Snake venom

About: Snake venom is a research topic. Over the lifetime, 3138 publications have been published within this topic receiving 86729 citations. The topic is also known as: snake venoms.

Phospholipase A2 enzymes: physical structure, biological function, disease implication, chemical inhibition, and therapeutic intervention.

Abstract: 1.1. Discovery of the Phospholipase A2 Superfamily Phospholipases represent one of the earliest enzyme activities to be identified and studied and the phospholipase A2 (PLA2) superfamily (see defining specificity1 in Figure 1) traces its roots to the identification of lytic actions of snake venom at the end of the 19th century. The enzyme was first purified and characterized from cobra venom and later from rattlesnake venom. As protein sequencing methodologies advanced in the 1970’s, it became apparent that these enzymes had an unusually large number of cysteines (over 10% of the amino acids) and as secreted enzymes, that they were all in the form of disulfide bonds. It was further recognized that in the case of PLA2, cobras and rattlesnakes had six disulfides in common, but one disulfide bond is located in distinctly different locations. This led to the designation of Type 1 and Type 2 for cobras (old world snakes) and rattlesnakes (new world snakes), respectively.2 During that same period, studies on the porcine pancreatic digestive enzyme that hydrolyzes phospholipids led to the determination that this mammalian enzyme (and also the human pancreatic enzyme) had the same disulfide bonding pattern as cobras and hence the designation as IB with the cobra enzyme as IA. Open in a separate window Figure 1 The specific reaction catalyzed by phospholipase A2 at the sn-2 position of the glycerol backbone is shown. X, any of a number of polar headgroups; R1, fatty acids, or alkyl, or alkenyl groups and R2, fatty acids or acyl moieties.

Diet and snake venom evolution

Abstract: Venom composition within snake species can show considerable geographical variation, an important consideration because bites by conspecific populations may differ in symptomatology and require different treatments. The underlying causes of this phenomenon have never been explained. Here we present evidence that the variation in the venom of the pitviper Calloselasma rhodostoma (Serpentes: Viperidae) is closely associated with its diet. We also evaluated other possible causes of geographic variation in venom using partial Mantel tests and independent contrasts, but rejected both contemporary gene flow (estimated from geographical proximity) and the phylogenetic relationships (assessed by analysis of mitochondrial DNA) among populations as important influences upon venom evolution. As the primary function of viperid venom is to immobilize and digest prey and prey animals vary in their susceptibility to venom, we suggest that geographical variation in venom composition reflects natural selection for feeding on local prey.

Use of a Snake Venom Toxin to Characterize the Cholinergic Receptor Protein

Abstract: α-Bungarotoxin, a polypeptide of mol wt 8000 purified from the venom of Bungarus multicinctus, blocks irreversibly and specifically the excitation by cholinergic agonists on the isolated electroplax and on purified membrane fragments in vitro. The toxin also blocks the in vitro binding of decamethonium to a protein recently isolated from electric tissue. This observation strengthens our earlier conclusion that this protein is the cholinergic receptor macromolecule.