Ophidian envenomation strategies and the role of purines

Aird, Steven D.

doi:10.1016/s0041-0101(01)00232-x

Cited by 280 publications

(271 citation statements)

References 640 publications

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“…Cerastes cerastes venom is highly toxic, primarily attributable to the activity of various proteolytic enzymes it contains (23) (24) . Cerastes cerastes venom also exhibits a range of biological activities including antiangiogenic (25) , antitumor (26) , antibacterial (27) , and antiprotozoal (16) effects.…”

Section: Introductionmentioning

confidence: 99%

In vitro antischistosomal activity of venom from the Egyptian snake Cerastes cerastes

Hassan

Abdel-Rahman

Ibrahim

et al. 2016

Rev. Soc. Bras. Med. Trop.

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Introduction:We studied the potential in vitro antischistosomal activity of Cerastes cerastes venom on adult Schistosoma mansoni worms. Methods: Live specimens of the horned viper snake, C. cerastes were collected from the Aswan Governorate (Egypt). Venom was collected from snakes by manual milking. Worms of S. mansoni were obtained from infected hamsters by perfusion and isolated from blood using phosphate buffer. Mortality rates of worms were monitored after 3 days of exposure to snake venom at LC 50 and various sublethal concentrations (10, 5, 2.5µg/ml). Scanning electron microscopy was used to investigate tegumental changes in treated worms after exposure to LC 50 doses of venom. Results: The LC 50 of C. cerastes venom was 21.5µg/ml. The effect of C. cerastes venom on Schistosoma worms varied according to their sex. The mortality rate of male and female worms after 48-h exposure was 83.3% and 50% , respectively. LC 50 of C. cerastes venom induced mild to severe tegumental damage in Schistosoma worms in the form of destruction of the oral sucker, shrinkage and erosion of the tegument, and loss of some tubercle spines. Conclusions: The present study demonstrated that C. cerastes venom exerts potential in vitro antischistosomal activity in a time and dose-dependent manner. These results may warrant further investigations to develop novel schistosomicidal agents from C. cerastes snake venom.

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Section: Introductionmentioning

confidence: 99%

In vitro antischistosomal activity of venom from the Egyptian snake Cerastes cerastes

Hassan

Abdel-Rahman

Ibrahim

et al. 2016

Rev. Soc. Bras. Med. Trop.

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“…An estimated 2.5 million people are bitten by snakes each year and these are estimated to result in up to as high as 95000 deaths worldwide [2, 3]. Snake venoms are complex mixtures of enzymatic [4,5] and non enzymatic proteins [6], together with other components such as carbohydrates, lipids, nucleosides and metals [4,7]. Snake venom serine proteases are major components and have been identified mainly in the venoms of snakes belonging to the viperidae family with a few occurring in members of the elapidae, colubridae and hydrophidae families [8].…”

Section: Introductionmentioning

confidence: 99%

Sequence and phylogenetic analysis of viper venom serine proteases

Vaiyapuri¹,

Thiyagarajan²,

Hutchinson³

et al. 2012

Bioinformation

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Abstract:Snakebites are a major neglected tropical disease responsible for as many as 95000 deaths every year worldwide. Viper venom serine proteases disrupt haemostasis of prey and victims by affecting various stages of the blood coagulation system. A better understanding of their sequence, structure, function and phylogenetic relationships will improve the knowledge on the pathological conditions and aid in the development of novel therapeutics for treating snakebites. A large dataset for all available viper venom serine proteases was developed and analysed to study various features of these enzymes. Despite the large number of venom serine protease sequences available, only a small proportion of these have been functionally characterised. Although, they share some of the common features such as a C-terminal extension, GWG motif and disulphide linkages, they vary widely between each other in features such as isoelectric points, potential N-glycosylation sites and functional characteristics. Some of the serine proteases contain substitutions for one or more of the critical residues in catalytic triad or primary specificity pockets. Phylogenetic analysis clustered all the sequences in three major groups. The sequences with substitutions in catalytic triad or specificity pocket clustered together in separate groups. Our study provides the most complete information on viper venom serine proteases to date and improves the current knowledge on the sequence, structure, function and phylogenetic relationships of these enzymes. This collective analysis of venom serine proteases will help in understanding the complexity of envenomation and potential therapeutic avenues. Background:Snakebite is a major neglected public health issue particularly among agricultural communities living in rural regions throughout the world [1, 2]. An estimated 2.5 million people are bitten by snakes each year and these are estimated to result in up to as high as 95000 deaths worldwide . Snake venom serine proteases are major components and have been identified mainly in the venoms of snakes belonging to the viperidae family with a few occurring in members of the elapidae, colubridae and hydrophidae families [8]. Many snake venom serine proteases exert their effects through the ability to disrupt the normal haemostasis of envenomed prey and victims [9]. Indeed, viper venom serine proteases (VVSPs) affect various stages of the blood coagulation system, activate platelets and directly act upon fibrinogen. These include pro-coagulant

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“…Many toxins that affect hemostasis are produced by venomous animals such as snakes and spiders, which use these compounds to facilitate capture and digestion of prey (Markland, 1997;Aird, 2002). Some lepidopteran larvae, notably those of the family Saturniidae, also produce venoms that adversely impact hemostasis.…”

Section: Introductionmentioning

confidence: 99%

A catalog for the transcripts from the venomous structures of the caterpillar Lonomia obliqua: Identification of the proteins potentially involved in the coagulation disorder and hemorrhagic syndrome

Veiga

Ribeiro

Guimarães

et al. 2005

Gene

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Accidents with the caterpillar Lonomia obliqua are often associated with a coagulation disorder and hemorrhagic syndrome in humans. In the present study, we have constructed cDNA libraries from two venomous structures of the caterpillar, namely the tegument and the bristle. Highthroughput sequencing and bioinformatics analyses were performed in parallel. Over one thousand cDNAs were obtained and clustered to produce a database of 538 contigs and singletons (clusters) for the tegument library and 368 for the bristle library. We have thus identified dozens of fulllength cDNAs coding for proteins with sequence homology to snake venom prothrombin activator, trypsin-like enzymes, blood coagulation factors and prophenoloxidase cascade activators. We also report cDNA coding for cysteine proteases, Group III phospholipase A2, Ctype lectins, lipocalins, in addition to protease inhibitors including serpins, Kazal-type inhibitors, cystatins and trypsin inhibitor-like molecules. Antibacterial proteins and housekeeping genes are also described. A significant number of sequences were devoid of database matches, suggesting that their biologic function remains to be defined. We also report the N-terminus of the most abundant proteins present in the bristle, tegument, hemolymph, and "cryosecretion". Thus, we have created a catalog that contains the predicted molecular weight, isoelectric point, accession number, and putative function for each selected molecule from the venomous structures of L. obliqua. The role of these molecules in the coagulation disorder and hemorrhagic syndrome caused by envenomation with this caterpillar is discussed. All sequence information and the Supplemental Data, including Figures and Tables with hyperlinks to FASTA-formatted files for each contig and the best match to the Databases, are available at http://www.ncbi.nih.gov/projects/omes.

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Ophidian envenomation strategies and the role of purines

Cited by 280 publications

References 640 publications

In vitro antischistosomal activity of venom from the Egyptian snake Cerastes cerastes

In vitro antischistosomal activity of venom from the Egyptian snake Cerastes cerastes

Sequence and phylogenetic analysis of viper venom serine proteases

A catalog for the transcripts from the venomous structures of the caterpillar Lonomia obliqua: Identification of the proteins potentially involved in the coagulation disorder and hemorrhagic syndrome

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