Drosomycin

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Drosomycin
Drosomycin
according to PDB  1MYN
other names

Cysteine-rich peptides

Mass / length primary structure 70 amino acids , 7,752 Da
Identifier
External IDs
Orthologue (fruit fly)
Entrez 38419
UniProt P41964
Refseq (mRNA) NM_079177.4
Refseq (protein) NP_523901.1
PubMed search 38419

Comparison of the Toll signaling pathway in mammals, shrimp, and fruit flies

Drosomycin is an antifungal peptide from the fruit fly Drosophila melanogaster .

properties

Drosomycin is produced in the fat body and secreted into the hemolymph . Six hours after activation of the innate immune response , the production of drosomycin increases and then drosomycin circulates for about three weeks. In the larvae of D. melanogaster , drosomycin is produced in the visceral branches and the posterior injection holes of the trachea . Drosomycin has four disulfide bridges . Drosomycin is partially homologous to an antifungal peptide from Brassicaceae . The four disulfide bridges stabilize the protein structure , consisting of an α-helix and a β-sheet , which is also found in other defensins of D. melanogaster and some plant defensins, for example drosomycin is 40% homologous to the defensin of the garden radish . The structure was first clarified in 1997.

The systemic gene expression of drosomycin is induced by Spaetzle , while the gene expression in the trachea is controlled by the Immune Deficiency Pathway (IMD). The gene of drosomycin drs is 387 bp long and lies on chromosome 3. It lies in a gene cluster with six other genes ( dro 1-6) and with them forms the drosomycin multigene family of different functions. Some of these genes were duplicated in the related fly D. takahashii and the drosomycin multigene family has eleven representatives there. Drosomycin is constitutively expressed in some organs through all stages of development (larva, pupa and adult fruit fly) of D. melanogaster .

Besides Drosomycin more antimicrobial peptides in the fruit fly are formed as Cecropine , diptericin , drosocin , Metchnikowin and Attacin .

The antifungal properties of the Drosomycins consist of a lysis of hyphae , a delay hyphal growth, which results in a premature branch, and in higher concentrations, the germination is spores inhibited.

Individual evidence

  1. ↑ a b S. Uttenweiler-Joseph, M. Moniatte, M. Lagueux, A. Van Dorsselaer, JA Hoffmann, P. Bulet: Differential display of peptides induced during the immune response of Drosophila: a matrix-assisted laser desorption ionization time- of-flight mass spectrometry study. In: Proceedings of the National Academy of Sciences . Volume 95, Number 19, September 1998, pp. 11342-11347, PMID 9736738 , PMC 21644 (free full text).
  2. ↑ I. Akhouayri, C. Turc, J. Royet, B. Charroux: Toll-8 / Tollo negatively Regulates antimicrobial response in the Drosophila respiratory epithelium. In: PLoS pathogens. Volume 7, number 10, October 2011, p. E1002319, doi : 10.1371 / journal.ppat.1002319 , PMID 22022271 , PMC 3192845 (free full text).
  3. ↑ a b P. Fehlbaum, P. Bulet, L. Michaut, M. Lagueux, WF Broekaert, C. Hetru, JA Hoffmann: Insect immunity. Septic injury of Drosophila induces the synthesis of a potent antifungal peptide with sequence homology to plant antifungal peptides. In: Journal of Biological Chemistry . Volume 269, Number 52, December 1994, pp. 33159-33163, PMID 7806546 .
  4. ↑ Franky Fant, Wim Vranken, Willem Broekaert, Frans Borremans: Determination of the three-dimensional solution structure of Raphanus sativus Antifungal Protein 1 by 1H NMR1 . In: Journal of Molecular Biology . 279, No. 1, May 29, 1998, pp. 257-270. doi : 10.1006 / jmbi.1998.1767 .
  5. ↑ Celine Landon, Patrick Sodano, Charles Hetru, Jules Hoffmann, Marius Ptak: Solution structure of drosomycin, the first inducible antifungal protein from insects . In: Protein Science . 6, No. 9, September 1, 1997, ISSN  1469-896X , pp. 1878-1884. doi : 10.1002 / pro.5560060908 . PMID 9300487 . PMC 2143780 (free full text).
  6. ↑ B. Lemaitre, E. Nicolas, L. Michaut, JM Reichhart, JA Hoffmann: The dorsoventral regulatory gene cassette spätzle / Toll / cactus controls the potent antifungal response in Drosophila adults. In: Cell . Volume 86, Number 6, September 1996, pp. 973-983, PMID 8808632 .
  7. ↑ ZT. Zhang, SY. Zhu: Drosomycin, an essential component of antifungal defense in Drosophila . In: Insect Molecular Biology . 18, No. 5, October 1, 2009, ISSN  1365-2583 , pp. 549-556. doi : 10.1111 / j.1365-2583.2009.00907.x .
  8. ↑ Drs Drosomycin [Drosophila melanogaster (fruit fly) - Gene - NCBI] .
  9. ↑ FM Jiggins and KW Kim, “The evolution of antifungal peptides in Drosophila,” Genetics, vol. 171, no. 4, pp. 1847-1859, 2005
  10. ^ WY Yang, SY Wen, YD Huang, et al., "Functional divergence of six isoforms of antifungal peptide drosomycin in Drosophila melanogaster," Gene, vol. 379, pp. 26-32, 2006
  11. ↑ Bin Gao, Shunyi Zhu: The drosomycin multigene family: three-disulfide variants from Drosophila takahashii possess antibacterial activity. In: Scientific Reports. 6, 2016, doi : 10.1038 / srep32175 .
  12. ↑ D. Ferrandon, AC Jung, M. Criqui, B. Lemaitre, S. Uttenweiler-Joseph, L. Michaut, J. Reichhart, JA Hoffmann: A drosomycin-GFP reporter transgene reveals a local immune response in Drosophila that is not dependent on the toll pathway . In: The EMBO Journal . 17, No. 5, August 10, 1998, ISSN  0261-4189 , pp. 1217-1227. doi : 10.1093 / emboj / 17.5.1217 . PMID 9482719 . PMC 1170470 (free full text).
  13. ↑ P. Kylsten, C. Samakovlis, D. Hultmark: The cecropin locus in Drosophila; a compact gene cluster involved in the response to infection . In: The EMBO Journal . 9, No. 1, January 1, 1990, ISSN  0261-4189 , pp. 217-224. PMID 2104802 . PMC 551649 (free full text).
  14. ↑ Y. Tryselius, C. Samakovlis, DA Kimbrell, D. Hultmark: CECC, a cecropin gene overexpressed during metamorphosis in Drosophila pupae . In: European Journal of Biochemistry . 204, No. 1, February 15, 1992, ISSN  0014-2956 , pp. 395-399. PMID 1740152 .
  15. ↑ C. Wicker, JM Reichhart, D. Hoffmann, D. Hultmark, C. Samakovlis, JA Hoffmann: Insect immunity. Characterization of a Drosophila cDNA encoding a novel member of the diptericin family of immune peptides. . In: Journal of Biological Chemistry . 265, No. 36, December 25, 1990, ISSN  0021-9258 , pp. 22493-22498. PMID 2125051 .
  16. ↑ P. Bulet, JL Dimarcq, C. Hetru, M. Lagueux, M. Charlet, G. Hegy, A. Van Dorsselaer, JA Hoffmann: A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution. . In: Journal of Biological Chemistry . 268, No. 20, July 15, 1993, ISSN  0021-9258 , pp. 14893-14897. PMID 8325867 .
  17. ↑ EA Levashina, p ear Esser, P. Bulet, JM Reichhart, C. Hetru, JA Hoffmann: Metchnikowin, a novel immune-inducible proline-rich peptide from Drosophila with antibacterial and antifungal properties . In: European Journal of Biochemistry . 233, No. 2, October 15, 1995, ISSN  0014-2956 , pp. 694-700. PMID 7588819 .
  18. ↑ B. Asling, MS Dushay, D. Hultmark: 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 . In: Insect Biochemistry and Molecular Biology . 25, No. 4, April 1, 1995, ISSN  0965-1748 , pp. 511-518. PMID 7742836 .
  19. ↑ Phillipe Bulet, Charles Hetru, Jean-Luc Dimarcq, Daniéle Hoffmann: Antimicrobial peptides in insects; structure and function . In: Developmental & Comparative Immunology . 23, No. 4-5, June 1, 1999, pp. 329-344. doi : 10.1016 / S0145-305X (99) 00015-4 .