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αD-Conotoxins in Species of the Eastern Pacific: The Case of Conus princeps from Mexico

1
Laboratorio de Neurofarmacología Marina, Departamento de Neurobiología Celular y Molecular, Instituto de Neurobiología, Universidad Nacional Autónoma de México, Juriquilla, Querétaro 76230, Mexico
2
Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca, Morelos 62210, Mexico
3
Laboratorio Universitario de Proteómica, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca, Morelos 62210, Mexico
4
Departamento de Estudios para el Desarrollo Sustentable de Zonas Costeras, CUCSUR-Universidad de Guadalajara, San Patricio-Melaque, Jalisco 48980, Mexico
5
Laboratorio de Toxinología Marina, Unidad Académica de Ecología y Biodiversidad Acuática, Instituto de Ciencias del Mar y Limnología, Universidad Nacional Autónoma de México, Ciudad de México 04510, Mexico
6
Unidad de Proteogenómica, Instituto de Neurobiología, Universidad Nacional Autónoma de México, Juriquilla, Querétaro 76230, Mexico
*
Author to whom correspondence should be addressed.
Toxins 2019, 11(7), 405; https://doi.org/10.3390/toxins11070405
Received: 12 June 2019 / Revised: 9 July 2019 / Accepted: 10 July 2019 / Published: 12 July 2019
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Abstract

Conus snails produce venoms containing numerous peptides such as the α-conotoxins (α-CTXs), which are well-known nicotinic acetylcholine receptor (nAChR) antagonists. Thirty-eight chromatographic fractions from Conus princeps venom extract were isolated by RP-HPLC. The biological activities of 37 fractions (0.07 µg/µL) were assayed by two-electrode voltage clamp on human α7 nAChRs expressed in Xenopus laevis oocytes. Fractions F7 and F16 notably inhibited the response elicited by acetylcholine by 52.7 ± 15.2% and 59.6 ± 2.5%, respectively. Fraction F7 was purified, and an active peptide (F7-3) was isolated. Using a combination of Edman degradation, mass spectrometry, and RNASeq, we determined the sequence of peptide F7-3: AVKKTCIRSTOGSNWGRCCLTKMCHTLCCARSDCTCVYRSGKGHGCSCTS, with one hydroxyproline (O) and a free C-terminus. The average mass of this peptide, 10,735.54 Da, indicates that it is a homodimer of identical subunits, with 10 disulfide bonds in total. This peptide is clearly similar to αD-CTXs from species of the Indo-Pacific. Therefore, we called it αD-PiXXA. This toxin slowly and reversibly inhibited the ACh-induced response of the hα7 nAChR subtype, with an IC50 of 6.2 μM, and it does not affect the hα3β2 subtype at 6.5 μM. View Full-Text
Keywords: Cone snail; Conus princeps; αD-conotoxin; nAChR; hα7 nAChR; hα3β2 nAChR Cone snail; Conus princeps; αD-conotoxin; nAChR; hα7 nAChR; hα3β2 nAChR
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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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Hernández-Sámano, A.C.; Falcón, A.; Zamudio, F.; Batista, C.V.; Michel-Morfín, J.E.; Landa-Jaime, V.; López-Vera, E.; Jeziorski, M.C.; Aguilar, M.B. αD-Conotoxins in Species of the Eastern Pacific: The Case of Conus princeps from Mexico. Toxins 2019, 11, 405.

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