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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...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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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. |
format | Online Article Text |
id | pubmed-6410186 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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