Biochemical and pharmacological characterization of <i>Trimersurus malabaricus</i> snake venom

Gowda, Raghavendra; Rajesh, R.; Angaswamy, Nataraj; Krishna, Sharath; Sannanayak, Vishwanath Bannikuppe

doi:10.1002/jcb.26782

Cited by 7 publications

(3 citation statements)

References 40 publications

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“…In addition, green pit vipers were responsible for 58% of snakebites reported in Vietnam in 2017 [9]. Trimeresurus venom varies in toxicity between species; prolonged clotting time is a significant symptom observed in humans [10], and tissue damage and hematotoxicity in bite victims have also been reported [11,12]. Since there is no species-specific antivenom available for Trimeresurus, except T. albolabris, the only treatment available for bite cases has been a hetero-specific antivenom [13].…”

Section: Introductionmentioning

confidence: 99%

Venomics and Cellular Toxicity of Thai Pit Vipers (Trimeresurus macrops and T. hageni)

Kumkate

Chanhome

Thiangtrongjit

et al. 2020

Toxins

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The two venomous pit vipers, Trimeresurus macrops and T. hageni, are distributed throughout Thailand, although their abundance varies among different areas. No species-specific antivenom is available for their bite victims, and the only recorded treatment method is a horse antivenom raised against T. albolabris crude venom. To facilitate assessment of the cross-reactivity of heterologous antivenoms, protein profiles of T. macrops and T. hageni venoms were explored using mass-spectrometry-based proteomics. The results show that 185 and 216 proteins were identified from T. macrops and T. hageni venoms, respectively. Two major protein components in T. macrops and T. hageni venoms were snake venom serine protease and metalloproteinase. The toxicity of the venoms on human monocytes and skin fibroblasts was analyzed, and both showed a greater cytotoxic effect on fibroblasts than monocytic cells, with toxicity occurring in a dose-dependent rather than a time-dependent manner. Exploring the protein composition of snake venom leads to a better understanding of the envenoming of prey. Moreover, knowledge of pit viper venomics facilitates the selection of the optimum heterologous antivenoms for treating bite victims.

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Section: Introductionmentioning

confidence: 99%

Venomics and Cellular Toxicity of Thai Pit Vipers (Trimeresurus macrops and T. hageni)

Kumkate

Chanhome

Thiangtrongjit

et al. 2020

Toxins

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“…As in our previous study [ 13 ], here we found a hyaluronidase in the venom of N. fodiens . This non-toxic protein is commonly present in many animal venoms, including venoms of snakes, spiders and ants [ 44 , 61 , 62 ], and acts as a toxin spreading factor [ 60 , 61 ]. Due to its ability to hydrolyze connective tissue, hyaluronidase facilitates the action of other venom components [ 26 ].…”

Section: Discussionmentioning

confidence: 99%

A new, widespread venomous mammal species: hemolytic activity of Sorex araneus venom is similar to that of Neomys fodiens venom

2022

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Background Venom production has evolved independently many times in the animal kingdom, although it is rare among mammals. Venomous shrews produce toxins in their salivary glands and use their venoms to hunt and store prey. Thus far, the toxicity and composition of shrew venoms have been studied only in two shrew species: the northern short-tailed shrew, Blarina brevicauda, and the Eurasian water shrew, Neomys fodiens. Venom of N. fodiens has potent paralytic activity which enables hunting and storing prey in a comatose state. Here, we assayed the hemolytic effects of extracts from salivary glands of N. fodiens and the common shrew, Sorex araneus, in erythrocytes of Pelophylax sp. frogs. We identified toxins in shrew venom by high-performance liquid chromatography coupled to tandem mass spectrometry. Results Our results prove, confirming a suggestion made four centuries ago, that S. araneus is venomous. We also provide the first experimental evidence that shrew venoms produce potent hemolysis in frog erythrocytes. We found significant concentration-dependent effects of venoms of N. fodiens and S. araneus on hemolysis of red blood cells evaluated as hemoglobin release. Treatment of erythrocytes with N. fodiens venom at concentrations of 1.0 and 0.5 mg/ml and with S. araneus venom at concentration of 1.0 mg/ml caused an increased release of hemoglobin. Our findings confirm that hemolytic effects of N. fodiens venom are stronger than those produced by S. araneus venom. We identified four toxins in the venom of N. fodiens: proenkephalin, phospholipase A2 (PLA2), a disintegrin and metalloproteinase domain-containing protein (ADAM) and lysozyme C, as well as a non-toxic hyaluronidase. In the venom of S. araneus we found five toxins: proenkephalin, kallikrein 1-related peptidase, beta-defensin, ADAM and lysozyme C. PLA2 and ADAMs are likely to produce hemolysis in frog erythrocytes. Conclusions Our results clearly show that shrew venoms possess hemolytic action that may allow them to hunt larger prey. Since a member of the numerous genus Sorex is venomous, it is likely that venom production among shrews and other eulipotyphlans may be more widespread than it has previously been assumed.

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“…These components are linked to the toxic activities of these venoms, such as paralysis and convulsions, irregular respiration, inhibition of heart rate, increase in vascular permeability, decrease in blood pressure, haemolysis, and death [ 7 , 9 , 10 , 14 ]. Hyaluronidase commonly occurs in venoms of various animal taxa, but is devoid of toxic activity [ 16 , 17 ]. Instead, due to its ability to hydrolyse connective tissue, it promotes the spreading of toxins after envenomation [ 8 , 18 ].…”

Section: Introductionmentioning

confidence: 99%

Proteins from shrews’ venom glands play a role in gland functioning and venom production

Kowalski,

Marciniak,

Nekaris

et al. 2024

Zoological Lett

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Venom production has evolved independently many times in the animal kingdom, although it is rare among mammals. Venomous shrews produce venom in their submandibular salivary glands and use it for food acquisition. Only a few toxins have been identified in shrew venoms thus far, and their modes of action require investigation. The biological and molecular processes relating to venom production and gland functioning also remain unknown. To address this gap, we investigated protein content in extracts from venom glands of two shrew species, Neomys fodiens and Sorex araneus, and interpreted their biological functions. Applying a proteomic approach coupled with Gene Ontology enrichment analysis, we identified 313 and 187 putative proteins in venom glands of N. fodiens and S. araneus, respectively. A search of the UniProt database revealed that most of the proteins found in both shrew species were involved in metabolic processes and stress response, while GO enrichment analysis revealed more stress-related proteins in the glands of S. araneus. Molecules that regulate molecule synthesis, cell cycles, and cell divisions are necessary to enable venom regeneration and ensure its effectiveness in predation and food hoarding. The presence of proteins involved in stress response may be the result of shrews’ high metabolic rate and the costs of venom replenishment. Some proteins are likely to promote toxin spreading during envenomation and, due to their proteolytic action, reinforce venom toxicity. Finally, finding numerous proteins involved in immune response suggests a potential role of shrew venom gland secretions in protection against pathogens. These findings open up new perspectives for studying biological functions of molecules from shrew venom glands and extend our knowledge on the functioning of eulipotyphlan venom systems. Because the majority of existing and putative venomous mammals use oral venom systems to inject venom into target species, the methods presented here provide a promising avenue for confirming or discovering new taxa of venomous mammals.

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Biochemical and pharmacological characterization of Trimersurus malabaricus snake venom

Cited by 7 publications

References 40 publications

Venomics and Cellular Toxicity of Thai Pit Vipers (Trimeresurus macrops and T. hageni)

Venomics and Cellular Toxicity of Thai Pit Vipers (Trimeresurus macrops and T. hageni)

A new, widespread venomous mammal species: hemolytic activity of Sorex araneus venom is similar to that of Neomys fodiens venom

Proteins from shrews’ venom glands play a role in gland functioning and venom production

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