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 , is a potent antimicrobial peptide against infection, which causes enteric diseases. However, there exist some limits for its practical application due to the loss of its activity in an increased...

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Bibliographic Details
Published in:Toxins 2017-10, Vol.9 (10), p.321
Main Authors: 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
Format: Article
Language:English
Subjects:
AMP
Antiinfectives and antibacterials
Antimicrobial activity
Antimicrobial agents
Bacteria
bacterial secretion system
E coli
Escherichia coli
inoculum effect
Mastoparan
MP-V1
Population
Protease
protease inhibitor
Protease inhibitors
Proteinase inhibitors
Salmonella
Secretion
Serotypes
Toxins
Venom
wasp venom toxin
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Summary:A previous study highlighted that mastoparan V1 (MP-V1), a mastoparan from the venom of the social wasp , is a potent antimicrobial peptide against 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 population using protease inhibitors, and developed an 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 serotypes, Gallinarum, Typhimurium and Enteritidis. Meanwhile, the strain harboring was identified to successfully secrete active MP-V1 into cell-free supernatant, whose antimicrobial activity disappeared in the increased population (10⁸ cfu/mL) of Typhimurium recovered by adding a protease inhibitor cocktail. Therefore, it has been concluded that our challenge using the secretion system with the protease inhibitors is an attractive strategy for practical application of peptide toxins, such as MP-V1.
ISSN:2072-6651
2072-6651
DOI:10.3390/toxins9100321