Abstract |
We report the identification, cloning, heterologous expression and functional characterization of a novel antifungal peptide named lucimycin from the common green bottle fly Lucilia sericata. The lucimycin cDNA was isolated from a library of genes induced during the innate immune response in L. sericata larvae, which are used as therapeutic maggots. The peptide comprises 77 amino acid residues with a molecular mass of 8.2 kDa and a pI of 6.6. It is predicted to contain a zinc-binding motif and to form a random coil, lacking β-sheets or other secondary structures. Lucimycin was active against fungi from the phyla Ascomycota, Basidiomycota and Zygomycota, in addition to the oomycete Phytophtora parasitica, but it was inactive against bacteria. A mutant version of lucimycin, lacking the four C-terminal amino acid residues, displayed 40-fold lower activity. The activity of lucimycin against a number of highly-destructive plant pathogens could be exploited to produce transgenic crops that are resistant against fungal diseases.
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Authors | Anne-Kathrin Pöppel, Aline Koch, Karl-Heinz Kogel, Heiko Vogel, Christian Kollewe, Jochen Wiesner, Andreas Vilcinskas |
Journal | Biological chemistry
(Biol Chem)
Vol. 395
Issue 6
Pg. 649-56
(Jun 2014)
ISSN: 1437-4315 [Electronic] Germany |
PMID | 24622788
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Antifungal Agents
- Peptides
- Lucensomycin
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Topics |
- Animals
- Antifungal Agents
(metabolism)
- Larva
- Lucensomycin
(metabolism)
- Peptides
(metabolism)
- Sequence Analysis, Protein
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