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Identification of New Ocellatin Antimicrobial Peptides by cDNA Precursor Cloning in the Frame of This Family of Intriguing Peptides
Ocellatins are a family of antimicrobial peptides found exclusively in the Leptodactylus genus. To date, 10 species have been studied and more than 23 peptides described. Here we report the sequences of five new peptides from the skin of the frog Leptodactylus latrans (Anura: Leptodactylidae) determ...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7693824/ https://www.ncbi.nlm.nih.gov/pubmed/33138046 http://dx.doi.org/10.3390/antibiotics9110751 |
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author | Marani, Mariela M. Aguilar, Silvana Cuzziol Boccioni, Ana P. Cancelarich, Natalia L. Basso, Néstor G. Albericio, Fernando |
author_facet | Marani, Mariela M. Aguilar, Silvana Cuzziol Boccioni, Ana P. Cancelarich, Natalia L. Basso, Néstor G. Albericio, Fernando |
author_sort | Marani, Mariela M. |
collection | PubMed |
description | Ocellatins are a family of antimicrobial peptides found exclusively in the Leptodactylus genus. To date, 10 species have been studied and more than 23 peptides described. Here we report the sequences of five new peptides from the skin of the frog Leptodactylus latrans (Anura: Leptodactylidae) determined by cDNA cloning of the complete prepro-peptide structures. The mature peptides were characterized with in silico tools and compared with those previously described. With 21 amino acid residues, this new set of peptides not previously described in the Leptodactylus genus share between 100 and 76.2% similarity to ocellatin antimicrobial peptides. These novel peptides are cationic and their three-dimensional (3D) structure holds the highly conserved residues G(1), D(4), K(7), and K(11) and a high theoretical amphipathic α-helix content. Furthermore, in silico analyses of these new peptides predicted antimicrobial activity. This study is framed in the context of previous work published about ocellatins, and therefore, provides a review of this intriguing family of peptides. |
format | Online Article Text |
id | pubmed-7693824 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-76938242020-11-28 Identification of New Ocellatin Antimicrobial Peptides by cDNA Precursor Cloning in the Frame of This Family of Intriguing Peptides Marani, Mariela M. Aguilar, Silvana Cuzziol Boccioni, Ana P. Cancelarich, Natalia L. Basso, Néstor G. Albericio, Fernando Antibiotics (Basel) Article Ocellatins are a family of antimicrobial peptides found exclusively in the Leptodactylus genus. To date, 10 species have been studied and more than 23 peptides described. Here we report the sequences of five new peptides from the skin of the frog Leptodactylus latrans (Anura: Leptodactylidae) determined by cDNA cloning of the complete prepro-peptide structures. The mature peptides were characterized with in silico tools and compared with those previously described. With 21 amino acid residues, this new set of peptides not previously described in the Leptodactylus genus share between 100 and 76.2% similarity to ocellatin antimicrobial peptides. These novel peptides are cationic and their three-dimensional (3D) structure holds the highly conserved residues G(1), D(4), K(7), and K(11) and a high theoretical amphipathic α-helix content. Furthermore, in silico analyses of these new peptides predicted antimicrobial activity. This study is framed in the context of previous work published about ocellatins, and therefore, provides a review of this intriguing family of peptides. MDPI 2020-10-29 /pmc/articles/PMC7693824/ /pubmed/33138046 http://dx.doi.org/10.3390/antibiotics9110751 Text en © 2020 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 Marani, Mariela M. Aguilar, Silvana Cuzziol Boccioni, Ana P. Cancelarich, Natalia L. Basso, Néstor G. Albericio, Fernando Identification of New Ocellatin Antimicrobial Peptides by cDNA Precursor Cloning in the Frame of This Family of Intriguing Peptides |
title | Identification of New Ocellatin Antimicrobial Peptides by cDNA Precursor Cloning in the Frame of This Family of Intriguing Peptides |
title_full | Identification of New Ocellatin Antimicrobial Peptides by cDNA Precursor Cloning in the Frame of This Family of Intriguing Peptides |
title_fullStr | Identification of New Ocellatin Antimicrobial Peptides by cDNA Precursor Cloning in the Frame of This Family of Intriguing Peptides |
title_full_unstemmed | Identification of New Ocellatin Antimicrobial Peptides by cDNA Precursor Cloning in the Frame of This Family of Intriguing Peptides |
title_short | Identification of New Ocellatin Antimicrobial Peptides by cDNA Precursor Cloning in the Frame of This Family of Intriguing Peptides |
title_sort | identification of new ocellatin antimicrobial peptides by cdna precursor cloning in the frame of this family of intriguing peptides |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7693824/ https://www.ncbi.nlm.nih.gov/pubmed/33138046 http://dx.doi.org/10.3390/antibiotics9110751 |
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