Purification and characterization of a toxin from brown recluse spider (Loxosceles reclusa) venom gland extracts

Babcock, James L.; Civello, David J.; Geren, Collis R.

doi:10.1016/0041-0101(81)90105-7

Cited by 30 publications

(6 citation statements)

References 20 publications

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“…We searched the Scytodes venom gland transcripts specifically for sequences with homology to sphingomyelinase D (SMase D), a highly abundant 30–35 kDa venom protein that is neurotoxic to insects 71 and causes cell death in vivo in mammals 38,39,72–81 . Sicariid venoms include multiple paralogs of the SMase D gene family ( SicTox ) 76,82–90 . While the SMase D enzyme plays an important role in prey capture in sicariids, we have not found it in the venom transcriptome or proteome of Scytodes or any other haplogyne venom gland transcriptome so far.…”

Section: Resultsmentioning

confidence: 99%

Spit and Venom from Scytodes Spiders: A Diverse and Distinct Cocktail

et al. 2013

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Spiders from the family Scytodidae have a unique prey capturing technique: they spit a zig-zagged silken glue to tether prey to a surface. Effectiveness of this sticky mixture is based on a combination of contraction and adhesion, trapping prey until the spider immobilizes it by envenomation and then feeds. We identify components expressed in Scytodes thoracica venom glands using combined transcriptomic and proteomic analyses. These include homologues of toxic proteins astacin metalloproteases and potentially toxic proteins including venom allergen, longistatin, and translationally controlled tumor protein (TCTP). We classify 19 distinct groups of candidate peptide toxins; 13 of these were detected in the venom, making up 35% of the proteome. Six have significant similarity to toxins from spider species spanning mygalomorph and nonhaplogyne araneomorph lineages, suggesting their expression in venom is phylogenetically widespread. Twelve peptide toxin groups have homologues in venom gland transcriptomes of other haplogynes. Of the transcripts, approximately 50% encode glycine-rich peptides that may contribute to sticky fibers in Scytodes spit. Fifty-one percent of the identified venom proteome is a family of proteins that is homologous to sequences from Drosophila sp. and Latrodectus hesperus with uncharacterized function. Characterization of these components holds promise for discovering new functional activity.

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Section: Resultsmentioning

confidence: 99%

Spit and Venom from Scytodes Spiders: A Diverse and Distinct Cocktail

et al. 2013

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“…The exact mechanisms by which the S.S. Veiga et al venoms cause their deleterious effects are currently under investigation, with putative explanations involving an indirect event, as is the case for endothelial cell-dependent neutrophil activation caused by the venoms and seemingly related to the dermonecrotic lesion (4,(12)(13)(14). The presence of a sphingomyelinase D-like enzyme (32-35 kDa) probably associated with necrotic, hemolytic and thrombocytopenic activities triggered by the venoms has also been identified in different Loxosceles species (3,4,6,10,15,16). Other enzymes such as a hyaluronidase have been postulated to be a spreading factor during the lesions (4,17), and protease activities also appear to have some participation in the noxious effects of the venoms (11,(18)(19)(20)(21).…”

Section: Introductionmentioning

confidence: 99%

“…Envenomation provokes two major kinds of signals, i.e., local lesions at the bite site characterized by edema followed by vasodilatation, blood vessel degeneration, local hemorrhage and a significant cutaneous tissue injury with gravitational spreading, that can exacerbate to necrotic skin ulcers and degeneration (1)(2)(3)(4), and systemic effects that begin as a malaise and can become generalized, with hemolysis, thrombocytopenia, disseminated intravascular coagulation and renal failure. These clinical signs and toxicological effects appear to be phenomena similar for several Loxosceles species including the more studied L. reclusa, L. laeta, L. intermedia and L. gaucho species (4)(5)(6)(7)(8).…”

Section: Introductionmentioning

confidence: 99%

Extracellular matrix molecules as targets for brown spider venom toxins

Veiga

Zanetti

Braz

et al. 2001

Braz J Med Biol Res

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Loxoscelism, the term used to describe lesions and clinical manifestations induced by brown spiders venom (Loxosceles genus), has attracted much attention over the last years. Brown spider bites have been reported to cause a local and acute inflammatory reaction that may evolve to dermonecrosis (a hallmark of envenomation) and hemorrhage at the bite site, besides systemic manifestations such as thrombocytopenia, disseminated intravascular coagulation, hemolysis, and renal failure. The molecular mechanisms by which Loxosceles venoms induce injury are currently under investigation. In this review, we focused on the latest reports describing the biological and physiopathological aspects of loxoscelism, with reference mainly to the proteases recently described as metalloproteases and serine proteases, as well as on the proteolytic effects triggered by L. intermedia venom upon extracellular matrix constituents such as fibronectin, fibrinogen, entactin and heparan sulfate proteoglycan, besides the disruptive activity of the venom on Engelbreth-Holm-Swarm basement membranes. Degradation of these extracellular matrix molecules and the observed disruption of basement membranes could be related to deleterious activities of the venom such as loss of vessel and glomerular integrity and spreading of the venom toxins to underlying tissues. Correspondence

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“…The use of preparative gel electrophoresis and gel filtration provided tools for investigation of each protein fraction from brown spider venom [ 42 – 44 ]. Cation-exchange chromatography at pH 4.0 purified the toxin fraction responsible for lethality in mice, induction of necrosis in rabbits, calcium-dependent hemolysis of human erythrocytes, and a decrease in the calcium-induced coagulation time of human plasma [ 45 ]. Indeed, a fraction of the L. reclusa venom has also shown to produce hematological effects in albino mice [ 46 , 47 ].…”

Section: History Of the Brown Spider Venom Toxinologymentioning

confidence: 99%

Highlights in the knowledge of brown spider toxins

Chaves-Moreira

Senff‐Ribeiro

Wille

et al. 2017

J Venom Anim Toxins Incl Trop Dis

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Brown spiders are venomous arthropods that use their venom for predation and defense. In humans, bites of these animals provoke injuries including dermonecrosis with gravitational spread of lesions, hematological abnormalities and impaired renal function. The signs and symptoms observed following a brown spider bite are called loxoscelism. Brown spider venom is a complex mixture of toxins enriched in low molecular mass proteins (4–40 kDa). Characterization of the venom confirmed the presence of three highly expressed protein classes: phospholipases D, metalloproteases (astacins) and insecticidal peptides (knottins). Recently, toxins with low levels of expression have also been found in Loxosceles venom, such as serine proteases, protease inhibitors (serpins), hyaluronidases, allergen-like toxins and histamine-releasing factors. The toxin belonging to the phospholipase-D family (also known as the dermonecrotic toxin) is the most studied class of brown spider toxins. This class of toxins single-handedly can induce inflammatory response, dermonecrosis, hemolysis, thrombocytopenia and renal failure. The functional role of the hyaluronidase toxin as a spreading factor in loxoscelism has also been demonstrated. However, the biological characterization of other toxins remains unclear and the mechanism by which Loxosceles toxins exert their noxious effects is yet to be fully elucidated. The aim of this review is to provide an insight into brown spider venom toxins and toxicology, including a description of historical data already available in the literature. In this review article, the identification processes of novel Loxosceles toxins by molecular biology and proteomic approaches, their biological characterization and structural description based on x-ray crystallography and putative biotechnological uses are described along with the future perspectives in this field.

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Purification and characterization of a toxin from brown recluse spider (Loxosceles reclusa) venom gland extracts

Cited by 30 publications

References 20 publications

Spit and Venom from Scytodes Spiders: A Diverse and Distinct Cocktail

Spit and Venom from Scytodes Spiders: A Diverse and Distinct Cocktail

Extracellular matrix molecules as targets for brown spider venom toxins

Highlights in the knowledge of brown spider toxins

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