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Phylogenetic analysis of serine proteases from Russell’s viper (Daboia russelli siamensis) and Agkistrodon piscivorus leucostoma venom
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...
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Published in: | Toxicon (Oxford) 2011-08, Vol.58 (2), p.168-178 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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.
► cDNAs of venom serine proteases from D. r. siamensis and A. p. leucostoma were cloned. ► The amino acid sequences of the cDNAs were analyzed by multiple sequence alignment. ► Phylogenetic trees were constructed to study their evolutionary relationship. ► KA/KS values suggested that accelerated evolution has occurred. |
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ISSN: | 0041-0101 1879-3150 |
DOI: | 10.1016/j.toxicon.2011.05.014 |