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Expression of the Shrimp wap gene in Drosophila elicits defense responses and protease inhibitory activity
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Number of Authors: 82018 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 8, article id 8779Article in journal (Refereed) Published
Abstract [en]

The wap gene encodes a single whey acidic protein (WAP) domain-containing peptide from Chinese white shrimp (Fenneropenaeus chinensis), which shows broad-spectrum antimicrobial activities and proteinase inhibitory activities in vitro. To explore the medical applications of the WAP peptide, a wap gene transgenic Drosophila melanogaster was constructed. In wap-expressing flies, high expression levels of wap gene (> 100 times) were achieved, in contrast to those of control flies, by qRT-PCR analysis. The wap gene expression was associated with increased resistance to microbial infection and decreased bacterial numbers in the flies. In addition, the WAP protein extract from wap-expressing flies, compared with control protein extract from control flies, showed improved antimicrobial activities against broad Gram-positive and Gram-negative bacteria, including the clinical drug resistant bacterium of methicillin-resistant S. aureus (MRSA), improved protease inhibitor activities against crude proteinases and commercial proteinases, including elastase, subtilis proteinase A, and proteinase K in vitro, and improved growth rate and microbial resistance, as well as wound-healing in loach and mouse models. These results suggest that wap-expressing flies could be used as a food additive in aquaculture to prevent infections and a potential antibacterial for fighting drug-resistant bacteria.

Place, publisher, year, edition, pages
2018. Vol. 8, article id 8779
National Category
Medical Biotechnology Biological Sciences
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URN: urn:nbn:se:su:diva-157650DOI: 10.1038/s41598-018-26466-6ISI: 000434641100009PubMedID: 29884877OAI: oai:DiVA.org:su-157650DiVA, id: diva2:1223504
Available from: 2018-06-25 Created: 2018-06-25 Last updated: 2018-06-25Bibliographically approved

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Arefin, Badrul
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Department of Molecular Biosciences, The Wenner-Gren Institute
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