1. Screening, Expression, Purification and Functional Characterization of Novel Antimicrobial Peptide Genes from Hermetia illucens (L.).
- Author
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Elhag O, Zhou D, Song Q, Soomro AA, Cai M, Zheng L, Yu Z, and Zhang J
- Subjects
- Animals, Anti-Infective Agents metabolism, DNA, Complementary, Diptera chemistry, Gram-Negative Bacteria drug effects, Gram-Positive Bacteria drug effects, Insect Proteins genetics, Insect Proteins metabolism, Microbial Sensitivity Tests, Plasmids, Anti-Infective Agents pharmacology, Insect Proteins pharmacology
- Abstract
Antimicrobial peptides from a wide spectrum of insects possess potent microbicidal properties against microbial-related diseases. In this study, seven new gene fragments of three types of antimicrobial peptides were obtained from Hermetia illucens (L), and were named cecropinZ1, sarcotoxin1, sarcotoxin (2a), sarcotoxin (2b), sarcotoxin3, stomoxynZH1, and stomoxynZH1(a). Among these genes, a 189-basepair gene (stomoxynZH1) was cloned into the pET32a expression vector and expressed in the Escherichia coli as a fusion protein with thioredoxin. Results show that Trx-stomoxynZH1 exhibits diverse inhibitory activity on various pathogens, including Gram-positive bacterium Staphylococcus aureus, Gram-negative bacterium Escherichia coli, fungus Rhizoctonia solani Khün (rice)-10, and fungus Sclerotinia sclerotiorum (Lib.) de Bary-14. The minimum inhibitory concentration of Trx-stomoxynZH1 is higher against Gram-positive bacteria than against Gram-negative bacteria but similar between the fungal strains. These results indicate that H. illucens (L.) could provide a rich source for the discovery of novel antimicrobial peptides. Importantly, stomoxynZH1 displays a potential benefit in controlling antibiotic-resistant pathogens., Competing Interests: The authors have declared that no competing interests exist.
- Published
- 2017
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