New Sea Anemone Toxin RTX-VI Selectively Modulates Voltage-Gated Sodium Channels.

A new neurotoxin RTX-VI that modulates the voltage-gated sodium channels (Na_V) was isolated from the ethanolic extract of the sea anemone Heteractis crispa. Its amino acid sequence was determined using the combination of Edman degradation and tandem mass spectrometry. RTX-VI turned out to be an unusual natural analogue of the previously described sea anemone toxin RTX-III. The RTX-VI molecule consists of two disulfide-linked peptide chains and is devoid of Arg13, which is important for the selectivity and affinity of such peptides for the Na_V channels. Electrophysiological screening of RTV-VI on Na_V channel subtypes showed its selective interaction with the central nervous system (Na_V1.2, Na_V1.6) and insect (BgNa_V1, VdNa_V1) sodium channels. [ABSTRACT FROM AUTHOR]