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Identification of a Killer Toxin from Wickerhamomyces anomalus with β-Glucanase Activity
The yeast Wickerhamomyces anomalus has several applications in the food industry due to its antimicrobial potential and wide range of biotechnological properties. In particular, a specific strain of Wickerhamomyces anomalus isolated from the malaria mosquito Anopheles stephensi, namely WaF17.12, was...
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/PMC6832412/ https://www.ncbi.nlm.nih.gov/pubmed/31569379 http://dx.doi.org/10.3390/toxins11100568 |
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author | Cecarini, Valentina Cuccioloni, Massimiliano Bonfili, Laura Ricciutelli, Massimo Valzano, Matteo Cappelli, Alessia Amantini, Consuelo Favia, Guido Eleuteri, Anna Maria Angeletti, Mauro Ricci, Irene |
author_facet | Cecarini, Valentina Cuccioloni, Massimiliano Bonfili, Laura Ricciutelli, Massimo Valzano, Matteo Cappelli, Alessia Amantini, Consuelo Favia, Guido Eleuteri, Anna Maria Angeletti, Mauro Ricci, Irene |
author_sort | Cecarini, Valentina |
collection | PubMed |
description | The yeast Wickerhamomyces anomalus has several applications in the food industry due to its antimicrobial potential and wide range of biotechnological properties. In particular, a specific strain of Wickerhamomyces anomalus isolated from the malaria mosquito Anopheles stephensi, namely WaF17.12, was reported to secrete a killer toxin with strong anti-plasmodial effect on different developmental stages of Plasmodium berghei; therefore, we propose its use in the symbiotic control of malaria. In this study, we focused on the identification/characterization of the protein toxin responsible for the observed antimicrobial activity of the yeast. For this purpose, the culture medium of the killer yeast strain WaF17.12 was processed by means of lateral flow filtration, anion exchange and gel filtration chromatography, immunometric methods, and eventually analyzed by liquid chromatography-tandem mass spectrometry (LC–MS/MS). Based on this concerted approach, we identified a protein with a molecular weight of approximately 140 kDa and limited electrophoretic mobility, corresponding to a high molecular weight β-glucosidase, as confirmed by activity tests in the presence of specific inhibitors. |
format | Online Article Text |
id | pubmed-6832412 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-68324122019-11-25 Identification of a Killer Toxin from Wickerhamomyces anomalus with β-Glucanase Activity Cecarini, Valentina Cuccioloni, Massimiliano Bonfili, Laura Ricciutelli, Massimo Valzano, Matteo Cappelli, Alessia Amantini, Consuelo Favia, Guido Eleuteri, Anna Maria Angeletti, Mauro Ricci, Irene Toxins (Basel) Article The yeast Wickerhamomyces anomalus has several applications in the food industry due to its antimicrobial potential and wide range of biotechnological properties. In particular, a specific strain of Wickerhamomyces anomalus isolated from the malaria mosquito Anopheles stephensi, namely WaF17.12, was reported to secrete a killer toxin with strong anti-plasmodial effect on different developmental stages of Plasmodium berghei; therefore, we propose its use in the symbiotic control of malaria. In this study, we focused on the identification/characterization of the protein toxin responsible for the observed antimicrobial activity of the yeast. For this purpose, the culture medium of the killer yeast strain WaF17.12 was processed by means of lateral flow filtration, anion exchange and gel filtration chromatography, immunometric methods, and eventually analyzed by liquid chromatography-tandem mass spectrometry (LC–MS/MS). Based on this concerted approach, we identified a protein with a molecular weight of approximately 140 kDa and limited electrophoretic mobility, corresponding to a high molecular weight β-glucosidase, as confirmed by activity tests in the presence of specific inhibitors. MDPI 2019-09-28 /pmc/articles/PMC6832412/ /pubmed/31569379 http://dx.doi.org/10.3390/toxins11100568 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 Cecarini, Valentina Cuccioloni, Massimiliano Bonfili, Laura Ricciutelli, Massimo Valzano, Matteo Cappelli, Alessia Amantini, Consuelo Favia, Guido Eleuteri, Anna Maria Angeletti, Mauro Ricci, Irene Identification of a Killer Toxin from Wickerhamomyces anomalus with β-Glucanase Activity |
title | Identification of a Killer Toxin from Wickerhamomyces anomalus with β-Glucanase Activity |
title_full | Identification of a Killer Toxin from Wickerhamomyces anomalus with β-Glucanase Activity |
title_fullStr | Identification of a Killer Toxin from Wickerhamomyces anomalus with β-Glucanase Activity |
title_full_unstemmed | Identification of a Killer Toxin from Wickerhamomyces anomalus with β-Glucanase Activity |
title_short | Identification of a Killer Toxin from Wickerhamomyces anomalus with β-Glucanase Activity |
title_sort | identification of a killer toxin from wickerhamomyces anomalus with β-glucanase activity |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6832412/ https://www.ncbi.nlm.nih.gov/pubmed/31569379 http://dx.doi.org/10.3390/toxins11100568 |
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