberry. The experiments were conducted in laboratory conditions on leaves of Aga and Kent cultivars. Leaves were treated with: a. solution of 0.1% JA-Me in 0.05% Triton X-100 (by spraying); b. beta-glucosidase dissolved in 0.1 M citrate buffer at pH 6 (by petiole); c. 0.05% solution of the Triton X-100 (by spraying); d. 0.1 M citrate buffer at pH 6 (by petiole). In the no-choice test, application of JA-Me on leaves of strawberry caused reducing of number of eggs laid during three days of the experiment. In the choice test, which was carried out for determination of non-preference mechanism of resistance, there was a statistically significant lower number of mites on leaves treated with JA-Me compared to leaves treated with other compounds as well as to non-treated leaves after 24 hours from solutions application. Moreover, at the same experiment, females of two-spotted spider mite laid the least number of eggs on leaves treated with JA-Me. Analysis conducted using liquid chromatography method, revealed increase of the level of phenolic compounds like chlorogenic acid and rutin on leaves treated with JA-Me. Thus, it appears that JA-Me may be involved in antybiosis or non-preference mechanisms of resistance of strawberry to two-spotted spider mite.

Acetates↗
PubMed1997

Detection of new spider toxins from a Nephilengys borbonica venom gland using on-line mu-column HPLC continuous flow (FRIT) FAB LC/MS and MS/MS.

Spider venom glands store various novel neurotoxic acylpolyamines which present potent and irreversible inhibition of the glutamatergic synapses. We have developed a new highly sensitive analytical method to detect and characterize structures of those neurotoxins stored in a single venom gland using micro bore column high performance liquid chromatography (HPLC)-continuous flow FRIT fast atom bombardment mass spectrometry (HPLC-FAB/MS) and tandem mass spectrometry (MS/MS) array detection system. The high-energy collision induced dissociation (CID) spectra of sodium cationized spider toxins produced very strong structurally informative product ions which afforded the location of nitrogen atoms and the connectivity of methylene units within the polyamines. This methodology permitted detection of 40 amino acid containing acylpolyamines in the venom of Nephilengys borbonica from which structures of only five compounds were previously known.

Animals↗
PubMed1998

Novel insecticidal peptides from Tegenaria agrestis spider venom may have a direct effect on the insect central nervous system.

Fractionation of venom from an agelenid spider, Tegenaria agrestis, resulted in the isolation of a family of three peptides with potent insecticidal activity. These peptide toxins, TaITX-1, -2, and -3, whose sequences were revealed from cloned cDNAs, each consist of 50 amino acid residues, six of which are cysteines. They appear to be amidated at their C-termini and exhibit greater than 90% sequence identity. Unlike other reported spider toxins, the TaI toxins are processed from precursors containing no propeptide sequences. In lepidopteran larvae and corn rootworm beetles, the insecticidal Tegenaria toxins caused an unusual excitatory symptomatology with 50% paralytic doses ranging from 0.23 to 2.6 nmol/g. In a series of electrophysiological experiments performed in house fly larvae, these toxins caused an elevated rate of firing from central nervous system neurons. No significant effects were found when any peripheral sensory or motor systems were examined. Thus, it appears that the TaI toxins may act in a fashion not previously reported for insecticidal peptide toxins; they may act directly on the insect central nervous system.

Amino Acid Sequence↗
PubMed2025

Gene and Genome Duplication in Spiders.

Gene and genome duplications are widely observed across various organisms, including plants, yeasts, and animals. Numerous studies link gene duplications to the emergence of novel phenotypes, supporting the hypothesis that duplication events are advantageous for adaptive evolution. Whole-genome duplications (WGD) are especially prevalent in plants and have also occurred ancestrally in vertebrates. However, large-scale duplication events in other animal groups remain understudied, partly due to limited genomic resources. Arthropods, particularly insects, represent one of the most diverse animal clades in terms of both species and phenotypic diversity. With increasing availability of chromosome-level genomes, large-scale duplications appear to be rare in insects but are more frequent in chelicerates (e.g. spiders, scorpions, and horseshoe crabs). This makes chelicerates an intriguing group for comparing the mechanisms, fates, and evolutionary impacts of large-scale duplications with those seen in plants and vertebrates. In this review, we synthesize and discuss current research on WGD in spiders and discuss different scenarios for genes following gene duplication events (conservation, nonfunctionalization, subfunctionalization, specialization, drift, neofunctionalization) in the context of experimental studies. We hypothesize if there might be common trajectories after duplication and how these could be tested.

Animals↗
PubMed2006

Spider venom toxin protects plants from insect attack.

Many of the toxin proteins, that have been heterogeneously expressed in agricultural crops to provide resistance to insect pests, are too specific or are only mildly effective against the major insect pests. Spider venoms are a complex cocktail of toxins that have evolved specifically to kill insects. Here we show that the omega-ACTX-Hv1a toxin (Hvt), a component of the venom of the Australian funnel web spider (Hadronyche versuta) that is a calcium channel antagonist, retains its biological activity when expressed in a heterologous system. Expressed as a fusion protein in E. coli, the purified toxin fusion immobilized and killed Helicoverpa armigera and Spodoptera littoralis caterpillars when applied topically. Transgenic expression of Hvt in tobacco effectively protected the plants from H. armigera and S. littoralis larvae, with 100% mortality within 48 h. We conclude that the Hvt is an attractive and effective molecule for the transgenic protection of plants from herbivorous insects which should be evaluated further for possible application in agriculture.

Agatoxins↗
PubMed1993

Properties and amino acid sequence of huwentoxin-I, a neurotoxin purified from the venom of the Chinese bird spider Selenocosmia huwena.

By means of reverse phase and ion-exchange high performance liquid chromatography, a neurotoxic peptide named huwentoxin-I was purified from the venom of the Chinese bird spider Selenocosmia huwena. The intraperitoneal and intracisternal LD50 in mice of the toxin were 0.70 mg/kg and 9.40 micrograms/kg, respectively. This toxin at the concentration of 1 x 10(-5) g/ml can irreversibly block the neuromuscular transmission of the isolated mouse phrenic nerve-diaphragm preparation in 13.4 +/- 1.3 min (mean +/- S.D., n = 5). The isoelectric point is 8.95 determined by isoelectric focusing electrophoresis. It consists of 33 amino acids including 6 Cys and 6 Lys determined by amino acid analysis. The complete amino sequence of huwentoxin-I was determined. The N-terminal and C-terminal residues were Ala and Leu, respectively. The primary structure showed partial homology with that of mu-agatoxins from the funnel-web spider Agelenopsis aperta.

Amino Acid Sequence↗
PubMed1987

Joro spider venom: glutamate agonist and antagonist on the rod retina of the dogfish.

The venom of the Joro spider, reported to block glutamate action selectively at some glutaminergic synapses, was applied focally to rod horizontal and on-bipolar cells in dark-adapted retinal slices. The venom hyperpolarized horizontal cells in the dark and blocked their responses to light. Depolarization of horizontal cells by ionophoretic pulses of L-glutamate, L-aspartate or kainate was antagonized by the toxin in a slowly reversible manner. These results are consistent with other evidence for glutamate as the rod neurotransmitter acting on a single postsynaptic receptor type on horizontal cells. In contrast, the venom, like glutamate, closed the same ion channels of on-bipolar cells as the transmitter, thereby blocking light responses of on-bipolars. Joro spider toxin distinguishes the glutamate receptor-channel complexes of rod horizontal and on-bipolar cells.

Animals↗
PubMed2006

Molecular cloning and functional characterization of two isoforms of dermonecrotic toxin from Loxosceles intermedia (brown spider) venom gland.

Brown spider (Genus Loxosceles) bites are normally associated with necrotic skin degeneration, gravitational spreading, massive inflammatory response at injured region, platelet aggregation causing thrombocytopenia and renal disturbances. Brown spider venom has a complex composition containing many different toxins, of which a well-studied component is the dermonecrotic toxin. This toxin alone may produce necrotic lesions, inflammatory response and platelet aggregation. Biochemically, dermonecrotic toxin belongs to a family of toxins with 30-35 kDa characterized as sphingomyelinase-D. Here, employing a cDNA library of Loxosceles intermedia venom gland, we cloned and expressed two recombinant isoforms of the dermonecrotic toxin LiRecDT2 (1062 bp cDNA) and LiRecDT3 (1007 bp cDNA) that encode for signal peptides and complete mature proteins. Phylogenetic tree analysis revealed a structural relationship for these toxins compared to other members of family. Recombinant molecules were expressed as N-terminal His-tag fusion proteins in Escherichia coli and were purified to homogeneity from cell lysates by Ni(2+) chelating chromatography, resulting in proteins of 33.8 kDa for LiRecDT2 and 34.0 kDa for LiRecDT3. Additional evidence for related toxins containing sequence/epitopes identity comes from antigenic cross-reactivity using antibodies against crude venom toxins and antibodies raised with a purified dermonecrotic toxin. Recombinant toxins showed differential functionality in rabbits: LiRecDT2 caused a macroscopic lesion with gravitational spreading upon intradermal injection, while LiRecDT3 evoked transient swelling and erythema upon injection site. Light microscopic analysis of skin biopsies revealed edema, a collection of inflammatory cells in and around blood vessels and a proteinaceous network at the dermis. Moreover, differential functionality for recombinant toxins was also demonstrated by a high sphingomyelinase activity for LiRecDT2 and low activity for LiRecDT3 as well as greater in vitro platelet aggregation and blood vessel permeability induced by LiRecDT2 and residual activity for LiRecDT3. Cloning and expression of two recombinant dermonecrotic toxins demonstrate an intraspecific family of homologous toxins that act in synergism for deleterious activities of the venom and open possibilities for biotechnological applications for recombinant toxins as research tools for understanding the inflammatory response, vascular integrity and platelet aggregation modulators.

Amino Acid Sequence↗
PubMed2026

Divergent evolutionary strategies in spider venoms: A comparative proteomic profiling of four sympatric species from Yunnan.

Spider venoms comprise complex cocktails of bioactive molecules evolved for predation and defense, representing a valuable resource for biological research and pharmaceutical discovery. In this study, we performed a systematic analysis of venom gland extracts from four common spider species indigenous to Yunnan, China: Agelena limbata, Hippasa lycosina, Lycosa grahami, and Sinopoda pengi. Using an integrated transcriptomic and proteomic targeted profiling approach, we successfully annotated 141 distinct toxins. Comparative analysis revealed significant interspecific heterogeneity, suggesting distinct evolutionary trajectories and "weapon system economics." Both A. limbata and L. grahami exhibited a "peptide-dominant" profile anchored by neurotoxic peptides and isomerases, optimized for rapid chemical paralysis. In contrast, S. pengi displayed a distinct "protein-dominant" signature enriched with high-molecular-weight enzymes and CAP superfamily proteins, likely functioning to facilitate tissue degradation and toxin diffusion. Occupying an intermediate position, H. lycosina demonstrated a hybrid composition. These findings suggest that although these species share the same geographical range, their venom systems have undergone divergent evolutionary adaptations driven by specific ecological niches and hunting strategies. This study represents the first systematic proteomic characterization of these venom components, providing a valuable reservoir of molecular candidates while highlighting the bioinformatic nuances of analyzing whole-gland homogenates.

Animals↗
PubMed2004

Tandem mass spectrometric investigation of acylpolyamines of spider venoms and their 15N-labeled derivatives.

The fragmentation mechanism of the acylpentamine toxins 1-4 found in the venom of the spider Agelenopsis aperta has been investigated in detail. To identify the origin of the two doublets of unexpected fragment ions at m/z 129/112 and m/z 115/98, three synthetic 15N-labeled analogs 5-7 have been prepared and subjected to CID fragmentation on a triple quadrupole mass spectrometer. It appears that the unexpected doublet of fragment ions arises from an internal portion of the polyamine backbone after either a transaminative Zip reaction or a sequential fragmentation of the quasi-molecular ion. The second option has been proven by in-source CID experiments. The detailed knowledge of acylpentamine fragmentation mechanisms is essential for the correct characterization of isomeric compounds, particularly for coeluting compounds within complex mixtures such as spider venoms.

Animals↗
PubMed2004

Fusion proteins containing insect-specific toxins as pest control agents: snowdrop lectin delivers fused insecticidal spider venom toxin to insect haemolymph following oral ingestion.

The mannose-specific snowdrop lectin (Galanthus nivalis agglutinin: GNA), when fed to insects, binds to the gut epithelium and passes into the haemolymph. The ability of GNA to act as a carrier protein to deliver an insecticidal spider venom neurotoxin (Segestria florentina toxin 1: SFI1) to the haemolymph of lepidopteran larvae was investigated. Constructs encoding SFI1 and an SFI1/GNA fusion protein were expressed in Pichia pastoris. The insecticidal activity of purified recombinant proteins on injection was found to be comparable to published values for SfI1 purified from spider venom [Toxicon 40 (2002) 125]. Whereas neither GNA nor SFI1 alone showed acute toxicity when fed to larvae of tomato moth (Lacanobia oleracea), feeding SFI1/GNA fusion at 2.5% of dietary proteins was insecticidal to first stadium larvae, causing 100% mortality after 6 days. The protein also showed a significant, dose dependent, toxicity towards fourth and fifth stadium larvae, with growth reduced by up to approximately 90% over a 4-day assay period compared to controls. Delivery of intact SFI1/GNA to the haemolymph in these insects was shown by western blotting; haemolymph samples from fusion-fed larvae contained a GNA-immunoreactive protein of the same molecular weight as the SFI1/GNA fusion. SFI1/GNA and similar fusion proteins offer a novel and effective approach for delivering haemolymph active toxins by oral administration, which could be used in crop protection by expression in transgenic plants.

Animals↗
PubMed2005

Discovery of an MIT-like atracotoxin family: spider venom peptides that share sequence homology but not pharmacological properties with AVIT family proteins.

This project identified a novel family of six 66-68 residue peptides from the venom of two Australian funnel-web spiders, Hadronyche sp. 20 and H. infensa: Orchid Beach (Hexathelidae: Atracinae), that appear to undergo N- and/or C-terminal post-translational modifications and conform to an ancestral protein fold. These peptides all show significant amino acid sequence homology to atracotoxin-Hvf17 (ACTX-Hvf17), a non-toxic peptide isolated from the venom of H. versuta, and a variety of AVIT family proteins including mamba intestinal toxin 1 (MIT1) and its mammalian and piscine orthologs prokineticin 1 (PK1) and prokineticin 2 (PK2). These AVIT family proteins target prokineticin receptors involved in the sensitization of nociceptors and gastrointestinal smooth muscle activation. Given their sequence homology to MIT1, we have named these spider venom peptides the MIT-like atracotoxin (ACTX) family. Using isolated rat stomach fundus or guinea-pig ileum organ bath preparations we have shown that the prototypical ACTX-Hvf17, at concentrations up to 1muM, did not stimulate smooth muscle contractility, nor did it inhibit contractions induced by human PK1 (hPK1). The peptide also lacked activity on other isolated smooth muscle preparations including rat aorta. Furthermore, a FLIPR Ca2+ flux assay using HEK293 cells expressing prokineticin receptors showed that ACTX-Hvf17 fails to activate or block hPK1 or hPK2 receptors. Therefore, while the MIT-like ACTX family appears to adopt the ancestral disulfide-directed beta-hairpin protein fold of MIT1, a motif believed to be shared by other AVIT family peptides, variations in the amino acid sequence and surface charge result in a loss of activity on prokineticin receptors.

Amino Acid Sequence↗
PubMed2004

Australian funnel-web spiders: master insecticide chemists.

Arthropods are the most diverse animal group on the planet. Their ability to inhabit a vast array of ecological niches has inevitably brought them into conflict with humans. Although only a small minority are classified as pest species, they nevertheless destroy about a quarter of the world's annual crop production and transmit an impressive array of pathogens of human and veterinary public health importance. Arthropod pests have been controlled almost exclusively with chemical insecticides since the introduction of DDT in the 1940s. However, the evolution of resistance to many insecticides, coupled with increased awareness of the potential environmental and human and animal health impacts of these chemicals, has stimulated the search for new insecticidal compounds, novel molecular targets, and alternative control methods. Spider venoms are complex chemical cocktails that have evolved to kill or paralyze arthropod prey, and they represent a largely untapped reservoir of insecticidal compounds. This review focuses on several families of invertebrate-specific peptide neurotoxins that were isolated from the venom of Australian funnel-web spiders. These peptides are promising insecticide leads because of their selectivity for invertebrates and activity on previously unvalidated targets. These toxins should facilitate the development of novel target-based screens for new insecticide leads, while their mapped pharmacophores will provide templates for rational design of mimetics that act at these target sites. Furthermore, genes encoding these toxins can be used to improve the efficacy of insect-specific viruses.

Amino Acid Sequence↗
PubMed2004

Ontogenetic changes in Phoneutria nigriventer (Araneae, Ctenidae) spider venom.

Venom-yield and composition of differently sized individuals of the medically most important Brazilian spider Phoneutria nigriventer (Keyserling, 1891) was analysed. During growth the venom-mass increases according to a fourth order function of the prosoma size, which mainly reflects an increase of the venom gland volume. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed increasing percentages of proteins < or = 17 kDa from 4.1% in the smallest analysed spiders (2-3 months-old) to 79.1% in adult female venom. Additionally, high-pressure liquid-chromatography showed an increase of a single ('main') peak from 4.6 to 64.9%, while the overall number of other major-peaks decreased. Venom from young instars completely lacked lethality in mice up to a dose of 3.28 mg/kg i.v. as compared to a LD(50) of 0.63 mg/kg for adult female or 1.57 mg/kg for adult male venom that we reported previously. In conclusion, ontogenetic changes in venom protein-composition of growing P. nigriventer are suggested to produce increasing lethality in vertebrates.

Age Factors↗
PubMed2006

Venom landscapes: mining the complexity of spider venoms via a combined cDNA and mass spectrometric approach.

The complexity of Australian funnel-web spider venoms has been explored via the combined use of MALDI-TOF mass spectrometry coupled with chromatographic separation and the analysis of venom-gland cDNA libraries. The results show that these venoms are far more complex than previously realized. We show that the venoms of Australian funnel-web spiders contain many hundreds of peptides that follow a bimodal distribution, with about 75% of the peptides having a mass of 3000-5000 Da. The mass spectral data were validated by matching the experimentally observed masses with those predicted from peptide sequences derived from analysis of venom-gland cDNA libraries. We show that multiple isoforms of these peptides are found in small chromatographic windows, which suggests that the wide distribution of close molecular weights among the chromatographic fractions probably reflects a diversity of structures and physicochemical properties. The combination of all predicted and measured parameters permits the interpretation of three-dimensional 'venom landscapes' derived from LC-MALDI analysis. We propose that these venom landscapes might have predictive value for the discovery of various groups of pharmacologically distinct toxins in complex venoms.

Amino Acid Sequence↗
PubMed2006

The effect of brown spider venom on endothelial cell morphology and adhesive structures.

Spiders of the Loxosceles genus have been responsible for severe clinical cases of envenomation worldwide. Accidents involving brown spiders can cause dermonecrotic injury, hemorrhage, hemolysis, platelet aggregation and renal failure. Histological findings of animals treated by venom have shown subendothelial blebs, vacuoles and endothelial cell membrane degeneration of blood vessel walls, as well as fibrin and thrombus formation. The mechanisms by which the venom causes these disorders are poorly understood. In this work, with an endothelial cell line derived from rabbit aorta, we were able to demonstrate that venom binds to the cell surface and the extracellular matrix. Moreover, we observed that the venom also induced morphological alterations, such as cell retraction, homophilic disadhesion and an increasing in filopodia projections. We also demonstrated that toxins present in the venom disorganized focal adhesion points and actin microfilaments of endothelial cells. Nevertheless, endothelial cell viability showed no alterations compared to controls. Additionally, venom treatment changed the fibronectin matrix profile synthesized by these cells as well as cell adhesion to fibronectin. These results suggest that the deleterious effects of venom on blood vessel walls could be a consequence of the direct effect on the endothelial cell surface and adhesive structures involved in blood vessel stability. These effects indirectly lead to leukocyte and platelet activation, disseminated intravascular coagulation and an increase in vessel permeability.

Animals↗
PubMed2006

Acid and alkaline phosphatase activities of a fraction isolated from Parawixia bistriata spider venom.

This present study describes the isolation of a high molecular weight fraction (F1) from the venom of the social spider Parawixia bistriata, by gel filtration and also its subfractions by further purification with affinity chromatography on a Concanavalin A-Sepharose column. Acid and an alkaline phosphatase activities were found in fractions. The effects of pH, temperature and metallic ions on these activities were evaluated. Optimal temperature for both enzymes was 55 degrees C and optimal pH was 5.0 and 8.5 for the acid and alkaline phosphatase activities, respectively. As ZnCl(2) inhibited enzymatic activities and the chelating agent ethylenediaminetetracetic acid (EDTA) raised the basal phosphatase activities, it was speculated that the venom itself could contain Zn(+ +); this was confirmed with the use of an atomic absorption flame spectrometer. In conclusion, the high molecular weight components of the spider venom of P. bistriata have acid and alkaline phosphatase activities, which may reflect the presence of at least two different enzymes.

Acid Phosphatase↗
PubMed2006

Hyaluronidases in Loxosceles intermedia (Brown spider) venom are endo-beta-N-acetyl-d-hexosaminidases hydrolases.

In studying Loxosceles venom, we detected degradation of purified hyaluronic acid (HA) and hydrolysis of purified chondroitin sulphate (CS) while neither dermatan sulphate, heparin or heparan sulphate were affected. In addition, with HA-degrading kinetic assays, we show that a hydrolase enzyme was involved in the HA cleavage. By use of the Reissig colorimetric reaction, we found that venom hyaluronidase is an endo-beta-N-acetyl-d-hexosaminidase that generates terminal N-acetylglucosamine residues upon cleavage of HA. Zymogram analysis of L. intermedia venom showed HA lytic activities at 41 and 43kDa, and, when CS was used as a substrate, zymograph experiments resulted in 41 and 43kDa lytic zones. Thus, these results support the hypothesis that the same molecules are involved in cleaving HA and CS residues. Experiments to compare L. intermedia electrostimulated venom and venom gland extract also demonstrated very similar HA lytic activity, suggesting again that hyaluronidases are self-components of Loxosceles spider venom instead of oral egesta contamination. HA degradation as a function of pH in these hydrolase enzymes showed no apparent activities at low or high pH, with optimal activity at 6.0-8.0 pH. Finally, we confirmed the cleaving action of the venom hyaluronidases on HA in the extracellular matrix of the dermis of rabbit by fluorescence reaction to HA and confocal microscope analysis. Thus, hyaluronidases type hydrolases endo-beta-N-acetyl-d-hexosaminidase are implicated as self-components of Loxosceles spider venom and can be involved in venom effects as spreading factors.

Animals↗