ArticleScientific reports2016
The drosomycin multigene family: three-disulfide variants from Drosophila takahashii possess antibacterial activity.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed.
- Pathogen-induced damage in Drosophila: Uncoupling disease tolerance from resistance.PLoS pathogens · 2025Article
- MdSVWC1, a new pattern recognition receptor triggers multiple defense mechanisms against invading bacteria in Musca domestica.BMC biology · 2024Article
- Mutation-driven evolution of antibacterial function in an ancestral antifungal scaffold: Significance for peptide engineering.Frontiers in microbiology · 2022Article
- Blattella germanica displays a large arsenal of antimicrobial peptide genes.Scientific reports · 2020Article
- Rapid Gene Family Evolution of a Nematode Sperm Protein Despite Sequence Hyper-conservation.G3 (Bethesda, Md.) · 2018Article
- Article
- Natural Antimicrobial Peptides as Inspiration for Design of a New Generation Antifungal Compounds.Journal of fungi (Basel, Switzerland) · 2017Review
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2 authors.
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Abstract
Drosomycin (DRS) is a strictly antifungal peptide in Drosophila melanogaster, which contains four disulfide bridges (DBs) with three buried in molecular interior and one exposed on molecular surface to tie the amino- and carboxyl-termini of the molecule together (called wrapper disulfide bridge, WDB). Based on computational analysis of genomes of Drosophila species belonging to the Oriental lineage, we identified a new multigene family of DRS in Drosphila takahashii that includes a total of 11 DRS-encoding genes (termed DtDRS-1 to DtDRS-11) and a pseudogene. Phylogenetic tree and synteny analyses reveal orthologous relationship between DtDRSs and DRSs, indicating that orthologous genes of DRS-1, DRS-2, DRS-3 and DRS-6 have undergone duplication in D. takahashii and three amplifications (DtDRS-9 to DtDRS-11) of DRS-3 have lost WDB. Among the 11 genes, five are transcriptionally active in adult fruitflies. The ortholog of DRS (DtDRS-1) shows high structural and functional similarity to DRS while two WDB-deficient members display antibacterial activity accompanying complete loss or remarkable reduction of antifungal activity. To the best of our knowledge, this is the first report on the presence of three-disulfide antibacterial DRSs in a specific Drosophila species, suggesting a potential role of DB loss in neofunctionalization of a protein via structural adjustment.
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