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Diptericin

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Diptericin
Identifiers
SymbolDiptericin, Dpt
InterProIPR040428

Diptericin is an antimicrobial peptide of flies first isolated in the blowfly Phormia terranova.[1] It is primarily active against Gram-negative bacteria, disrupting bacterial membrane integrity. The structure of this protein includes a proline-rich domain with similarities to the AMPs Drosocin, Pyrrhocoricin, and Abaecin, and a Glycine-rich domain with similarity to Attacin.[2][3] Diptericin is an iconic readout of immune system activity in flies, used ubiquitously in studies of Drosophila immunity.[4]

Structure and Function

Diptericins are found throughout Diptera[5], but are most extensively characterized in Drosophila. The mature structure of Diptericin is unknown, but its activity is strongly tied to residues in the Glycine-rich domain. A polymorphism at a single residue in the Diptericin Glycine-rich domain drastically affects its activity against the Gram-negative bacterium Providencia rettgeri.[6] This close association between Diptericin and P. rettgeri is further supported by genetic approaches that show that Diptericin is the only antimicrobial peptide of the Drosophila immune response that affects resistance to P. rettgeri.[7] These observations are part of a growing body of evidence that antimicrobial peptides can have intimate associations with microbes, in contrast to the previous philosophy that these peptides act in generalist and redundant fashions.[8][9][10] Diptericins can also have properties that reduce oxidative damage during the immune response.[11]

Roles Beyond Immunity

Overexpression of Diptericin and other antimicrobial peptides in the brains of flies leads to neurodegeneration.[12] The Drosophila Diptericin B gene is required for memory formation.[13]

References

  1. ^ Dimarcq, J. L.; Keppi, E.; Dunbar, B.; Lambert, J.; Reichhart, J. M.; Hoffmann, D.; Rankine, S. M.; Fothergill, J. E.; Hoffmann, J. A. (15 January 1988). "Insect immunity. Purification and characterization of a family of novel inducible antibacterial proteins from immunized larvae of the dipteran Phormia terranovae and complete amino-acid sequence of the predominant member, diptericin A". European Journal of Biochemistry. 171 (1–2): 17–22. PMID 3276515 – via PubMed.
  2. ^ "ScienceDirect". www.sciencedirect.com.
  3. ^ Cudic, Mare; Bulet, Philippe; Hoffmann, Ralf; Craik, David J.; Jr, Laszlo Otvos (17 February 1999). "Chemical synthesis, antibacterial activity and conformation of diptericin, an 82-mer peptide originally isolated from insects". European Journal of Biochemistry. 266 (2): 549–558. doi:10.1046/j.1432-1327.1999.00894.x – via Wiley Online Library.
  4. ^ Lemaitre, Bruno; Hoffmann, Jules (17 February 2019). "The host defense of Drosophila melanogaster". Annual Review of Immunology. 25: 697–743. doi:10.1146/annurev.immunol.25.022106.141615. PMID 17201680 – via PubMed.
  5. ^ Hanson, Mark A.; Hamilton, Phineas T.; Perlman, Steve J. (24 October 2016). "Immune genes and divergent antimicrobial peptides in flies of the subgenus Drosophila". BMC Evolutionary Biology. 16. doi:10.1186/s12862-016-0805-y. PMC 5078906. PMID 27776480 – via PubMed Central.{{cite journal}}: CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link)
  6. ^ Unckless, Robert L.; Howick, Virginia M.; Lazzaro, Brian P. (25 January 2016). "Convergent Balancing Selection on an Antimicrobial Peptide in Drosophila". Current biology: CB. 26 (2): 257–262. doi:10.1016/j.cub.2015.11.063. PMC 4729654. PMID 26776733 – via PubMed.{{cite journal}}: CS1 maint: PMC format (link)
  7. ^ Lemaitre, Bruno; Kondo, Shu; Poidevin, Mickael; Ceroni, Camilla; Dostalova, Anna; Hanson, Mark Austin (13 December 2018). "Synergy and remarkable specificity of antimicrobial peptides in vivo using a systematic knockout approach". bioRxiv: 493817. doi:10.1101/493817 – via www.biorxiv.org.
  8. ^ Imler, Jean-Luc; Bulet, Philippe (17 February 2019). "Antimicrobial peptides in Drosophila: structures, activities and gene regulation". Chemical Immunology and Allergy. 86: 1–21. doi:10.1159/000086648. PMID 15976485 – via PubMed.
  9. ^ Heddi, Abdelaziz; Rochat, Didier; Weiss-Gayet, Michèle; Vigneron, Aurélien; Vincent-Monégat, Carole; Vallier, Agnès; Balmand, Séverine; Login, Frédéric H. (21 October 2011). "Antimicrobial Peptides Keep Insect Endosymbionts Under Control". Science. 334 (6054): 362–365. doi:10.1126/science.1209728. PMID 22021855 – via science.sciencemag.org.
  10. ^ https://royalsocietypublishing.org/doi/full/10.1098/rstb.2015.0291
  11. ^ Zhao, Huiwen W.; Zhou, Dan; Haddad, Gabriel G. (25 February 2011). "Antimicrobial peptides increase tolerance to oxidant stress in Drosophila melanogaster". The Journal of Biological Chemistry. 286 (8): 6211–6218. doi:10.1074/jbc.M110.181206. PMC 3057857. PMID 21148307 – via PubMed.{{cite journal}}: CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link)
  12. ^ Ganetzky, Barry; Petersen, Andrew J.; Chtarbanova, Stanislava; Cao, Yang (7 May 2013). "Dnr1 mutations cause neurodegeneration in Drosophila by activating the innate immune response in the brain". Proceedings of the National Academy of Sciences. 110 (19): E1752–E1760. doi:10.1073/pnas.1306220110. PMID 23613578 – via www.pnas.org.
  13. ^ Si, Kausik; Dissel, Stephane; McKinney, Sean; Seidel, Chris; Welte, Ryan; Gill, Jason; Wu, Jianping; Barajas-Azpeleta, Raquel (12 October 2018). "Antimicrobial peptides modulate long-term memory". PLOS Genetics. 14 (10): e1007440. doi:10.1371/journal.pgen.1007440. PMC 6224176. PMID 30312294 – via PLoS Journals.{{cite journal}}: CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link)
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