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Toxins 2017, 9(10), 321; https://doi.org/10.3390/toxins9100321

Anti-Salmonella Activity Modulation of Mastoparan V1—A Wasp Venom Toxin—Using Protease Inhibitors, and Its Efficient Production via an Escherichia coli Secretion System

1
Swine Science and Technology Center, Gyeongnam National University of Science and Technology, Gyeongnam 52725, Korea
2
National Institute of Biological Resources (NIBR), Environmental Research Complex, Incheon 22689, Korea
3
Veterinary Public Health, College of Veterinary Medicine and Bio-Safety Research Institute, Chonbuk National University, Iksan 54596, Korea
4
Komipharm International Co. Ltd., Gyeonggi 15094, Korea
5
Department of Alternative Medicine, Kyonggi University, Gyeonggi 16227, Korea
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Steve Peigneur
Received: 15 September 2017 / Revised: 10 October 2017 / Accepted: 11 October 2017 / Published: 13 October 2017
(This article belongs to the Special Issue Toxins in Drug Discovery and Pharmacology)
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Abstract

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. View Full-Text
Keywords: AMP; bacterial secretion system; inoculum effect; mastoparan; MP-V1; protease inhibitor; Salmonella; wasp venom toxin AMP; bacterial secretion system; inoculum effect; mastoparan; MP-V1; protease inhibitor; Salmonella; wasp venom toxin
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Ha, Y.J.; Kim, S.W.; Lee, C.W.; Bae, C.-H.; Yeo, J.-H.; Kim, I.-S.; Gal, S.W.; Hur, J.; Jung, H.-K.; Kim, M.-J.; Bang, W.Y. 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 2017, 9, 321.

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