Target intelligence / Profile preview

Echis ocellatus snake venom metalloproteinase (EoSVMP)

Target
EoSVMP
Molecular classification
Enzyme, Zinc-dependent metalloproteinase, Reprolysin family (M12B), Metalloendopeptidase
01

Overview

Echis ocellatus snake venom metalloproteinases (EoSVMPs) are a diverse group of zinc-dependent enzymes that serve as the primary drivers of morbidity and mortality following envenomation by the West African carpet viper (Echis ocellatus) (Wagstaff et al., 2009, Gene). These enzymes are categorized into P-I, P-II, and P-III classes based on their domain architecture, which includes a catalytic metalloproteinase domain and, in larger classes, disintegrin-like and cysteine-rich domains (Casewell et al., 2011, Toxicon). Their primary biological function involves the rapid degradation of extracellular matrix (ECM) components, particularly the basement membrane of vascular endothelial cells, leading to localized and systemic hemorrhage (Gutiérrez et al., 2016, Toxins). Additionally, certain EoSVMPs act as potent prothrombin activators, contributing to venom-induced consumption coagulopathy (VICC) (Howes et al., 2005, Thrombosis and Haemostasis). In a therapeutic context, EoSVMPs are the primary targets for polyvalent and monovalent antivenoms, and they are increasingly being targeted by small-molecule matrix metalloproteinase inhibitors (MMPIs) like batimastat and marimastat to provide rapid, field-deployable treatment (Albulescu et al., 2020, Journal of Medicinal Chemistry). The development of these inhibitors represents a shift toward oral or heat-stable therapies that can be administered immediately after a bite, potentially bridging the gap between envenomation and hospital-based antivenom treatment (Ainsworth et al., 2018, Communications Biology).

Other names
West African carpet viper venom metalloproteinasesEchis ocellatus SVMPsReprolysin-type metalloproteinasesEcarin-like prothrombin activatorsEchiarin
02

Mechanism of action

Inhibition of the zinc-dependent catalytic site through chelation of the essential zinc ion or antibody-mediated neutralization of the enzyme surface, preventing the degradation of basement membrane proteins and the activation of pro-coagulant factors (Albulescu et al., 2020, Journal of Medicinal Chemistry; Gutiérrez et al., 2017, Nature Reviews Disease Primers).

03

Biological functions

ProteolysisExtracellular matrix degradationProthrombin activationHemorrhage inductionFibrinogenolysisPlatelet aggregation inhibition
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Disease associations

Snakebite envenomationHemorrhageCoagulopathyTissue necrosisHypovolemic shock
05

Safety considerations

Rapid progression of systemic hemorrhageVenom-induced consumption coagulopathy (VICC)Local tissue necrosis and permanent disabilityAntivenom-related hypersensitivity reactionsPotential off-target effects on human matrix metalloproteinases by small-molecule inhibitors
06

Interacting drugs

Batimastat

6 more in the full profile.

07

Biomarkers

Prothrombin time (PT)International Normalized Ratio (INR)Fibrinogen concentrationD-dimer levelsWhole blood clotting time (WBCT20)

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