A novel fibrinolytic metalloproteinase, barnettlysin-I from Bothrops barnetti (barnett´s pitviper) snake venom with anti-platelet properties

Sanchez, Eládio Flores; Richardson, Michael; Gremski, Luiza Helena; Veiga, Sílvio Sanches; Yarlequé, Armando; Niland, Stephan; Lima, Augusto Martins; Estevão-Costa, Maria Inácia; Eble, Johannes A.

doi:10.1016/j.bbagen.2015.12.021

Cited by 29 publications

(35 citation statements)

References 51 publications

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“…Thus, acurhagin exhibits its function mainly through its binding to GPVI and collagen, instead of binding to α 2 β 1 , or cleaving platelet membrane glycoproteins [104]. Recently, a P-I SVMP from Bothrops barnetti venom that inhibits platelet aggregation induced by vWF plus ristocetin and collagen was characterized [107]. It presumably cleaves both vWF and GPIb and thus, inhibits vWF-induced platelet aggregation.…”

Section: Platelet Aggregation Antagonistsmentioning

confidence: 99%

“…It presumably cleaves both vWF and GPIb and thus, inhibits vWF-induced platelet aggregation. It also cleaves the collagen-binding α 2 A domain of α 2 β 1 integrin and thus, inhibits collagen-induced platelet aggregation [107]. Despite the missing D and C domains, this P-I SVMP has similar properties compared jararhagin, a P-III SVMP.…”

Section: Platelet Aggregation Antagonistsmentioning

confidence: 99%

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Metalloproteases Affecting Blood Coagulation, Fibrinolysis and Platelet Aggregation from Snake Venoms: Definition and Nomenclature of Interaction Sites

Kini

Koh

2016

Toxins

131

123

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Snake venom metalloproteases, in addition to their contribution to the digestion of the prey, affect various physiological functions by cleaving specific proteins. They exhibit their activities through activation of zymogens of coagulation factors, and precursors of integrins or receptors. Based on their structure–function relationships and mechanism of action, we have defined classification and nomenclature of functional sites of proteases. These metalloproteases are useful as research tools and in diagnosis and treatment of various thrombotic and hemostatic conditions. They also contribute to our understanding of molecular details in the activation of specific factors involved in coagulation, platelet aggregation and matrix biology. This review provides a ready reference for metalloproteases that interfere in blood coagulation, fibrinolysis and platelet aggregation.

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Section: Platelet Aggregation Antagonistsmentioning

confidence: 99%

Section: Platelet Aggregation Antagonistsmentioning

confidence: 99%

Metalloproteases Affecting Blood Coagulation, Fibrinolysis and Platelet Aggregation from Snake Venoms: Definition and Nomenclature of Interaction Sites

Kini

Koh

2016

Toxins

131

123

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“…Sanchez et al . [19] reported BarI, isolated from the venom of Bothrops barnetti found to dissolves fibrin clots made either from purified fibrinogen or from whole blood. In H. anatolicm maximum inhibitory activity was found to be in range of 33-35.8% in different fractions.…”

Section: Discussionmentioning

confidence: 99%

Inhibition of bovine platelets aggregation in response to Hyalomma anatolicum salivary gland proteins/peptides

Surbhi

Sangwan

et al. 2016

Vet World

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Aim:Ticks are obligate ectoparasites that have an impact on wide range of vertebrates and also act as a potential vector for the transmission of tropical theileriosis, babesiosis, etc., causing significant loss to livestock production worldwide. While feeding, they introduce their saliva containing different bioactive molecules into the host. These molecules have the capability to counteract the host hemostatic mechanism to suck host blood successfully. Therefore, the study was aimed to isolate anti-platelet aggregating peptides from salivary gland extract (SGE) of Hyalomma anatolicum ticks, a commonly available tick in India.Materials and Methods:Female H. anatolicum salivary glands were dissected out and SGE was prepared by homogenizing it in a suitable buffer under ice. Extract so obtained was fractionated by gel filtration chromatography using Sephacryl S-200 column. Total protein concentration in fractions was estimated and bovine platelets were isolated, stimulated with thrombin (positive control), treated with Gly-Pro-Arg-Pro amide (negative control) and with salivary gland fractions for identification of proteins/peptides having anti-platelet aggregating activities.Results:Proteins/peptides present in various salivary gland fractions inhibited the bovine platelet aggregation and the percent inhibition ranged between 33% and 35.8%.Conclusion:The results suggests that the fractions of H. anatolicum salivary glands possess thrombin-induced anti-platelet aggregating activity and which could be further exploited for raising anti-tick vaccine and also for therapeutic purpose.

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“…jararacussu (Marcussi et al, 2007), atroxlysin-I from B. atrox (Sanchez et al, 2010), BmooMPα-II from B. moojeni (Queiroz et al, 2014), and barnettlysin-I (Bar-I) from B. barnetti (Sanchez et al, 2016). The enzymatic activity of these PI SVMPs is critical for significant inhibition of platelet function.…”

Section: Accepted Manuscriptmentioning

confidence: 98%

The role of platelets in hemostasis and the effects of snake venom toxins on platelet function

Queiroz

Sousa

Pereira

et al. 2017

Toxicon

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A novel fibrinolytic metalloproteinase, barnettlysin-I from Bothrops barnetti (barnett´s pitviper) snake venom with anti-platelet properties

Abstract: This study provides new opportunities for drug development of a fibrinolytic agent with antithrombotic effect.

Cited by 29 publications

References 51 publications

Metalloproteases Affecting Blood Coagulation, Fibrinolysis and Platelet Aggregation from Snake Venoms: Definition and Nomenclature of Interaction Sites

Metalloproteases Affecting Blood Coagulation, Fibrinolysis and Platelet Aggregation from Snake Venoms: Definition and Nomenclature of Interaction Sites

Inhibition of bovine platelets aggregation in response to Hyalomma anatolicum salivary gland proteins/peptides

The role of platelets in hemostasis and the effects of snake venom toxins on platelet function

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