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

Autor: Kumkate S; Department of Biology, Faculty of Science, Mahidol University, Ratchathewi, Bangkok 10400, Thailand., Chanhome L; Snake Farm, Queen Saovabha Memorial Institute, The Thai Red Cross Society, Pathumwan, Bangkok 10330, Thailand., Thiangtrongjit T; Department of Molecular Tropical Medicine and Genetics, Faculty of Tropical Medicine, Mahidol University, Ratchathewi, Bangkok 10400, Thailand., Noiphrom J; Department of Research and Development, Queen Saovabha Memorial Institute, The Thai Red Cross Society, Pathumwan, Bangkok 10330, Thailand., Laoungboa P; Snake Farm, Queen Saovabha Memorial Institute, The Thai Red Cross Society, Pathumwan, Bangkok 10330, Thailand., Khow O; Department of Research and Development, Queen Saovabha Memorial Institute, The Thai Red Cross Society, Pathumwan, Bangkok 10330, Thailand., Vasaruchapong T; Snake Farm, Queen Saovabha Memorial Institute, The Thai Red Cross Society, Pathumwan, Bangkok 10330, Thailand., Sitprija S; Department of Biology, Faculty of Science, Mahidol University, Ratchathewi, Bangkok 10400, Thailand., Chaiyabutr N; Snake Farm, Queen Saovabha Memorial Institute, The Thai Red Cross Society, Pathumwan, Bangkok 10330, Thailand., Reamtong O; Department of Molecular Tropical Medicine and Genetics, Faculty of Tropical Medicine, Mahidol University, Ratchathewi, Bangkok 10400, Thailand.
Jazyk: angličtina
Zdroj: Toxins [Toxins (Basel)] 2020 Jan 16; Vol. 12 (1). Date of Electronic Publication: 2020 Jan 16.
DOI: 10.3390/toxins12010054
Abstrakt: 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.
Competing Interests: The authors declare no conflict of interest.
Databáze: MEDLINE
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