Thrombin-Like Serine Proteinases in Reptile Venoms

Swenson, Stephen D.; Stack, Samantha; Markl, Francis S.

doi:10.1201/9780429054204-27

Cited by 3 publications

(3 citation statements)

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“…Also, a large diversity of identified components (>60% of all proteins), appear to target cellular integrity, and may thus cause tissue damage and/or cytotoxicity. Two protein groups, svMPs and svSPs, comprising together about 50% of the detected venom protein diversity, are known to express strong proteolytic activity ( Gutiérrez et al, 2010 ; Swenson et al, 2021 ). These first insights into the composition of Milos viper venom are in line with the clinical manifestations elicited by envenomations caused by this species: indeed, bites by M. schweizeri are reported to cause lasting pain, swelling, decrease in erythrocytes and heart rate, increase of blood sugar, and hypotension ( Cattaneo, 2020 ).…”

Section: Resultsmentioning

confidence: 99%

Venomics of the milos viper (Macrovipera schweizeri) unveils patterns of venom composition and exochemistry across blunt-nosed viper venoms

Schulte,

Damm,

Avella

et al. 2023

Front. Mol. Biosci.

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Introduction: Snakebite is a neglected tropical disease and a globally important driver of death and morbidity. Vipers of the genus Macrovipera (Viperidae: Viperinae) are among the snakes of higher medical importance in the Old World. Despite the medical relevance of Macrovipera venoms, the knowledge regarding them is heterogeneously distributed with virtually all works conducted so far focusing on subspecies of Macrovipera lebetinus, while other species within the genus are largely overlooked. Here we present the first proteomic evaluation of the venom from the Greek endemic Milos viper (Macrovipera schweizeri). In line with clinical symptoms typically elicited by Macrovipera envenomations, Milos viper venom primarily comprises coagulotoxic and cytotoxic protein families, such as metalloproteinases (svMP) and serine proteases (svSP).Methods: We conducted comparative bioactivity assays on venoms from M. schweizeri and the M. lebetinus subspecies M. lebetinus cernovi, M. lebetinus obtusa, and M. lebetinus turanica, and showed that they all exhibit similarities in levels of cytotoxicity proteolytic activity, and inhibition of prokaryotic growth. Lastly, we compared Macrovipera venom profiles by 1D-SDS-PAGE and RP-HPLC, as well as our proteomic data with previously published Macrovipera venom proteomes.Results and discussion: The analyzes performed to reveal that a general venom profile seems to be conserved across blunt-nosed vipers, and that, M. schweizeri envenomations, similarly to those caused by other blunt-nosed vipers, are able to cause significant tissue damage. The present work represents an important starting point for the development of comparative studies across the full taxonomic range of the genus Macrovipera and can potentially help optimize the treatment of envenomations caused by M. schweizeri.

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Section: Resultsmentioning

confidence: 99%

Venomics of the milos viper (Macrovipera schweizeri) unveils patterns of venom composition and exochemistry across blunt-nosed viper venoms

Schulte,

Damm,

Avella

et al. 2023

Front. Mol. Biosci.

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“…Snake venom serine proteinases (SVSPs) catalyze a broad range of reactions targeting the coagulation cascade, kallikrein-kinin and fibrinolytic systems, complement system, endothelial cells, and platelets, all of which eventually augment the hemotoxic effect of viperid envenoming [ 91 ]. The SVSP abundance in C. rhodostoma venom proteome is well established to be around 15–25% of total venom proteins [ 17 , 18 , 20 ], while in the current transcriptomic study, the SVSP transcript level is disproportionately low (2.8% of all toxin FPKM) ( Figure 1 ).…”

Section: Resultsmentioning

confidence: 99%

De Novo Venom Gland Transcriptome Assembly and Characterization for Calloselasma rhodostoma (Kuhl, 1824), the Malayan Pit Viper from Malaysia: Unravelling Toxin Gene Diversity in a Medically Important Basal Crotaline

Tan

et al. 2023

Toxins

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In Southeast Asia, the Malayan Pit Viper (Calloselasma rhodostoma) is a venomous snake species of medical importance and bioprospecting potential. To unveil the diversity of its toxin genes, this study de novo assembled and analyzed the venom gland transcriptome of C. rhodostoma from Malaysia. The expression of toxin genes dominates the gland transcriptome by 53.78% of total transcript abundance (based on overall FPKM, Fragments Per Kilobase Million), in which 92 non-redundant transcripts belonging to 16 toxin families were identified. Snake venom metalloproteinase (SVMP, PI > PII > PIII) is the most dominant family (37.84% of all toxin FPKM), followed by phospholipase A2 (29.02%), bradykinin/angiotensin-converting enzyme inhibitor-C-type natriuretic peptide (16.30%), C-type lectin (CTL, 10.01%), snake venom serine protease (SVSP, 2.81%), L-amino acid oxidase (2.25%), and others (1.78%). The expressions of SVMP, CTL, and SVSP correlate with hemorrhagic, anti-platelet, and coagulopathic effects in envenoming. The SVMP metalloproteinase domains encode hemorrhagins (kistomin and rhodostoxin), while disintegrin (rhodostomin from P-II) acts by inhibiting platelet aggregation. CTL gene homologues uncovered include rhodocytin (platelet aggregators) and rhodocetin (platelet inhibitors), which contribute to thrombocytopenia and platelet dysfunction. The major SVSP is a thrombin-like enzyme (an ancrod homolog) responsible for defibrination in consumptive coagulopathy. The findings provide insight into the venom complexity of C. rhodostoma and the pathophysiology of envenoming.

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“…Snake venom serine proteinases (SVSPs) catalyze a broad range of reactions targeting the coagulation cascade, kallikrein-kinin and fibrinolytic systems, complement system, endothelial cells and platelets, all of which eventually augment the hemotoxic effect of viperid envenoming [86]. The SVSP abundance in C. rhodostoma venom proteome is well established to be around 15-25% of total venom proteins [12,13,15], while in the current transcriptomic study, the SVSP transcript level is disproportionately low (2.8% of all toxin FPKM) (Figure 1).…”

Section: Snake Venom Serine Proteinase (Svsp)mentioning

confidence: 99%

<em>De Novo </em>Venom Gland Transcriptome Assembly and Characterization for <em>Calloselasma rhodostoma</em> (Kuhl, 1824), the Malayan Pit Viper from Malaysia: Unravelling Toxin Gene Diversity in a Medically Important Basal Crotaline

Tan¹,

Tan²,

Ng³

et al. 2023

Preprint

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In Southeast Asia, the Malayan Pit Viper (Calloselasma rhodostoma) is a venomous snake species of medical importance and bioprospecting potential. To unveil the diversity of its toxin genes, this study assembled and analyzed the de novo venom gland transcriptome of C. rhodostoma from Malaysia. The expression of toxin genes dominates the gland transcriptome by 53.78% of total transcript abundance (based on overall FPKM), in which 92 non-redundant transcripts belonging to 16 toxin families were identified. Snake venom metalloproteinase (SVMP, PI&gt;PII&gt;PIII) is the most dominant family (37.84% of all toxin FPKM), followed by phospholipase A2 (29.02%), bradykinin/angiotensinogen-converting enzyme inhibitor-C-type natriuretic peptide (16.30%), C-type lectin (CTL, 10.01%), snake venom serine protease (SVSP, 2.81%), L-amino acid oxidase (2.25%) and others (1.78%). The expressions of SVMP, CTL and SVSP correlate with hemorrhagic, anti-platelet and coagulopathic effects in envenoming. The SVMP metalloproteinase domains encode hemorrhagins (kistomin and rhodostoxin), while disintegrin (rhodostomin from P-II) is platelet-inhibitory. CTL gene homologues uncovered include rhodocytin (platelet aggregators) and rhodocetin (platelet inhibitor), which contribute to thrombocytopenia and platelet dysfunction. The major SVSP is a thrombin-like enzyme (ancrod homolog) responsible for defibrination in consumptive coagulopathy. The findings provide insight into the venom complexity of C. rhodostoma and the pathophysiology of envenoming.

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Thrombin-Like Serine Proteinases in Reptile Venoms

Cited by 3 publications

References 1 publication

Venomics of the milos viper (Macrovipera schweizeri) unveils patterns of venom composition and exochemistry across blunt-nosed viper venoms

Venomics of the milos viper (Macrovipera schweizeri) unveils patterns of venom composition and exochemistry across blunt-nosed viper venoms

De Novo Venom Gland Transcriptome Assembly and Characterization for Calloselasma rhodostoma (Kuhl, 1824), the Malayan Pit Viper from Malaysia: Unravelling Toxin Gene Diversity in a Medically Important Basal Crotaline

<em>De Novo </em>Venom Gland Transcriptome Assembly and Characterization for <em>Calloselasma rhodostoma</em> (Kuhl, 1824), the Malayan Pit Viper from Malaysia: Unravelling Toxin Gene Diversity in a Medically Important Basal Crotaline

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