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The Diversified O-Superfamily in Californiconus californicus Presents a Conotoxin with Antimycobacterial Activity

Californiconus californicus, previously named Conus californicus, has always been considered a unique species within cone snails, because of its molecular, toxicological and morphological singularities; including the wide range of its diet, since it is capable of preying indifferently on fish, snail...

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Autores principales: Bernáldez-Sarabia, Johanna, Figueroa-Montiel, Andrea, Dueñas, Salvador, Cervantes-Luévano, Karla, Beltrán, Jesús A., Ortiz, Ernesto, Jiménez, Samanta, Possani, Lourival D., Paniagua-Solís, Jorge F., Gonzalez-Canudas, Jorge, Licea-Navarro, Alexei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6410186/
https://www.ncbi.nlm.nih.gov/pubmed/30791616
http://dx.doi.org/10.3390/toxins11020128
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author Bernáldez-Sarabia, Johanna
Figueroa-Montiel, Andrea
Dueñas, Salvador
Cervantes-Luévano, Karla
Beltrán, Jesús A.
Ortiz, Ernesto
Jiménez, Samanta
Possani, Lourival D.
Paniagua-Solís, Jorge F.
Gonzalez-Canudas, Jorge
Licea-Navarro, Alexei
author_facet Bernáldez-Sarabia, Johanna
Figueroa-Montiel, Andrea
Dueñas, Salvador
Cervantes-Luévano, Karla
Beltrán, Jesús A.
Ortiz, Ernesto
Jiménez, Samanta
Possani, Lourival D.
Paniagua-Solís, Jorge F.
Gonzalez-Canudas, Jorge
Licea-Navarro, Alexei
author_sort Bernáldez-Sarabia, Johanna
collection PubMed
description Californiconus californicus, previously named Conus californicus, has always been considered a unique species within cone snails, because of its molecular, toxicological and morphological singularities; including the wide range of its diet, since it is capable of preying indifferently on fish, snails, octopus, shrimps, and worms. We report here a new cysteine pattern conotoxin assigned to the O1-superfamily capable of inhibiting the growth of Mycobacterium tuberculosis (Mtb). The conotoxin was tested on a pathogen reference strain (H37Rv) and multidrug-resistant strains, having an inhibition effect on growth with a minimal inhibitory concentration (MIC) range of 3.52–0.22 μM, similar concentrations to drugs used in clinics. The peptide was purified from the venom using reverse phase high-performance liquid chromatography (RP-HPLC), a partial sequence was constructed by Edman degradation, completed by RACE and confirmed with venom gland transcriptome. The 32-mer peptide containing eight cysteine residues was named O1_cal29b, according to the current nomenclature for this type of molecule. Moreover, transcriptomic analysis of O-superfamily toxins present in the venom gland of the snail allowed us to assign several signal peptides to O2 and O3 superfamilies not described before in C. californicus, with new conotoxins frameworks.
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spelling pubmed-64101862019-04-01 The Diversified O-Superfamily in Californiconus californicus Presents a Conotoxin with Antimycobacterial Activity Bernáldez-Sarabia, Johanna Figueroa-Montiel, Andrea Dueñas, Salvador Cervantes-Luévano, Karla Beltrán, Jesús A. Ortiz, Ernesto Jiménez, Samanta Possani, Lourival D. Paniagua-Solís, Jorge F. Gonzalez-Canudas, Jorge Licea-Navarro, Alexei Toxins (Basel) Article Californiconus californicus, previously named Conus californicus, has always been considered a unique species within cone snails, because of its molecular, toxicological and morphological singularities; including the wide range of its diet, since it is capable of preying indifferently on fish, snails, octopus, shrimps, and worms. We report here a new cysteine pattern conotoxin assigned to the O1-superfamily capable of inhibiting the growth of Mycobacterium tuberculosis (Mtb). The conotoxin was tested on a pathogen reference strain (H37Rv) and multidrug-resistant strains, having an inhibition effect on growth with a minimal inhibitory concentration (MIC) range of 3.52–0.22 μM, similar concentrations to drugs used in clinics. The peptide was purified from the venom using reverse phase high-performance liquid chromatography (RP-HPLC), a partial sequence was constructed by Edman degradation, completed by RACE and confirmed with venom gland transcriptome. The 32-mer peptide containing eight cysteine residues was named O1_cal29b, according to the current nomenclature for this type of molecule. Moreover, transcriptomic analysis of O-superfamily toxins present in the venom gland of the snail allowed us to assign several signal peptides to O2 and O3 superfamilies not described before in C. californicus, with new conotoxins frameworks. MDPI 2019-02-20 /pmc/articles/PMC6410186/ /pubmed/30791616 http://dx.doi.org/10.3390/toxins11020128 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Bernáldez-Sarabia, Johanna
Figueroa-Montiel, Andrea
Dueñas, Salvador
Cervantes-Luévano, Karla
Beltrán, Jesús A.
Ortiz, Ernesto
Jiménez, Samanta
Possani, Lourival D.
Paniagua-Solís, Jorge F.
Gonzalez-Canudas, Jorge
Licea-Navarro, Alexei
The Diversified O-Superfamily in Californiconus californicus Presents a Conotoxin with Antimycobacterial Activity
title The Diversified O-Superfamily in Californiconus californicus Presents a Conotoxin with Antimycobacterial Activity
title_full The Diversified O-Superfamily in Californiconus californicus Presents a Conotoxin with Antimycobacterial Activity
title_fullStr The Diversified O-Superfamily in Californiconus californicus Presents a Conotoxin with Antimycobacterial Activity
title_full_unstemmed The Diversified O-Superfamily in Californiconus californicus Presents a Conotoxin with Antimycobacterial Activity
title_short The Diversified O-Superfamily in Californiconus californicus Presents a Conotoxin with Antimycobacterial Activity
title_sort diversified o-superfamily in californiconus californicus presents a conotoxin with antimycobacterial activity
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6410186/
https://www.ncbi.nlm.nih.gov/pubmed/30791616
http://dx.doi.org/10.3390/toxins11020128
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