Phylogenetic analysis of serine proteases from Russell's viper (Daboia russelli siamensis) and Agkistrodon piscivorus leucostoma venom

Authors

Pattadon Sukkapan
Ying Jia, The University of Texas Rio Grande ValleyFollow
Issarang Nuchprayoon
John C. Pérez

Document Type

Article

Publication Date

8-2011

Abstract

Serine proteases are widely found in snake venoms. They have variety of functions including contributions to hemostasis. In this study, five serine proteases were cloned and characterized from two different cDNA libraries: factor V activator (RVV-V), alpha fibrinogenase (RVAF) and beta fibrinogenase (RVBF) from Russell's viper (Daboia russelli siamensis), and plasminogen activator (APL-PA) and protein C activator (APL-C) from Agkistrodon piscivorus leucostoma. The snake venom serine proteases were clustered in phylogenetic tree according to their functions. KA/KS values suggested that accelerated evolution has occurred in the mature protein coding regions in cDNAs of snake venom serine proteases.

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Recommended Citation

Sukkapan, P., Jia, Y., Nuchprayoon, I., & Pérez, J. C. (2011). Phylogenetic analysis of serine proteases from Russell's viper (Daboia russelli siamensis) and Agkistrodon piscivorus leucostoma venom. Toxicon : official journal of the International Society on Toxinology, 58(2), 168–178. https://doi.org/10.1016/j.toxicon.2011.05.014

Publication Title

Toxicon

DOI

10.1016/j.toxicon.2011.05.014