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Toxins 2016, 8(2), 39; doi:10.3390/toxins8020039

A New Member of Gamma-Conotoxin Family Isolated from Conus princeps Displays a Novel Molecular Target

1
Departamento de Innovación Biomédica, CICESE, Carretera Ensenada-Tijuana 3918, Ensenada, Baja California, C.P. 22860, Mexico
2
Laboratorio de Espectrometría de Masas, Departamento de Proteómica, Centro de Ingeniería Genética y Biotecnología, Avenida 31 e/158 y 190, Cubanacán, Playa, PO Box 6162. C.P. 10600, La Habana, Cuba
3
Instituto de Fisiología, Benemerita Universidad de Puebla, 14 sur 6301, CU, San Manuel, Puebla, Pue, C.P. 72570, Mexico
4
Laboratorio de Neurofarmacología Marina, Departamento de Neurobiología Celular y Molecular, UNAM, Juriquilla, Queretaro, C.P. 76230, Mexico
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Luis M. Botana
Received: 3 November 2015 / Revised: 22 January 2016 / Accepted: 25 January 2016 / Published: 5 February 2016
(This article belongs to the Collection Marine and Freshwater Toxins)
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Abstract

A novel conotoxin, named as PiVIIA, was isolated from the venom of Conus princeps, a marine predatory cone snail collected in the Pacific Southern Coast of Mexico. Chymotryptic digest of the S-alkylated peptide in combination with liquid chromatography coupled to tandem mass spectrometry, were used to define the sequencing of this peptide. Eleven N-terminal amino acids were verified by automated Edman degradation. PiVIIA is a 25-mer peptide (CDAOTHYCTNYWγCCSGYCγHSHCW) with six cysteine residues forming three disulphide bonds, a hydroxyproline (O) and two gamma carboxyglutamic acid (γ) residues. Based on the arrangement of six Cys residues (C-C-CC-C-C), this conotoxin might belong to the O2-superfamily. Moreover, PiVIIA has a conserved motif (-γCCS-) that characterizes γ-conotoxins from molluscivorous Conus. Peptide PiVIIA has 45% sequence identity with γ-PnVIIA—the prototype of this family. Biological activity of PiVIIA was assessed by voltage-clamp recording in rat dorsal root ganglion neurons. Perfusion of PiVIIA in the µM range produces a significant increase in the Ca2+ currents, without significantly modifying the Na+, K+ or proton-gated acid sensing ionic currents. These results indicate that PiVIIA is a new conotoxin whose activity deserves further studies to define its potential use as a positive modulator of neuronal activity. View Full-Text
Keywords: Conus princeps; calcium channel; gamma-conotoxin; mass spectrometry; dorsal root ganglion neurons Conus princeps; calcium channel; gamma-conotoxin; mass spectrometry; dorsal root ganglion neurons
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Bernáldez, J.; Jiménez, S.; González, L.J.; Ferro, J.N.; Soto, E.; Salceda, E.; Chávez, D.; Aguilar, M.B.; Licea-Navarro, A. A New Member of Gamma-Conotoxin Family Isolated from Conus princeps Displays a Novel Molecular Target. Toxins 2016, 8, 39.

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