Malabarase, a serine protease with anticoagulant activity from Trimeresurus malabaricus venom

Kumar, R. Venkatesh; Manjunath, Yariswamy; Joshi, Vikram; Dharmappa, K.K.; Venkatesha, Shivaprasad H.; Sharath, B. K.; Vishwanath, Bannikuppe S.

doi:10.1016/j.cbpb.2012.11.004

Cited by 10 publications

(3 citation statements)

References 31 publications

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“…We also determined the hemorrhagic activity of the enzyme in vivo [ 28 ]. Groups of three specific pathogen free (SPF) male BALB/c mice (n = 3 per group) were injected intradermally with different concentrations of Velefibrinase (0.5 and 1.0 mg/kg) in 100 μL of isotonic saline.…”

Section: Methodsmentioning

confidence: 99%

Purification and Characterization of a Fibrinolytic Enzyme from Marine Bacillus velezensis Z01 and Assessment of Its Therapeutic Efficacy In Vivo

Zhou¹,

Chen²,

Yu³

et al. 2022

Microorganisms

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Fibrinolytic enzymes are the most effective agents for the treatment of thrombotic diseases. In the present study, we purified and characterized an extracellular fibrinolytic serine metalloprotease (named Velefibrinase) that is produced by marine Bacillus velezensis Z01 and assessed its thrombolysis in vivo. SDS-PAGE and MALDI-TOF-MS analyses showed that the molecular mass of Velefibrinase was 32.3 KDa and belonged to the peptidase S8 family. The optimal fibrinolytic activity conditions of Velefibrinase were 40 °C and pH 7.0. Moreover, Velefibrinase exhibited high substrate specificity to fibrin, and a higher ratio of fibrinolytic/caseinolytic (1.48) values, which indicated that Velefibrinase had excellent fibrinolytic properties. Based on the degradation pattern of fibrin and fibrinogen, Velefibrinase could be classified as α/β-fibrinogenase. In vitro, Velefibrinase demonstrated efficient thrombolytic ability, anti-platelet aggregation, and amelioration of blood coagulation (APTT, PT, TT, and FIB), which were superior to those of commercial anticoagulant urokinase. Velefibrinase showed no hemolysis for erythrocyte in vitro and no hemorrhagic activity in vivo. Finally, Velefibrinase effectively prevented mouse tail thrombosis in a dose-dependent (0.22–0.88 mg/kg) manner. These findings suggested that Velefibrinase has the potential to becoming a new thrombolytic agent.

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Section: Methodsmentioning

confidence: 99%

Purification and Characterization of a Fibrinolytic Enzyme from Marine Bacillus velezensis Z01 and Assessment of Its Therapeutic Efficacy In Vivo

Zhou¹,

Chen²,

Yu³

et al. 2022

Microorganisms

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“…The mild coagulopathy caused by MPV venom is primarily fibrinolytic, mediated by phosphodiesterases, metalloproteinases, and serine-protease like proteins such as malabarase. 15 Although the patient had a positive 20 minute whole blood clotting test (MWBCT), the INR was only marginally elevated and TEG showed a mildly hypocoaguable state. 16 MPV venom has potent thrombin-like enzyme (TLE).…”

Section: Discussionmentioning

confidence: 97%

A Tropical Kiss by a Malabar Pit Viper

Sirur

Lath

Chethana

et al. 2022

Wilderness & Environmental Medicine

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Snakebite in India is often attributed to the "big 4," for which polyvalent anti-snake venom is effective. Also significant and less known is the burden of other venomous snakes, one of which is Trimeresurus malabaricus. We report a bite to the face of a tree climber by Trimeresurus malabaricus in the Western Ghats of India, which caused severe local envenomation in the form of facial edema and systemic signs of envenomation, including coagulopathy and hypotension. We discuss the role of thromboelastogram, infrared thermography, and routine diagnostics in this case, which led to the administration of Indianmade polyvalent anti-snake venom. The patient recovered and was discharged without any clinically evident physiological or physical dysfunction.

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“…3 Fibrinase comes from a wide range of sources and can be obtained from animals, plants and microorganisms. Fibrinases obtained from snake venom (Fgnase, malabarase), earthworms (lumbrokinase, protein Dpf3), cockroaches and other animals, [4][5][6][7][8] as well as proteases obtained from plants such as Aster yomena (kitamase), Leucas indica (lunathrombase), potato leaves and fig latex, showed efficient fibrinolytic activity and excellent specificity. [9][10][11][12] Compared with fibrinases from plants and animals, microbial fibrinases have the advantages of low cost and easy availability.…”

Section: Introductionmentioning

confidence: 99%