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Phylogenetic analysis of serine proteases from Russell’s viper (Daboia russelli siamensis) and Agkistrodon piscivorus leucostoma venom |
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| Authors: | Pattadon SukkapanYing Jia,Issarang Nuchprayoon,John C. Pé rez |
| Affiliation: | a Snake Bite and Venom Research Unit, Chula Medical Research Center, Faculty of Medicine, Chulalongkorn University, Rama IV Road, Patumwan district, Bangkok 10330, Thailand b National Natural Toxins Research Center, College of Arts and Sciences, Texas A & M University-Kingsville, Kingsville, TX 78363, USA c Department of Pediatrics, Faculty of Medicine, Chulalongkorn University, Rama IV Road, Patumwan district, Bangkok 10330, Thailand |
| 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. |
| Keywords: | Russell&rsquo s viper Agkistrodon piscivorus leucostoma Snake venom serine protease RT-PCR cDNA |
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