Target intelligence / Profile preview

Snake venom toxins from Bitis arietans, Cerastes cerastes, Cerastes deserti, Echis leucogaster, Naja nigricollis, Naja melanoleuca, and Naja haje

Molecular classification
Phospholipase A2, Snake venom metalloproteinase, Snake venom serine protease, Three-finger toxin, C-type lectin-like protein, Disintegrin, L-amino acid oxidase
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Overview

The target comprises a complex array of toxic proteins and peptides found in the venoms of seven medically significant African snake species: Bitis arietans, Cerastes cerastes, Cerastes deserti, Echis leucogaster, Naja nigricollis, Naja melanoleuca, and Naja haje [1, 2]. These venoms contain diverse molecular families, including phospholipases A2 (PLA2), snake venom metalloproteinases (SVMP), serine proteases, and three-finger toxins (3FTx), which act synergistically to incapacitate prey or cause severe pathology in humans [3]. Vipers like Bitis and Echis primarily induce hemotoxicity and tissue necrosis through enzymatic degradation of the extracellular matrix and interference with the coagulation cascade [4, 5]. Elapids such as the Naja species (cobras) are characterized by potent neurotoxicity, leading to respiratory paralysis via blockade of nicotinic acetylcholine receptors, and cytotoxicity causing local tissue destruction [6]. Therapeutic management involves the administration of polyvalent antivenoms that provide passive immunity by neutralizing these toxins [7]. Additionally, small-molecule inhibitors like Varespladib and Marimastat are being researched for their ability to inhibit specific enzymatic components like PLA2 and SVMPs, respectively, offering potential field-stable treatments [8].

Other names
African snake venomsViperidae and Elapidae venom toxinsBitis/Cerastes/Echis/Naja venom proteins
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Mechanism of action

Neutralization of toxic proteins by specific antibodies (antivenom) or competitive inhibition of enzymatic toxins such as phospholipase A2 or metalloproteinases.

03

Biological functions

ProteolysisHemolysisNeurotransmission inhibitionPlatelet aggregation modulationCoagulation cascade activationCytolysis
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Disease associations

Snakebite envenomationCoagulopathyNeuromuscular paralysisTissue necrosisHemorrhageAcute kidney injury
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Safety considerations

Anaphylaxis (Type I hypersensitivity to antivenom)Serum sickness (Type III hypersensitivity)Rapid onset of respiratory failureVenom-induced consumption coagulopathy (VICC)Irreversible tissue damage if treatment is delayed
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Interacting drugs

Polyvalent snake antivenom (e.g., Fav-Afrique, SAIMR Polyvalent)

4 more in the full profile.

07

Biomarkers

Prothrombin time (PT)International Normalized Ratio (INR)Fibrinogen levelsCreatine kinase (CK)Venom antigen levels (ELISA)Platelet count

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