Functional implications of the unique disulfide bond in venom factor V from the Australian common brown snake Pseudonaja textilis

Verhoef, D.; Yang, X.X.; Parthasarathy, S.; Reitsma, P.H.; Camire, R.M.; Bos, M.H.A. (2014)

Article / Letter to editor

The venom of the Australian brown snake Pseudonaja textilis contains a prothrombinase-like initiator of blood coagulation, which has evolved into a potent weapon through several gainof-function adaptations. Here we examined the functional implications of a disulfide bond exclusively found in the factor (F)Va-like cofactor component, ptFV. We found that this remarkable structural feature is not required for the procoagulant properties of ptFV. The nearly identical liver-derived plasma ptFV that lacks this disulfide link displayed a similar procoagulant profile. Whether the unique disulfide bond imposes conformational constraints essential to other aspects of the venom FV life cycle remains to be determined.

• Coagulation
• factor V
• hemostasis
• prothrombin activation
• pseudonaja textilis
• snake venom

• All authors: Verhoef, D.; Yang, X.X.; Parthasarathy, S.; Reitsma, P.H.; Camire, R.M.; Bos, M.H.A.
• Date: 2014-06-30
• Journal: Toxin Reviews
• Volume: 33
• Issue: 1-2
• Pages: 1 - 5
• DOI: doi:10.3109/15569543.2013.844712