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At least 19 recordsLinked to original sources
PubMed2002

Pharmacology and biochemistry of spider venoms.

Spider venoms represent an incredible source of biologically active substances which selectively target a variety of vital physiological functions in both insects and mammals. Many toxins isolated from spider venoms have been invaluable in helping to determine the role and diversity of neuronal ion channels and the process of exocytosis. In addition, there is enormous potential for the use of insect specific toxins from animal sources in agriculture. For these reasons, the past 15-20 years has seen a dramatic increase in studies on the venoms of many animals, particularly scorpions and spiders. This review covers the pharmacological and biochemical activities of spider venoms and the nature of the active components. In particular, it focuses on the wide variety of ion channel toxins, novel non-neurotoxic peptide toxins, enzymes and low molecular weight compounds that have been isolated. It also discusses the intraspecific sex differences in given species of spiders.

Amino Acids↗
PubMed1999

Polypeptide neurotoxins from spider venoms.

Spider venoms contain a variety of toxic components. The polypeptide toxins are divided into low and high molecular mass types. Small polypeptide toxins interacting with cation channels display spatial structure homology. They can affect the functioning of calcium, sodium, or potassium channels. A family of high molecular mass toxic proteins was found in the venom of the spider genus Latrodectus. These neurotoxins, latrotoxins, cause a massive transmitter release from a diversity of nerve endings. The latrotoxins are proteins of about 1000 amino acid residues and share a high level of structure identity. The structural and functional properties of spider polypeptide toxins are reviewed in this paper.

Amino Acid Sequence↗
PubMed2004

The wonderful world of spiders: preface to the special Toxicon issue on spider venoms.

Spiders are remarkable for their complete reliance on predation as a trophic strategy. Their evolutionary success is due in large part to production of a complex venom that is designed to rapidly subdue or kill their prey. This issue provides an overview of the fascinating complexity of these venoms, a realistic account of the danger they pose to humans, and an examination of their immense but largely untapped potential for drug and insecticide discovery.

Animals↗
PubMedDate not supplied

Structure and pharmacology of spider venom neurotoxins.

Spider venoms are complex mixtures of neurotoxic peptides, proteins and low molecular mass organic molecules. Their neurotoxic activity is due to the interaction of the venom components with cellular receptors, in particular ion channels. Spider venoms have proven to be a rich source of highly specific peptide ligands for selected subtypes of potassium, sodium and calcium channels, and these toxins have been used to elucidate the structure and physiological roles of the channels in excitable and non-excitable cells. Spider peptides show great variability in their pharmacological activity and primary structure but relative homogeneity in their secondary structure. Following diverse molecular evolution mechanisms, and in particular selective hypermutation, short spider peptides appear to have functionally diversified while retaining a conserved molecular scaffold. This paper reviews the composition and pharmacology of spider venoms with emphasis on polypeptide toxin structure, mode of action and molecular evolution.

Amino Acid Sequence↗
PubMed2004

A anticonvulsive fraction from Scaptocosa raptoria (Araneae: Lycosidae) spider venom.

Several spider neurotoxins are known to show highly selective effects on nervous tissues. Intracerebral injection into rats of spider venom from Scaptocosa raptoria, prevents seizures induced by convulsant agents. Injection of phenytoin (390 pmol/200 nl), muscimol (90 pmol/200 nl), baclofen (500 pmol/200 nl) into the substantia nigra (SN) pars reticulata, protected rats from convulsions evoked by unilateral focal injection of bicuculline into the area tempestas by 50, 80, and 100%, respectively. Denatured S. raptoria crude venom (4.6 microg, 2.3 microg, and 920 ng/200 nl), when administered into the SN, prevented seizures elicited by bicuculline in the area tempestas by 100, 100, and 87.5%, respectively. The injection into the SN of 160 ng/200 nl of fraction SrTx1 isolated from S. raptoria venom, reduced the magnitude of seizures. This fraction was rechromatographed affording fractions SrTx1.1, SrTx1.2 and SrTx1.3, and they were administered into the SN at doses of 100, 200, and 400 ng/200 nl respectively. Fraction SrTx1.3 protected 50, 85.7, and 100% of the animals against the seizures elicited by bicuculline injected into the area tempestas. This suggests that S. raptoria venom as well as its SrTx1.3 fraction, might be potential sources of new anticonvulsant drugs.

Animals↗
PubMed1985

[Venomous spiders and their venoms].

The history of araneidism is long and confusing. The superstition seems to be inexterminatable that tropical mygalomorphs and mediterranean tarantulas are dangerous for humans. It can be looked up even in the most recent edition of the widespread clinical dictionary of Pschyrembel. In contrast to this certain ctenids, the most dangerous spiders up to now known, are mentioned not at all in medical publications. Exaggerated spider-fear is out of place because about 0.1% of all species are dangerous for man only and many of the venomous species live as hidden as they scarcely come in contact with humans.

Animals↗
PubMed1992

Dermonecrotic and lethal components of Loxosceles gaucho spider venom.

Loxosceles gaucho spider venom causes a typical dermonecrotic lesion in bitten patients and rarely causes lethal systemic effects. Gel filtration on Sephadex G 100 of L. gaucho spider venom resulted in three fractions: fraction A, containing the higher mol. wt components (approximately 35,000); fraction B, containing lower mol. wt components (approximately 15,000); and fraction C, containing very low mol. wt components (probably small peptides). The dermonecrotic and lethal activities were detected exclusively in fraction A. The venom and fraction A produced large dermonecrotic lesions in rabbits with necrosis spreading by gravity to the skin of the lateral body wall. Analysis by SDS-PAGE showed that the proteins contained in fraction A are approximately 35,000 and 33,000 mol. wt. Immunoblotting analysis showed that the proteins responsible for the dermonecrotic and lethal activity are very immunogenic and the first to be detected by antibodies during the course of immunization.

Animals↗
PubMed1980

Inhibition of 5-hydroxytryptamine contraction of guinea-pig smooth muscle treated with black widow spider venom.

Black widow spider venom (BWSV) elicited a prolonged tonic contraction of guinea-pig ileum which abolished the nicotine-induced contraction; however, the subsequent acetylcholine stimulation was found to be unchanged. These findings indicate a depletion of nerve terminal transmitters caused by BWSV without a disruption of the muscle contractile mechanism. Following the BWSV-induced contraction, the stimulation to 5-hydroxytryptamine (5-HT) was found to be abolished. This abolishment indicates a mediation of 5-HT-induced smooth muscle contraction in the nerve rather than the muscle.

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↗
PubMed2005

Proteome analysis of brown spider venom: identification of loxnecrogin isoforms in Loxosceles gaucho venom.

Brown spiders of the Loxosceles genus are distributed worldwide. In Brazil, eight species are found in Southern states, where the envenomation by Loxosceles venom (loxoscelism) is a health problem. The mechanism of the dermonecrotic action of Loxosceles venom is not totally understood. Two isoforms of dermonecrotic toxins (loxnecrogins) from L. gaucho venom have been previously purified, and showed sequence similarities to sphingomyelinase. Herein we employed a proteomic approach to obtain a global view of the venom proteome, with a particular interest in the loxnecrogin isoforms' pattern. Proteomic two-dimensional gel electrophoresis maps for L. gaucho, L. intermedia, and L. laeta venoms showed a major protein region (30-35 kDa, pI 3-10), where at least eight loxnecrogin isoforms could be separated and identified. Their characterization used a combined approach composed of Edman chemical sequencing, matrix-assisted laser desorption/ionization-time of flight mass spectrometry, and electrospray ionization-quadropole-time of flight tandem mass spectrometry leading to the identification of sphingomyelinases D. The venom was also pre-fractionated by gel filtration on a Superose 12 fast protein liqiud chromatography column, followed by capillary liquid chromatography-mass spectrometry. Eleven possible loxnecrogin isoforms around 30-32 kDa were detected. The identification of dermonecrotic toxin isoforms in L. gaucho venom is an important step towards understanding the physiopathology of the envenomation, leading to improvements in the immunotherapy of loxoscelism.

Amino Acid Sequence↗
PubMed2002

Cross-reactivity of Sydney funnel-web spider antivenom: neutralization of the in vitro toxicity of other Australian funnel-web (Atrax and Hadronyche) spider venoms.

Australian funnel-web spiders are recognized as one of the most venomous spiders to humans world-wide. Funnel-web spider antivenom (FWS AV) reverses clinical effects of envenomation from the bite of Atrax robustus and a small number of related Hadronyche species. This study assessed the in vitro efficacy of FWS AV in neutralization of the effects of funnel-web spider venoms, collected from various locations along the eastern seaboard of Australia, in an isolated chick biventer cervicis nerve-muscle preparation. Venoms were separated by SDS-PAGE electrophoresis to compare protein composition and transblotted for Western blotting and incubation with FWS AV.SDS-PAGE of venoms revealed similar low and high molecular weight protein bands. Western blotting with FWS AV showed similar antivenom binding with protein bands in all the venoms tested. Male funnel-web spider venoms (7/7) and female venoms (5/10) produced muscle contracture and fasciculation when applied to the nerve-muscle preparation. Venom effects were reversed by subsequent application of FWS AV or prevented by pretreatment of the preparation with antivenom.FWS AV appears to reverse the in vitro toxicity of a number of funnel-web spider venoms from the eastern seaboard of Australia. FWS AV should be effective in the treatment of envenomation from most, if not all, species of Australian funnel-web spiders.

Antivenins↗
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↗
PubMed1971

Destruction of mammalian motor nerve terminals by black widow spider venom.

Black widow spider venom selectively poisons motor nerve endings. A progressive and irreversible failure of neuromuscular transmission occurs in the cat. Electron microscopy of the poisoned nerve-muscle junction shows a sequence of motor nerve ending damage that culminates in disruption of the prejunctional membrane and loss of all organelles, including synaptic vesicles. The postjunctional membrane was morphologically unaffected. After complete poisoning, the contractile response to exogenous acetylcholine was severely impaired, an indication that the prejunctional site is chiefly involved in the contractile response produced by exogenous acetylcholine and that the pre- and postjunctional effects of acetylcholine were separated.

Acetylcholine↗
PubMed1988

Effect of spider venom on cochlear nerve activity consistent with glutamatergic transmission at hair cell-afferent dendrite synapse.

Venom from the spider Argiope trifasciata, a highly specific blocker of the ionic channels associated with invertebrate glutamatergic receptors, was perfused through scala tympani of the basal turn of the pig cochlea. Its effect on spontaneous and driven activity of single afferent neurons was studied. 0.1 U/ml spider venom altered the maximum driven activity without an effect on spontaneous activity. 1 U/ml spider venom suppressed both spontaneous and driven activity. These findings are consistent with the hypothesis that L-glutamate is the neurotransmitter of the synapse between inner hair cells and primary auditory afferent neurons. The results also suggest that the differences in spontaneous activity between neurons may originate in variations in neurotransmitter release.

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↗
PubMed2001

Red-back spider (Latrodectus hasselti) antivenom prevents the toxicity of widow spider venoms.

STUDY OBJECTIVES: Widow spiders of the genus Latrodectus are found worldwide and produce similar clinical envenomation syndromes. In Australia, red-back spider antivenom (RBS-AV) is effective therapy for Latrodectus hasselti envenomation and it has been reported to reverse envenomation by other widow spiders. This study assessed the efficacy of RBS-AV in preventing in vitro and in vivo toxicity of widow spider venoms of North America and Europe. METHODS: The binding of RBS-AV to alpha-latrotoxin and Latrodectus venoms (Latrodectus spp mactans, hesperus, lugubris, tredecimguttatus, hasselti) was assayed using Western blotting. Prevention of in vitro toxicity to alpha-latrotoxin and the same venoms was tested by pretreating an isolated chick biventer cervicis nerve-muscle preparation with RBS-AV. Prevention of in vivo toxicity was determined by a lethality study in male Balb/c mice (2.5 to 5x median lethal dose [LD50]) or alpha-latrotoxin (10x LD50) preincubated with antivenom or without RBS-AV (control). RESULTS: In Western blots, RBS-AV bound to alpha-latrotoxin and similar widow spider proteins in all venoms tested, indicating antigenic similarity with proteins found in RBS venom. Antivenom prevented the typical in vitro muscle contracture and loss of twitch tension seen with alpha-latrotoxin and the venoms tested. Control mice rapidly developed signs of envenomation, but mice treated with RBS-AV remained free of signs of envenomation. CONCLUSION: RBS-AV prevented both in vitro and in vivo toxicity from Latrodectus venoms and alpha-latrotoxin in mice. These data suggest that RBS-AV may be clinically effective in the treatment of envenomation resulting from the bite of other widow spiders.

Animals↗
PubMed2005

New linear polyamine derivatives in spider venoms.

Linear free polyamines were characterized in the venom of the spiders Agelenopsis aperta, Hololena curta, and Paracoelotes birulai by RP-HPLC coupled to mass spectrometry. The several linear polyamines found were tetramine, pentamine, and hexamine derivatives. Some of these natural products were identified as N-hydroxylated, guanidylated, or acetylated compounds. In addition, the biosynthetical pathway leading to the formation of acylpolyamines in spider venoms is discussed.

Animals↗