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MBE Advance Access published online on June 1, 2005
Molecular Biology and Evolution, doi:10.1093/molbev/msi181
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© The Author 2005. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution. All rights reserved. For permissions, please e-mail: journals.permissions@oupjournals.org
Accepted May 23, 2005

Research Article

Comparative Analysis of Prothrombin activators from the Venom of Australian elapids

Liam St Pierre 1, Paul P Masci 2, Igor Filippovich 3, Natasha Sorokina 3, Neville Marsh 4, David J Miller 5, and Martin F Lavin 6*

1 The Queensland Institute of Medical Research, Royal Brisbane Hospital, Brisbane, Australia; School of Life Sciences, Queensland University of Technology, Brisbane, Australia
2 Southern Clinical Division, Faculty of Health Sciences, University of Queensland, Brisbane, Australia
3 The Queensland Institute of Medical Research, Royal Brisbane Hospital, Brisbane, Australia
4 School of Life Sciences, Queensland University of Technology, Brisbane, Australia
5 Comparative Genomics Centre, James Cook University, Townsville, Australia
6 The Queensland Institute of Medical Research, Royal Brisbane Hospital, Brisbane, Australia; Southern Clinical Division, Faculty of Health Sciences, University of Queensland, Brisbane, Australia

* To whom correspondence should be addressed.
Martin F Lavin, E-mail: martinL{at}qimr.edu.au


  Abstract

A key component of the venom of many Australian snakes belonging to the elapid family is a toxin that is structurally and functionally similar to that of the mammalian prothrombinase complex. In mammals this complex is responsible for the cleavage of prothrombin to thrombin and is composed of factor Xa in association with its cofactors calcium, phospholipids and factor Va. The snake prothrombin activators have been classified on the basis of their requirement for cofactors for activity. The two major subgroups described in Australian elapid snakes, groups C and D, are differentiated by their requirement for mammalian coagulation Factor Va. In this study we describe the cloning, characterisation and comparative analysis of the factor X- and factor V-like components of the prothrombin activators from the venom glands of snakes possessing either group C or group D prothrombin activators. The overall domain arrangement in these proteins was highly conserved between all elapids, and with the corresponding mammalian clotting factors. The deduced protein sequence for the factor X-like protease precursor, identified in elapids containing either group C or D prothrombin activators, demonstrated a remarkable degree of relatedness to each other (80-97%). The factor V-like component of the prothrombin activator, present only in snakes containing group C complexes, also showed a very high degree of homology (96-98%). Expression of both the factor X- and factor V-like proteins determined by immunoblotting provided an additional means of separating these two groups at the molecular level. The molecular phylogenetic analysis described here represents a new approach for distinguishing group C and D snake prothrombin activators and correlates well with previous classifications.

Keywords: Prothrombin activator; Factor X; Factor V; snake venom; gene cloning; Oxyuranus scutellatus.
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