Comparative study of the enzymatic, hemorrhagic, procoagulant and anticoagulant activities of some animal venoms

doi:10.1016/0742-8413(92)90011-U

Comparative Biochemistry and Physiology Part C: Comparative Pharmacology

Volume 103, Issue 2, October 1992, Pages 299-302

https://doi.org/10.1016/0742-8413(92)90011-U Get rights and content

Abstract

1. The enzymatic, hemorrhagic, procoagulant and anticoagulant activities of venoms of some animals including snakes, lizards, toads, scorpions, spider, wasps, bees and ants were compared.

2. Snake venom was the richest source of enzymes among the animal venoms. Most other animal venoms were devoid of phosphodiesterase, l-amino acid oxidase, alkaline phosphomonoesterase and acetylcholinesterase activities and only a few exhibited arginine ester hydrolase activity. These venoms, however, exhibited wide ranges of protease, 5'-nucleotidase and hyaluronidase activities. Most of the animal venoms examined exhibited some phospholipase A activity.

3. Other than snake venoms, only venoms of the toad Bufo calamita and the lizards were hemorrhagic, and only venoms of the social wasps, social bees and harvester ant exhibited strong anticoagulant activity. Procoagulant activity occurs only in snake venoms.

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The phylogenetic analyses demonstrated that the genes corresponding to BmooHyals sequences were orthologous, where BmooHyal-2 was closer to hyaluronidases from the families Colubridae and Pythonidae while BmooHyal-1 was closer to enzymes from Viperidae family (Fig. 5C). The hyaluronidase activity detected in the Bothrops snake venom varies among the snake species and with age (Antunes et al., 2010; Tan and Ponnudurai, 1991), and it is weaker than the hyaluronidase activity found in the venom of other animals (Lira et al., 2007; Tan and Ponnudurai, 1992). In our study, we detected hyaluronidase activity in the B. moojeni venom (specific activity of 1678.13 TRU/mg) confirming that these enzymes are present and active in this snake species.
Snakebites are a serious health problem in tropical countries. In Brazil, the genus Bothrops (Viperidae family) causes most of the ophidic accidents, characterized by proteolysis and haemorrhage. Snake venoms are rich sources of toxins with great therapeutic and biotechnological potential and omics approaches is a valuable tool for identification of new bioactive components in the venom. In this study, we described the first transcriptome of the venom gland of Bothrops moojeni snake, using the next-generation sequencing with the Illumina platform. We identified: (i) 20 venom components classes, among which metalloproteases were the most expressed ones, followed by serine proteases and phospholipases; and (ii) the 33 full-length amino acid sequences of toxins that have never been reported before in B. moojeni venom, such as one cysteine-rich secretory protein (Moojin), two hyaluronidases (BmooHyal-1 and BmooHyal-2), and one three-finger toxin (Bmoo-3FTx). Altogether, the transcripts identified herein represent a starting point for the analysis of structure-function relationships of toxins, which shall help develop novel biological tools and therapeutic drugs.
Pathophysiological effects caused by the venom of the social wasp Synoeca surinama
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In all doses tested, the nociceptive response was similar to the formalin group in both phases evaluated. As previously reported, pain after sting is the first symptom observed in 100% of cases and may require palliative care for its control (Balit et al., 2003; Brigatte et al., 2011; Tan and Ponnudurai, 1992). Besides the commom symptoms noted, oedema and pain, this study showed an unusual hemorrhagic effect with half of a venom reservoir equivalent of S. surinama crude venom (450 μg/animal).
Envenomation by wasp stings is a public health preoccupation, and signals after stings have variable effects depending on the number of attacks and individual sensitivities. Even with the high rate of wasp sting cases, the study of phatophysiological effects of the envenomation is still very incipient. In this context, early and accurate assessment of this prognostic can aid in the reduction of the symptomatology and complete remission of the later symptoms. Then, the present study evaluated the toxicological effects caused by envenomation produced by Synoeca surinama, a wasp easily found in Neotropical regions. In vivo tests comprised the evaluation of LD₅₀ (OECD 423), nociception, edema, myotoxic lesion and hemorrhage induction, in vitro tests were realized to evaluate hemolysis, contractile and coagulation alteration. The envenomation effects observed were dose- and time-dependent; the LD₅₀ observed for S. surinama was 178 μg/kg, approximately 17 times more lethal than that of the honeybee. Moreover, a potent algesic and oedema effect, and weak hemorrhagic signal were observed after injection of the venom wasp. Assays in vitro showed that this venom is able to prolong the clotting time of plasma and to increase creatine kinase levels. Our results demonstrated that this venom induced serious local and systemic effects in mammals and, so, to avoid permanent damage to the patient, health professionals should carefully investigate each accident. Moreover, due to its high occurrence in Neotropical regions, ecological management, particularly in areas with free access of children and elderly, should be performed.
Studies on biochemical and biomedical properties of Conus betulinus venom
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Molecular weight of the crude venom extract was determined by using SDS-PAGE. Toxicity studies were carried out using haemolytic and brine shrimp lethality assays. Fibrin plate assay and substrate SDS-PAGE were used to determine the effect of sample on fibrin(ogen)olytic and proteolytic activity. The FTIR characterisation and chemical fingerprinting of amino acid were done with HPTLC. Enzymatic activities like phospholipase and hyaluronidase were measured spectrophotometrically and calculated in units. Anticancer screening was carried out by MTT assay.
Studies on this deadly venom revealed six different molecular weight proteins of medical significance ranging between 20.0 kDa and 97.4 kDa. The protein content was estimated as 0.9 mg/mL. Haemolytic activity in erythrocytes was recorded and LC₅₀ (Artemia) at 31.5 μg/mL. Further the venom showed considerable enzymatic properties like gelatinolytic, caesinolytic, fibrinolytic and fibrinogenolytic activities. The hyaluronidase and phospholipase activities were recorded at meagre range. The venom exhibited significant activity against HeLa cell lines. Moreover the evolution of venom is the crucial nature of Conus peptides in their challenging ecosystem. Periodical study on these peptides will unveil more peptides of biomedical use.
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However, as indicated by previous studies, it is probably a multimediated phenomenon. Besides the significant hindpaw-induced oedema by S. cyanea venom, a slight hemorrhagic effect was observed at the assayed doses, contrary to that reported in previous studies which have shown that wasp venoms exhibit moderate to strong hemorrhagic activity (Schmidt et al., 1986; Tan and Ponnudurai, 1992). This hemorrhagic effect may indicate the low presence of molecules with fibrinolytic and anticoagulant activities in S. cyanea wasp venom, as already described for other wasp venoms (Czaikoski et al., 2010).
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2011, Toxicon
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All of these proteases in jellyfish venoms are likely to be metalloproteinases as they could be sufficiently inhibited by 1,10-phenanthroline (Fig. 2B). Additionally, hyaluronidase is also a common venom enzyme (Tan and Ponnudrai, 1992) and has been detected as a constituent of a number of animal venom (Geren and Odell, 1984). It is non-toxic and is known as ‘spreading factor’ (Kreil, 1995), due to its ability to hydrolyze connective tissue, thus facilitating the action of other venom components.
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Comparative Biochemistry and Physiology Part C: Comparative Pharmacology

Abstract

References (21)

Coagulant and anticoagulant action of snake venoms

Toxicon

A new and rapid colourimetric determination of acetyl-cholinesterase activity

Biochem. Pharmacol.

Enzymatic and hemolytic properties of brown recluse spider (Loxosceles reclusa) toxin and extracts of venom apparatus, cephalothorax and abdomen

Toxicon

A comparative study of the enzymatic and toxic properties of venoms of the Asian lance-headed pit viper (Genus Trimeresurus)

Comp. Biochem. Physiol.

A comparative study of the biological properties of venoms from snakes of the genus Vipera (true adders)

Comp. Biochem. Physiol.

A comparative study of the biological activities of venoms from snakes of the genus Agkistrodon (Moccasins and Copperheads)

Comp. Biochem. Physiol.

A comparative study of the biological properties of Australian elapid venoms

Comp. Biochem. Physiol.

A comparative study of cobra (Naja) venom enzymes

Comp. Biochem. Physiol.

Acidimetric assay for phospholipase A using egg yolk suspension as substrate

Anal. Biochem.

A brain extract as a substitute for platelet suspension in the thromboplastin generation test

Nature

Cited by (51)

Type I-like metalloproteinase in the venom of the West African saw-scaled carpet viper (Echis ocellatus) has anti-trypanosomal activity against African trypanosomes

New findings from the first transcriptome of the Bothrops moojeni snake venom gland

Pathophysiological effects caused by the venom of the social wasp Synoeca surinama

Studies on biochemical and biomedical properties of Conus betulinus venom

Pharmacological characterization of Synoeca cyanea venom: An aggressive social wasp widely distributed in the Neotropical region

Scyphozoan jellyfish venom metalloproteinases and their role in the cytotoxicity