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An O-conotoxin from the vermivorous Conus spurius active on mice and mollusks

by: Karen S. Luna-Ramírez, Manuel B. Aguilar, Andrés Falcón, Edgar P. Heimer de la Cotera, Baldomero M. Olivera, María Maillo
Peptides, Vol. 28, No. 1. (January 2007), pp. 24-30, doi:10.1016/j.peptides.2006.08.025  Key: citeulike:11903004

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Abstract

Here, we report the purification, amino acid sequence and a preliminary biological characterization of a peptide, sr7a, from the venom of Conus spurius, a vermivorous species collected in the Yucatan Channel, Mexico. The peptide consists of 32 amino acid residues (CLQFGSTCFLGDDDICCSGECFYSGGTFGICS&; &, amidated C-terminus) and contains six cysteines arranged in the pattern (C–C–CC–C–C) that characterizes the O-superfamily of conotoxins. This superfamily includes several pharmacological families (Ï-, κ-, μO-, δ- and γ-conotoxins) that target Ca2+, K+, Na+ and pacemaker voltage-gated ion channels. Compared with other O-conotoxins that were purified from venoms, this peptide displays sequence similarity with Ï-SVIA (from Conus striatus), δ-TxVIA/B (from Conus textile), Ï-CVID (from Conus catus) and κ-PVIIA (from Conus purpurascens). At a dose of 250 pmol, peptide sr7a elicited hyperactivity when injected intracranially into mice and produced paralysis when injected into the pedal muscle of freshwater snails, Pomacea paludosa, but it had no apparent effect after intramuscular injection into the limpet Patella opea or the freshwater fish Lebistes reticulatus.


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