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Recombinant snake venom prothrombin activators.

¹AstraZeneca R&D Bioscience, Mölndal, Sweden. ann.lovgren@astrazeneca.com

|November 1, 2012

Summary

Recombinant snake venom proteins, trocarin and oscutarin, were studied for their ability to activate prothrombin. Unlike ecarin, these proteins require cofactors, similar to human Factor X, for efficient thrombin generation.

Keywords:

FX coagulation Factor X prothrombin activator recombinant ecarin recombinant oscutarin recombinant trocarin thrombin

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Area of Science:

Biochemistry
Molecular Biology
Venom Research

Background:

Prothrombin activators are crucial for thrombin generation in the coagulation cascade.
Ecarin, a prothrombin activator from Echis carinatus venom, efficiently generates thrombin but lacks specificity.
Understanding the mechanisms of other snake venom prothrombin activators is important for biochemical research.

Purpose of the Study:

To express and characterize recombinant prothrombin activators from snake venom, specifically trocarin and oscutarin.
To investigate the cofactor requirements for thrombin generation by recombinant trocarin and oscutarin.
To elucidate the structural and functional similarities between oscutarin and human coagulation Factor X (FX).

Main Methods:

Recombinant expression of prothrombin activators in mammalian cells.
Assays to measure thrombin generation with and without cofactors.
Protein sequencing and genomic analysis to determine structural similarities.

Main Results:

Recombinant ecarin efficiently generates thrombin independently of cofactors.
Recombinant trocarin and oscutarin require additional protein cofactors for efficient thrombin generation.
Trocarin and oscutarin exhibit functional and structural similarities to human coagulation Factor X (FX).
Genomic sequencing confirmed the similarity of oscutarin to human FX.

Conclusions:

Trocarin and oscutarin function as prothrombin activators but require cofactors, unlike ecarin.
The cofactor dependency of trocarin and oscutarin is attributed to their similarity to human Factor X.
These findings contribute to the understanding of snake venom biochemistry and coagulation factor function.