Abstract
Sea anemone (Cnidaria, Anthozoa) venom is an important source of bioactive compounds used as tools to study the pharmacology and structure-function of voltage-gated K+ channels (KV). These neurotoxins can be divided into four different types, according to their structure and mode of action. In this work, for the first time, two toxins were purified from the venom of Bunodosoma caissarum population from Saint Peter and Saint Paul Archipelago, Brazil. Sequence alignment and phylogenetic analysis reveals that BcsTx1 and BcsTx2 are the newest members of the sea anemone type 1 potassium channel toxins. Their functional characterization was performed by means of a wide electrophysiological screening on 12 different subtypes of KV channels (KV1.1–KV1.6; KV2.1; KV3.1; KV4.2; KV4.3; hERG and Shaker IR). BcsTx1 shows a high affinity for rKv1.2 over rKv1.6, hKv1.3, Shaker IR and rKv1.1, while Bcstx2 potently blocked rKv1.6 over hKv1.3, rKv1.1, Shaker IR and rKv1.2. Furthermore, we also report for the first time a venom composition and biological activity comparison between two geographically distant populations of sea anemones.
Highlights
IntroductionAs the most ancient venomous animals on Earth, cnidarians (classes Anthozoa, Scyphozoa, Cubozoa and Hydrozoa) have evolved a large amount of pore-forming toxins, phospholipases A2, protease inhibitors, neurotoxins and toxic secondary metabolites [1,2,3,4,5,6]
As the most ancient venomous animals on Earth, cnidarians have evolved a large amount of pore-forming toxins, phospholipases A2, protease inhibitors, neurotoxins and toxic secondary metabolites [1,2,3,4,5,6]
We report for the first time the characterization of the ―neurotoxic fraction‖ from the venom of B. caissarum SPSPA population, and under the same experimental conditions, we compare it to the population found in the state of São Paulo littoral
Summary
As the most ancient venomous animals on Earth, cnidarians (classes Anthozoa, Scyphozoa, Cubozoa and Hydrozoa) have evolved a large amount of pore-forming toxins, phospholipases A2, protease inhibitors, neurotoxins and toxic secondary metabolites [1,2,3,4,5,6]. Sea anemones (Anthozoa, Actiniaria) are a well-known pharmacological source of a large number of neurotoxins acting upon a diverse panel of ion channels, such as voltage-gated sodium and potassium channels. Channel family, 15 subfamilies can be subdivided, according to their structure and function [14] Of these different subfamilies, the voltage-gated potassium channel (KV) subfamily represents one of them and has an essential role in repolarizing the membrane after the initiation of an action potential [15]. ―functional dyad‖ directly interacting with the channel pore These toxins were purified from the venom of sea anemones belonging to the Actiniidae, Hormathiidae, Thalassianthidae and Stichodactylidae families [13] and were exclusively characterized on mammalian KV channels, using. Cross indicates the southeast coast of Brazil (São Sebastião beach—S23°56′, W45°20′), more than 4000 km distant from the SPSPA
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