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Antimicrobial Peptides Pom-1 and Pom-2 from Pomacea poeyana Are Active against Candida auris, C. parapsilosis and C. albicans Biofilms
Recently two peptides isolated from the Cuban freshwater snail Pomacea poeyana (Pilsbry, 1927) were described to have antimicrobial activity against bacterial pathogens. Here we show considerable activities of Pom-1 and Pom-2 to reduce the viability of C. albicans, C. parapsilosis and the less commo...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8072573/ https://www.ncbi.nlm.nih.gov/pubmed/33924039 http://dx.doi.org/10.3390/pathogens10040496 |
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author | Raber, Heinz Fabian Sejfijaj, Jetmira Kissmann, Ann-Kathrin Wittgens, Andreas Gonzalez-Garcia, Melaine Alba, Annia Vázquez, Antonio A. Morales Vicente, Fidel E. Erviti, Julio Pérez Kubiczek, Dennis Otero-González, Anselmo Rodríguez, Armando Ständker, Ludger Rosenau, Frank |
author_facet | Raber, Heinz Fabian Sejfijaj, Jetmira Kissmann, Ann-Kathrin Wittgens, Andreas Gonzalez-Garcia, Melaine Alba, Annia Vázquez, Antonio A. Morales Vicente, Fidel E. Erviti, Julio Pérez Kubiczek, Dennis Otero-González, Anselmo Rodríguez, Armando Ständker, Ludger Rosenau, Frank |
author_sort | Raber, Heinz Fabian |
collection | PubMed |
description | Recently two peptides isolated from the Cuban freshwater snail Pomacea poeyana (Pilsbry, 1927) were described to have antimicrobial activity against bacterial pathogens. Here we show considerable activities of Pom-1 and Pom-2 to reduce the viability of C. albicans, C. parapsilosis and the less common species C. auris measured as the decrease of metabolic activity in the resazurin reduction assay for planktonic cells. Although these activities were low, Pom-1 and Pom-2 turned out to be highly potent inhibitors of biofilm formation for the three Candida species tested. Whereas Pom-1 was slightly more active against C. albicans and C. parapsilosis as representatives of the more common Candida species Pom-2 showed no preference and was fully active also against biofilms of the more uncommon species C. auris. Pom-1 and Pom-2 may represent promising lead structures for the development of a classical peptide optimization strategy with the realistic aim to further increase antibiofilm properties and other pharmacologic parameters and to generate finally the first antifungal drug with a pronounced dedication against Candida biofilms. |
format | Online Article Text |
id | pubmed-8072573 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-80725732021-04-27 Antimicrobial Peptides Pom-1 and Pom-2 from Pomacea poeyana Are Active against Candida auris, C. parapsilosis and C. albicans Biofilms Raber, Heinz Fabian Sejfijaj, Jetmira Kissmann, Ann-Kathrin Wittgens, Andreas Gonzalez-Garcia, Melaine Alba, Annia Vázquez, Antonio A. Morales Vicente, Fidel E. Erviti, Julio Pérez Kubiczek, Dennis Otero-González, Anselmo Rodríguez, Armando Ständker, Ludger Rosenau, Frank Pathogens Communication Recently two peptides isolated from the Cuban freshwater snail Pomacea poeyana (Pilsbry, 1927) were described to have antimicrobial activity against bacterial pathogens. Here we show considerable activities of Pom-1 and Pom-2 to reduce the viability of C. albicans, C. parapsilosis and the less common species C. auris measured as the decrease of metabolic activity in the resazurin reduction assay for planktonic cells. Although these activities were low, Pom-1 and Pom-2 turned out to be highly potent inhibitors of biofilm formation for the three Candida species tested. Whereas Pom-1 was slightly more active against C. albicans and C. parapsilosis as representatives of the more common Candida species Pom-2 showed no preference and was fully active also against biofilms of the more uncommon species C. auris. Pom-1 and Pom-2 may represent promising lead structures for the development of a classical peptide optimization strategy with the realistic aim to further increase antibiofilm properties and other pharmacologic parameters and to generate finally the first antifungal drug with a pronounced dedication against Candida biofilms. MDPI 2021-04-20 /pmc/articles/PMC8072573/ /pubmed/33924039 http://dx.doi.org/10.3390/pathogens10040496 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Communication Raber, Heinz Fabian Sejfijaj, Jetmira Kissmann, Ann-Kathrin Wittgens, Andreas Gonzalez-Garcia, Melaine Alba, Annia Vázquez, Antonio A. Morales Vicente, Fidel E. Erviti, Julio Pérez Kubiczek, Dennis Otero-González, Anselmo Rodríguez, Armando Ständker, Ludger Rosenau, Frank Antimicrobial Peptides Pom-1 and Pom-2 from Pomacea poeyana Are Active against Candida auris, C. parapsilosis and C. albicans Biofilms |
title | Antimicrobial Peptides Pom-1 and Pom-2 from Pomacea poeyana Are Active against Candida
auris, C. parapsilosis and C. albicans Biofilms |
title_full | Antimicrobial Peptides Pom-1 and Pom-2 from Pomacea poeyana Are Active against Candida
auris, C. parapsilosis and C. albicans Biofilms |
title_fullStr | Antimicrobial Peptides Pom-1 and Pom-2 from Pomacea poeyana Are Active against Candida
auris, C. parapsilosis and C. albicans Biofilms |
title_full_unstemmed | Antimicrobial Peptides Pom-1 and Pom-2 from Pomacea poeyana Are Active against Candida
auris, C. parapsilosis and C. albicans Biofilms |
title_short | Antimicrobial Peptides Pom-1 and Pom-2 from Pomacea poeyana Are Active against Candida
auris, C. parapsilosis and C. albicans Biofilms |
title_sort | antimicrobial peptides pom-1 and pom-2 from pomacea poeyana are active against candida
auris, c. parapsilosis and c. albicans biofilms |
topic | Communication |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8072573/ https://www.ncbi.nlm.nih.gov/pubmed/33924039 http://dx.doi.org/10.3390/pathogens10040496 |
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