Comparative analysis of prothrombin activators from the venom of Australian elapids

Pierre, LS, Masci, PP, Filippovich, I, Sorokina, N, Marsh, N, Miller, DJ and Lavin, MF (2005) Comparative analysis of prothrombin activators from the venom of Australian elapids. Molecular Biology And Evolution, 22 9: 1853-1864. doi:10.1093/molbev/msi181


Author Pierre, LS
Masci, PP
Filippovich, I
Sorokina, N
Marsh, N
Miller, DJ
Lavin, MF
Title Comparative analysis of prothrombin activators from the venom of Australian elapids
Journal name Molecular Biology And Evolution   Check publisher's open access policy
ISSN 0737-4038
Publication date 2005-01-01
Sub-type Article (original research)
DOI 10.1093/molbev/msi181
Volume 22
Issue 9
Start page 1853
End page 1864
Total pages 12
Editor W. Martin
Place of publication USA
Publisher Oxford University Press
Collection year 2005
Language eng
Subject C1
321206 Preventive Medicine
730220 Injury control
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, characterization, 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 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.
Keyword Biochemistry & Molecular Biology
Evolutionary Biology
Genetics & Heredity
Prothrombin Activator
Factor X
Factor V
Snake Venom
Gene Cloning
Oxyuranus Scutellatus
Coagulation-factor-xa
Pseudonaja-textilis Venom
Snake-venom
Pseutarin-c
Brown Snake
Factor-va
Structural Similarity
Tropidechis-carinatus
Blood
Complex
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
2006 Higher Education Research Data Collection
School of Medicine Publications
 
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Created: Wed, 15 Aug 2007, 17:47:20 EST