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Anti-Salmonella Activity Modulation of Mastoparan V1—A Wasp Venom Toxin—Using Protease Inhibitors, and Its Efficient Production via an Escherichia coli Secretion System
A previous study highlighted that mastoparan V1 (MP-V1), a mastoparan from the venom of the social wasp Vespula vulgaris, is a potent antimicrobial peptide against Salmonella infection, which causes enteric diseases. However, there exist some limits for its practical application due to the loss of i...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5666368/ https://www.ncbi.nlm.nih.gov/pubmed/29027924 http://dx.doi.org/10.3390/toxins9100321 |
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author | Ha, Yeon Jo Kim, Sam Woong Lee, Chae Won Bae, Chang-Hwan Yeo, Joo-Hong Kim, Il-Suk Gal, Sang Wan Hur, Jin Jung, Ho-Kyoung Kim, Min-Ju Bang, Woo Young |
author_facet | Ha, Yeon Jo Kim, Sam Woong Lee, Chae Won Bae, Chang-Hwan Yeo, Joo-Hong Kim, Il-Suk Gal, Sang Wan Hur, Jin Jung, Ho-Kyoung Kim, Min-Ju Bang, Woo Young |
author_sort | Ha, Yeon Jo |
collection | PubMed |
description | A previous study highlighted that mastoparan V1 (MP-V1), a mastoparan from the venom of the social wasp Vespula vulgaris, is a potent antimicrobial peptide against Salmonella infection, which causes enteric diseases. However, there exist some limits for its practical application due to the loss of its activity in an increased bacterial density and the difficulty of its efficient production. In this study, we first modulated successfully the antimicrobial activity of synthetic MP-V1 against an increased Salmonella population using protease inhibitors, and developed an Escherichia coli secretion system efficiently producing active MP-V1. The protease inhibitors used, except pepstatin A, significantly increased the antimicrobial activity of the synthetic MP-V1 at minimum inhibitory concentrations (determined against 10(6) cfu/mL of population) against an increased population (10(8) cfu/mL) of three different Salmonella serotypes, Gallinarum, Typhimurium and Enteritidis. Meanwhile, the E. coli strain harboring OmpA SS::MP-V1 was identified to successfully secrete active MP-V1 into cell-free supernatant, whose antimicrobial activity disappeared in the increased population (10(8) cfu/mL) of Salmonella Typhimurium recovered by adding a protease inhibitor cocktail. Therefore, it has been concluded that our challenge using the E. coli secretion system with the protease inhibitors is an attractive strategy for practical application of peptide toxins, such as MP-V1. |
format | Online Article Text |
id | pubmed-5666368 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-56663682017-11-09 Anti-Salmonella Activity Modulation of Mastoparan V1—A Wasp Venom Toxin—Using Protease Inhibitors, and Its Efficient Production via an Escherichia coli Secretion System Ha, Yeon Jo Kim, Sam Woong Lee, Chae Won Bae, Chang-Hwan Yeo, Joo-Hong Kim, Il-Suk Gal, Sang Wan Hur, Jin Jung, Ho-Kyoung Kim, Min-Ju Bang, Woo Young Toxins (Basel) Article A previous study highlighted that mastoparan V1 (MP-V1), a mastoparan from the venom of the social wasp Vespula vulgaris, is a potent antimicrobial peptide against Salmonella infection, which causes enteric diseases. However, there exist some limits for its practical application due to the loss of its activity in an increased bacterial density and the difficulty of its efficient production. In this study, we first modulated successfully the antimicrobial activity of synthetic MP-V1 against an increased Salmonella population using protease inhibitors, and developed an Escherichia coli secretion system efficiently producing active MP-V1. The protease inhibitors used, except pepstatin A, significantly increased the antimicrobial activity of the synthetic MP-V1 at minimum inhibitory concentrations (determined against 10(6) cfu/mL of population) against an increased population (10(8) cfu/mL) of three different Salmonella serotypes, Gallinarum, Typhimurium and Enteritidis. Meanwhile, the E. coli strain harboring OmpA SS::MP-V1 was identified to successfully secrete active MP-V1 into cell-free supernatant, whose antimicrobial activity disappeared in the increased population (10(8) cfu/mL) of Salmonella Typhimurium recovered by adding a protease inhibitor cocktail. Therefore, it has been concluded that our challenge using the E. coli secretion system with the protease inhibitors is an attractive strategy for practical application of peptide toxins, such as MP-V1. MDPI 2017-10-13 /pmc/articles/PMC5666368/ /pubmed/29027924 http://dx.doi.org/10.3390/toxins9100321 Text en © 2017 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 Ha, Yeon Jo Kim, Sam Woong Lee, Chae Won Bae, Chang-Hwan Yeo, Joo-Hong Kim, Il-Suk Gal, Sang Wan Hur, Jin Jung, Ho-Kyoung Kim, Min-Ju Bang, Woo Young Anti-Salmonella Activity Modulation of Mastoparan V1—A Wasp Venom Toxin—Using Protease Inhibitors, and Its Efficient Production via an Escherichia coli Secretion System |
title | Anti-Salmonella Activity Modulation of Mastoparan V1—A Wasp Venom Toxin—Using Protease Inhibitors, and Its Efficient Production via an Escherichia coli Secretion System |
title_full | Anti-Salmonella Activity Modulation of Mastoparan V1—A Wasp Venom Toxin—Using Protease Inhibitors, and Its Efficient Production via an Escherichia coli Secretion System |
title_fullStr | Anti-Salmonella Activity Modulation of Mastoparan V1—A Wasp Venom Toxin—Using Protease Inhibitors, and Its Efficient Production via an Escherichia coli Secretion System |
title_full_unstemmed | Anti-Salmonella Activity Modulation of Mastoparan V1—A Wasp Venom Toxin—Using Protease Inhibitors, and Its Efficient Production via an Escherichia coli Secretion System |
title_short | Anti-Salmonella Activity Modulation of Mastoparan V1—A Wasp Venom Toxin—Using Protease Inhibitors, and Its Efficient Production via an Escherichia coli Secretion System |
title_sort | anti-salmonella activity modulation of mastoparan v1—a wasp venom toxin—using protease inhibitors, and its efficient production via an escherichia coli secretion system |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5666368/ https://www.ncbi.nlm.nih.gov/pubmed/29027924 http://dx.doi.org/10.3390/toxins9100321 |
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