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...
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MDPI AG
2017-10-01
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| Series: | Toxins |
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| Online Access: | https://www.mdpi.com/2072-6651/9/10/321 |
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| author | Yeon Jo Ha Sam Woong Kim Chae Won Lee Chang-Hwan Bae Joo-Hong Yeo Il-Suk Kim Sang Wan Gal Jin Hur Ho-Kyoung Jung Min-Ju Kim Woo Young Bang |
| author_facet | Yeon Jo Ha Sam Woong Kim Chae Won Lee Chang-Hwan Bae Joo-Hong Yeo Il-Suk Kim Sang Wan Gal Jin Hur Ho-Kyoung Jung Min-Ju Kim Woo Young Bang |
| author_sort | Yeon Jo Ha |
| collection | DOAJ |
| 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 106 cfu/mL of population) against an increased population (108 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 (108 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. |
| first_indexed | 2024-04-12T19:42:37Z |
| format | Article |
| id | doaj.art-f7ee7aa1f56d45adab3f20beecb459e4 |
| institution | Directory Open Access Journal |
| issn | 2072-6651 |
| language | English |
| last_indexed | 2024-04-12T19:42:37Z |
| publishDate | 2017-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Toxins |
| spelling | doaj.art-f7ee7aa1f56d45adab3f20beecb459e42022-12-22T03:19:02ZengMDPI AGToxins2072-66512017-10-0191032110.3390/toxins9100321toxins9100321Anti-Salmonella Activity Modulation of Mastoparan V1—A Wasp Venom Toxin—Using Protease Inhibitors, and Its Efficient Production via an Escherichia coli Secretion SystemYeon Jo Ha0Sam Woong Kim1Chae Won Lee2Chang-Hwan Bae3Joo-Hong Yeo4Il-Suk Kim5Sang Wan Gal6Jin Hur7Ho-Kyoung Jung8Min-Ju Kim9Woo Young Bang10Swine Science and Technology Center, Gyeongnam National University of Science and Technology, Gyeongnam 52725, KoreaSwine Science and Technology Center, Gyeongnam National University of Science and Technology, Gyeongnam 52725, KoreaNational Institute of Biological Resources (NIBR), Environmental Research Complex, Incheon 22689, KoreaNational Institute of Biological Resources (NIBR), Environmental Research Complex, Incheon 22689, KoreaNational Institute of Biological Resources (NIBR), Environmental Research Complex, Incheon 22689, KoreaSwine Science and Technology Center, Gyeongnam National University of Science and Technology, Gyeongnam 52725, KoreaSwine Science and Technology Center, Gyeongnam National University of Science and Technology, Gyeongnam 52725, KoreaVeterinary Public Health, College of Veterinary Medicine and Bio-Safety Research Institute, Chonbuk National University, Iksan 54596, KoreaKomipharm International Co. Ltd., Gyeonggi 15094, KoreaDepartment of Alternative Medicine, Kyonggi University, Gyeonggi 16227, KoreaNational Institute of Biological Resources (NIBR), Environmental Research Complex, Incheon 22689, KoreaA 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 106 cfu/mL of population) against an increased population (108 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 (108 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.https://www.mdpi.com/2072-6651/9/10/321AMPbacterial secretion systeminoculum effectmastoparanMP-V1protease inhibitorSalmonellawasp venom toxin |
| spellingShingle | Yeon Jo Ha Sam Woong Kim Chae Won Lee Chang-Hwan Bae Joo-Hong Yeo Il-Suk Kim Sang Wan Gal Jin Hur Ho-Kyoung Jung Min-Ju Kim Woo Young Bang Anti-Salmonella Activity Modulation of Mastoparan V1—A Wasp Venom Toxin—Using Protease Inhibitors, and Its Efficient Production via an Escherichia coli Secretion System Toxins AMP bacterial secretion system inoculum effect mastoparan MP-V1 protease inhibitor Salmonella wasp venom toxin |
| 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 | AMP bacterial secretion system inoculum effect mastoparan MP-V1 protease inhibitor Salmonella wasp venom toxin |
| url | https://www.mdpi.com/2072-6651/9/10/321 |
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