Toxins (Jan 2020)

Venomics and Cellular Toxicity of Thai Pit Vipers (<i>Trimeresurus macrops</i> and <i>T. hageni</i>)

  • Supeecha Kumkate,
  • Lawan Chanhome,
  • Tipparat Thiangtrongjit,
  • Jureeporn Noiphrom,
  • Panithi Laoungboa,
  • Orawan Khow,
  • Taksa Vasaruchapong,
  • Siravit Sitprija,
  • Narongsak Chaiyabutr,
  • Onrapak Reamtong

DOI
https://doi.org/10.3390/toxins12010054
Journal volume & issue
Vol. 12, no. 1
p. 54

Abstract

Read online

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.

Keywords