Proteolytic activity of tarantula venoms due to contamination with saliva

Perret, Beat A.

doi:10.1016/0041-0101(77)90101-5

Cited by 25 publications

(8 citation statements)

References 28 publications

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“…An important observation is that P. regalis venom induces significantly higher hyaluronidase activity, which could be related to its higher toxicity. We also found that the venoms do not display phospholipase A 2 or caseinolytic activity, in agreement with previous studies that suggest that neither phospholipase A nor protease activity is present in tarantula venoms [35, 37]. …”

Section: Discussionsupporting

confidence: 93%

Pharmacological characterization of venoms from three theraphosid spiders: Poecilotheria regalis, Ceratogyrus darlingi and Brachypelma epicureanum

García-Arredondo¹,

Rodríguez-Rios²,

Díaz-Peña³

et al. 2015

J Venom Anim Toxins Incl Trop Dis

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BackgroundTarantulas (Theraphosidae) represent an important source of novel biologically active compounds that target a variety of ion channels and cell receptors in both insects and mammals. In this study, we evaluate and compare the pharmacological activity of venoms from three taxonomically different theraphosid spiders bred in captivity: Poecilotheria regalis, an aggressive arboreal tarantula from southeastern India; Ceratogyrus darlingi, an aggressive tarantula from southern Africa; and Brachypelma epicureanum, a docile tarantula from the Yucatan dry forest of Mexico. Prior to this study, no research had been conducted with regard to the composition and pharmacological activity of these venoms.MethodsThe pharmacological characterization of the venoms was described for the first time by the assessment of their toxicity in crickets (LD50) along with their nociceptive (by using the formalin test), hyaluronidase, phospholipase A2, edematogenic and caseinolytic activity.ResultsP. regalis and B. epicureanum venoms induced a similar lethal effect on crickets (LD50 = 5.23 ± 3.1 and 14.4 ± 5.0 μg protein/g 48 h post-injection, respectively), whereas C. darlingi venom (119.4 ± 29.5 μg protein/g 48 h post-injection) was significantly less lethal than the other two venoms. All three venoms induced similar edematogenic activity on rats but did not induce nociceptive behavior. The assessment of enzymatic activity indicated that P. regalis venom induces significantly higher hyaluronidase activity (27.6 ± 0.9 TRU/mg) than both C. darlingi (99.7 ± 1.9 TRU/mg) and B. epicureanum (99.6 ± 1.6 TRU/mg); these latter venoms did not display phospholipase A2 or caseinolytic activity.ConclusionsThis study demonstrates that these theraphosid spiders of different habitats produce venoms with different activities. P. regalis venom displays a high level of hyaluronidase activity, which may be associated with its potentially medically significant bite.

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Section: Discussionsupporting

confidence: 93%

Pharmacological characterization of venoms from three theraphosid spiders: Poecilotheria regalis, Ceratogyrus darlingi and Brachypelma epicureanum

García-Arredondo¹,

Rodríguez-Rios²,

Díaz-Peña³

et al. 2015

J Venom Anim Toxins Incl Trop Dis

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“…Significant proteolytic activity is generally a good indicator for contamination by regurgitates (Perret, 1977;Kuhn-Nentwig et al, 2004) and copper determinations have been used to check for contamination with hemolymph. As noted, the venom will contain small amount protease detectable in protracted 24 hour tests, but it is not a universal indicator for contamination as suggested.…”

Section: Characteristicsmentioning

confidence: 99%

Comments on the Natural Expression and Artificial Extraction of Venom Gland Components from Spiders

Kristensen¹

2005

Toxin Reviews

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Milking or gland extraction can be used to harvest mRNA, toxins, and other materials from spiders that are suitable for a wide variety of studies, but the milked venom and extracts should not be assumed to be equivalent to naturally expressed venoms injected into insects. A much better understanding of the diverse anatomies, physiologies, and dispersion mechanisms is required for this understanding.

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“…First, Mebs acknowledged that the venom was a gift (i.e., he did not collect it). Second, though there appear to be exceptions (Young and Pincus 2001;da Silva et al 2004), very little peptidase activity has been observed in spider venoms that have been collected so as to avoid contamination by regurgitated digestive fluid (see Perret 1977, Geren and Odell 1984, and Kuhn-Nentwig et al 1994 for reviews of this problem). And third, as indicated above, the digestive fluid peptidases share several characteristics with the peptidases Mebs described.…”

Section: Introductionmentioning

confidence: 99%

Astacin family metallopeptidases and serine peptidase inhibitors in spider digestive fluid

Foradori

Tillinghast

Smith

et al. 2006

Comparative Biochemistry and Physiology Part B: Biochemistry an

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Digestive fluid of the araneid spider Argiope aurantia is known to contain zinc metallopeptidases. Using anion-exchange chromatography, size-exclusion chromatography, sucrose density gradient centrifugation, and gel electrophoresis, we isolated two lower-molecular-mass peptidases, designated p16 and p18. The N-terminal amino acid sequences of p16 (37 residues) and p18 (20 residues) are 85% identical over the first 20 residues and are most similar to the N-terminal sequences of the fully active form of meprin (β subunits) from several vertebrates (47-52% and 50-60% identical, respectively). Meprin is a peptidase in the astacin (M12A) subfamily of the astacin (M12) family. Additionally, a 66-residue internal sequence obtained from p16 aligns with the conserved astacin subfamily domain. Thus, at least some spider digestive peptidases appear related to astacin of decapod crustaceans. However, important differences between spider and crustacean metallopeptidases with regard to isoelectric point and their susceptibility to hemolymph-borne inhibitors are demonstrated. Anomalous behavior of the lower-molecular-mass Argiope peptidases during certain fractionation procedures indicates that these peptidases may take part in reversible associations with each other or with other proteins. A. aurantia digestive fluid also contains inhibitory activity effective against insect digestive peptidases. Here we present evidence for at least thirteen, heat-stable serine peptidase inhibitors ranging in molecular mass from about 15 to 32 kDa.

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Proteolytic activity of tarantula venoms due to contamination with saliva

Cited by 25 publications

References 28 publications

Pharmacological characterization of venoms from three theraphosid spiders: Poecilotheria regalis, Ceratogyrus darlingi and Brachypelma epicureanum

Pharmacological characterization of venoms from three theraphosid spiders: Poecilotheria regalis, Ceratogyrus darlingi and Brachypelma epicureanum

Comments on the Natural Expression and Artificial Extraction of Venom Gland Components from Spiders

Astacin family metallopeptidases and serine peptidase inhibitors in spider digestive fluid

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