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Drosomycin

Drosomycin
Model of the AMP drosomycin
Identifiers
OrganismDrosophila melanogaster
SymbolDrs
UniProtP41964
Search for
StructuresSwiss-model
DomainsInterPro

Drosomycin is an antifungal peptide from Drosophila melanogaster and was the first antifungal peptide isolated from insects.[1] Drosomycin is induced by infection by the Toll signalling pathway,[2] while expression in surface epithelia like the respiratory tract is instead controlled by the immune deficiency pathway (Imd).[3] This means that drosomycin, alongside other antimicrobial peptides (AMPs) such as cecropins,[4][5] diptericin,[6] drosocin,[7] metchnikowin[8] and attacin,[9] serves as a first line defence upon septic injury. However drosomycin is also expressed constitutively to a lesser extent in different tissues and throughout development.[10]

  1. ^ Fehlbaum P, Bulet P, Michaut L, Lagueux M, Broekaert WF, Hetru C, Hoffmann JA (December 1994). "Insect immunity. Septic injury of Drosophila induces the synthesis of a potent antifungal peptide with sequence homology to plant antifungal peptides". The Journal of Biological Chemistry. 269 (52): 33159–63. doi:10.1016/S0021-9258(20)30111-3. PMID 7806546.
  2. ^ Lemaitre B, Nicolas E, Michaut L, Reichhart JM, Hoffmann JA (September 1996). "The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults". Cell. 86 (6): 973–83. doi:10.1016/S0092-8674(00)80172-5. PMID 8808632. S2CID 10736743.
  3. ^ Zhang ZT, Zhu SY (October 2009). "Drosomycin, an essential component of antifungal defence in Drosophila". Insect Molecular Biology. 18 (5): 549–56. doi:10.1111/j.1365-2583.2009.00907.x. PMID 19754735.
  4. ^ Kylsten P, Samakovlis C, Hultmark D (January 1990). "The cecropin locus in Drosophila; a compact gene cluster involved in the response to infection". The EMBO Journal. 9 (1): 217–24. doi:10.1002/j.1460-2075.1990.tb08098.x. PMC 551649. PMID 2104802.
  5. ^ Tryselius Y, Samakovlis C, Kimbrell DA, Hultmark D (February 1992). "CecC, a cecropin gene expressed during metamorphosis in Drosophila pupae". European Journal of Biochemistry. 204 (1): 395–9. doi:10.1111/j.1432-1033.1992.tb16648.x. PMID 1740152.
  6. ^ Wicker C, Reichhart JM, Hoffmann D, Hultmark D, Samakovlis C, Hoffmann JA (December 1990). "Insect immunity. Characterization of a Drosophila cDNA encoding a novel member of the diptericin family of immune peptides". The Journal of Biological Chemistry. 265 (36): 22493–8. doi:10.1016/S0021-9258(18)45732-8. PMID 2125051.
  7. ^ Bulet P, Dimarcq JL, Hetru C, Lagueux M, Charlet M, Hegy G, et al. (July 1993). "A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution". The Journal of Biological Chemistry. 268 (20): 14893–7. doi:10.1016/S0021-9258(18)82417-6. PMID 8325867.
  8. ^ Levashina EA, Ohresser S, Bulet P, Reichhart JM, Hetru C, Hoffmann JA (October 1995). "Metchnikowin, a novel immune-inducible proline-rich peptide from Drosophila with antibacterial and antifungal properties". European Journal of Biochemistry. 233 (2): 694–700. doi:10.1111/j.1432-1033.1995.694_2.x. PMID 7588819.
  9. ^ Asling B, Dushay MS, Hultmark D (April 1995). "Identification of early genes in the Drosophila immune response by PCR-based differential display: the Attacin A gene and the evolution of attacin-like proteins". Insect Biochemistry and Molecular Biology. 25 (4): 511–8. doi:10.1016/0965-1748(94)00091-C. PMID 7742836.
  10. ^ Ferrandon D, Jung AC, Criqui M, Lemaitre B, Uttenweiler-Joseph S, Michaut L, et al. (August 1998). "A drosomycin-GFP reporter transgene reveals a local immune response in Drosophila that is not dependent on the Toll pathway". The EMBO Journal. 17 (5): 1217–27. doi:10.1093/emboj/17.5.1217. PMC 1170470. PMID 9482719.

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