Drosomycin, an innate immunity peptide of Drosophila melanogaster, interacts with the fly voltage-gated sodium channel

Lior Cohen*, Yehu Moran, Amir Sharon, Daniel Segal, Dalia Gordon, Michael Gurevitz

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

31 Scopus citations


Several peptide families, including insect antimicrobial peptides, plant protease inhibitors, and ion channel gating modifiers, as well as blockers from scorpions, bear a common CSαβ scaffold. The high structural similarity between two peptides containing this scaffold, drosomycin and a truncated scorpion β-toxin, has prompted us to examine and compare their biological effects. Drosomycin is the most expressed antimicrobial peptide in Drosophila melanogaster immune response. A truncated scorpion β-toxin is capable of binding and inducing conformational alteration of voltage-gated sodium channels. Here, we show that both peptides (i) exhibit anti-fungal activity at micromolar concentrations; (ii) enhance allosterically at nanomolar concentration the activity of LqhαIT, a scorpion alpha toxin that modulates the inactivation of the D. melanogaster voltage-gated sodium channel (DmNav1); and (iii) inhibit the facilitating effect of the polyether brevetoxin-2 on DmNav1 activation. Thus, the short CSαβ scaffold of drosomycin and the truncated scorpion toxin can maintain more than one bioactivity, and, in light of this new observation, we suggest that the biological role of peptides bearing this scaffold should be carefully examined. As for drosomycin, we discuss the intriguing possibility that it has additional functions in the fly, as implied by its tight interaction with DmNav1.

Original languageAmerican English
Pages (from-to)23558-23563
Number of pages6
JournalJournal of Biological Chemistry
Issue number35
StatePublished - 28 Aug 2009
Externally publishedYes


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