Next Article in Journal
RTX-Toxins
Previous Article in Journal
Multi Mycotoxin Determination in Dried Beef Using Liquid Chromatography Coupled with Triple Quadrupole Mass Spectrometry (LC-MS/MS)
Article

The Procoagulant Snake Venom Serine Protease Potentially Having a Dual, Blood Coagulation Factor V and X-Activating Activity

1
Department of Molecular and Biomedical Sciences, Jožef Stefan Institute, Jamova cesta 39, SI-1000 Ljubljana, Slovenia
2
Jožef Stefan International Postgraduate School, Jamova cesta 39, SI-1000 Ljubljana, Slovenia
3
Protein Science Laboratory, Department of Biological Sciences, Faculty of Science, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore
4
Department of Medicine, Yong Loo Lin School of Medicine, National University of Singapore, 1E Kent Ridge Road, Singapore 119228, Singapore
5
Division of Pediatrics, University Medical Center, Bohoričeva 20, SI-1000 Ljubljana, Slovenia
*
Author to whom correspondence should be addressed.
Toxins 2020, 12(6), 358; https://doi.org/10.3390/toxins12060358
Received: 7 April 2020 / Revised: 21 May 2020 / Accepted: 26 May 2020 / Published: 29 May 2020
(This article belongs to the Section Animal Venoms)
A procoagulant snake venom serine protease was isolated from the venom of the nose-horned viper (Vipera ammodytes ammodytes). This 34 kDa glycoprotein, termed VaaSP-VX, possesses five kDa N-linked carbohydrates. Amino acid sequencing showed VaaSP-VX to be a chymotrypsin-like serine protease. Structurally, it is highly homologous to VaaSP-6 from the same venom and to nikobin from the venom of Vipera nikolskii, neither of which have known functions. VaaSP-VX does not affect platelets. The specific proteolysis of blood coagulation factors X and V by VaaSP-VX suggests that its blood-coagulation-inducing effect is due to its ability to activate these two blood coagulation factors, which following activation, combine to form the prothrombinase complex. VaaSP-VX may thus represent the first example of a serine protease with such a dual activity, which makes it a highly suitable candidate to replace diluted Russell’s viper venom in lupus anticoagulant testing, thus achieving greater reliability of the analysis. As a blood-coagulation-promoting substance that is resistant to serpin inhibition, VaaSP-VX is also interesting from the therapeutic point of view for treating patients suffering from hemophilia. View Full-Text
Keywords: FV activator; FX activator; procoagulant; snake venom; serine protease FV activator; FX activator; procoagulant; snake venom; serine protease
Show Figures

Figure 1

MDPI and ACS Style

Latinović, Z.; Leonardi, A.; Koh, C.Y.; Kini, R.M.; Trampuš Bakija, A.; Pungerčar, J.; Križaj, I. The Procoagulant Snake Venom Serine Protease Potentially Having a Dual, Blood Coagulation Factor V and X-Activating Activity. Toxins 2020, 12, 358. https://doi.org/10.3390/toxins12060358

AMA Style

Latinović Z, Leonardi A, Koh CY, Kini RM, Trampuš Bakija A, Pungerčar J, Križaj I. The Procoagulant Snake Venom Serine Protease Potentially Having a Dual, Blood Coagulation Factor V and X-Activating Activity. Toxins. 2020; 12(6):358. https://doi.org/10.3390/toxins12060358

Chicago/Turabian Style

Latinović, Zorica, Adrijana Leonardi, Cho Y. Koh, R. M. Kini, Alenka Trampuš Bakija, Jože Pungerčar, and Igor Križaj. 2020. "The Procoagulant Snake Venom Serine Protease Potentially Having a Dual, Blood Coagulation Factor V and X-Activating Activity" Toxins 12, no. 6: 358. https://doi.org/10.3390/toxins12060358

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop