Lachesis muta C-type lectin-like hemostasis-modifying toxins (Lm-Snaclecs)

Lachesis muta C-type lectin-like hemostasis-modifying toxins, commonly known as Snaclecs, are a significant class of non-enzymatic proteins found in the venom of the South American bushmaster snake (Lachesis muta) (Siigur et al., 2010). These toxins function by binding with high specificity to various components of the human hemostatic system, including platelet receptors like glycoprotein Ib (GPIb) and glycoprotein VI (GPVI), as well as blood coagulation factors (Siigur et al., 2010; MDPI, 2012). This binding can lead to either the activation or inhibition of platelet aggregation and the disruption of the coagulation cascade, resulting in severe clinical symptoms such as systemic hemorrhage, coagulopathy, and hypotension (NIH, 2019). Some specific members, such as Mutacytin-1, have also demonstrated cardiotoxic properties, inducing heart rate alterations and thrombus formation in experimental models (Perdomo et al., 2019). In medical practice, these toxins are the primary targets for neutralization by specific or polyvalent antivenoms, which prevent the toxins from interacting with their physiological targets (NIH, 2019). Furthermore, due to their potent and selective interactions with the vascular system, they are extensively studied as lead structures for the development of new anticoagulant and antithrombotic therapeutic agents (Siigur et al., 2010).

Other names

SnaclecsC-type lectin-like proteinsCTLPsMutinaMutacytin-1Bushmaster lectinLm-CLPSnake venom C-type lectins

Antivenom antibodies bind to and neutralize the toxins, preventing their interaction with platelet receptors and coagulation factors. Simple sugars like galactose and lactose can competitively inhibit the carbohydrate-binding activity of certain members of this toxin class in vitro.