Biology:Diptericin

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Diptericin
Pterraenovae.jpg
The blowfly Phormia terranova, in which Diptericin was first isolated
Identifiers
SymbolDiptericin, Dpt
InterProIPR040428

Diptericin is a 9 kDa antimicrobial peptide (AMP) of flies first isolated from 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] Diptericin is an iconic readout of immune system activity in flies, used ubiquitously in studies of Drosophila immunity.[3] Diptericin is named after the insect order Diptera.

Structure and function

Diptericins are found throughout Diptera,[4] but are most extensively characterized in Drosophila fruit flies. The mature structures of diptericins are unknown, though previous efforts to synthesize Diptericin have suggested Diptericin in Protophormia terraenovae is one linear peptide. Yet Drosophila melanogaster's Diptericin B peptide is likely cleaved into two separate peptides. Synthesis of Diptericin in vitro found activity of the full-length peptide, but independently synthesizing the two peptides and mixing them does not recapitulate Diptericin activity.[2][5] Diptericin A activity is strongly tied to residues in the glycine-rich domain.

Diptericin as a model for understanding the specificity of host-pathogen interactions

A polymorphism at a single residue in the diptericin glycine-rich domain drastically affects its activity against the Gram-negative bacterium Providencia rettgeri.[6] Flies with a Diptericin A gene encoding a serine allele survive infection significantly more than flies with an arginine allele. It is unclear how frequently such polymorphisms may dictate host-pathogen interactions, but there is evidence of widespread balancing selection that diptericin is not the only AMP with such polymorphisms.[7][8] 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.[9]

The fruit fly Diptericin gene "Diptericin B" has a unique structure that has been derived independently in both Tephritidae and Drosophila fruit flies. This represents convergent evolution of an antimicrobial peptide towards a common structure in two separate fruit-feeding lineages. This convergent evolution is driven by presence of Acetobacter bacteria in fruit-feeding ecologies.[10] Absence of Acetobacter in other ecologies has led to subsequent loss of Diptericin B.[10][11] Diptericin B loss is also convergent among lineages feeding on mushrooms or plants, including the mushroom-feeding fruit flies Leucophenga varia, Drosophila guttifera and Drosophila testacea, and plant-feeding Scaptomyza flies.[10]

These observations are part of a growing body of evidence that antimicrobial peptides can have intimate associations with microbes, and perhaps host ecology, in contrast to the previous philosophy that these peptides act in generalist and redundant fashions.[7][11][12][13]

Functions beyond antimicrobial activity

  • Diptericins can also have properties that reduce oxidative damage during the immune response.[14]
  • Suppression of the diptericin B and attacin C genes in Drosophila leads to increased Sindbis virus growth.[15]
  • Overexpression of diptericin and other antimicrobial peptides in the brains of flies leads to neurodegeneration.[16]
  • The Drosophila diptericin B gene is required for memory formation.[17]

References

  1. ↑ "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. January 1988. doi:10.1111/j.1432-1033.1988.tb13752.x. PMID 3276515. 
  2. ↑ 2.0 2.1 "Chemical synthesis, antibacterial activity and conformation of diptericin, an 82-mer peptide originally isolated from insects". European Journal of Biochemistry 266 (2): 549–58. December 1999. doi:10.1046/j.1432-1327.1999.00894.x. PMID 10561597. 
  3. ↑ "The host defense of Drosophila melanogaster". Annual Review of Immunology 25: 697–743. 17 February 2019. doi:10.1146/annurev.immunol.25.022106.141615. PMID 17201680. http://infoscience.epfl.ch/record/151765. 
  4. ↑ "Immune genes and divergent antimicrobial peptides in flies of the subgenus Drosophila". BMC Evolutionary Biology 16 (1): 228. October 2016. doi:10.1186/s12862-016-0805-y. PMID 27776480. Bibcode: 2016BMCEE..16..228H. 
  5. ↑ Hedengren, Marika; Borge, Karin; Hultmark, Dan (2000-12-20). "Expression and Evolution of the Drosophila Attacin/Diptericin Gene Family". Biochemical and Biophysical Research Communications 279 (2): 574–581. doi:10.1006/bbrc.2000.3988. ISSN 0006-291X. PMID 11118328. 
  6. ↑ "Convergent Balancing Selection on an Antimicrobial Peptide in Drosophila". Current Biology 26 (2): 257–262. January 2016. doi:10.1016/j.cub.2015.11.063. PMID 26776733. 
  7. ↑ 7.0 7.1 "The potential for adaptive maintenance of diversity in insect antimicrobial peptides". Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences 371 (1695): 20150291. May 2016. doi:10.1098/rstb.2015.0291. PMID 27160594. 
  8. ↑ Myers, Alexandra N.; Lawhon, Sara D.; Diesel, Alison B.; Bradley, Charles W.; Rodrigues Hoffmann, Aline; Murphy, William J.; 99 Lives Cat Genome Consortium (2022-02-14). Clark, Leigh Anne. ed. "An ancient haplotype containing antimicrobial peptide gene variants is associated with severe fungal skin disease in Persian cats" (in en). PLOS Genetics 18 (2): e1010062. doi:10.1371/journal.pgen.1010062. ISSN 1553-7404. PMID 35157719. 
  9. ↑ "Synergy and remarkable specificity of antimicrobial peptides in vivo using a systematic knockout approach". eLife 8. February 2019. doi:10.7554/eLife.44341. PMID 30803481. 
  10. ↑ 10.0 10.1 10.2 Hanson, M. A.; Grollmus, L.; Lemaitre, B. (2023-07-21). "Ecology-relevant bacteria drive the evolution of host antimicrobial peptides in Drosophila" (in en). Science 381 (6655): eadg5725. doi:10.1126/science.adg5725. ISSN 0036-8075. PMID 37471548. https://www.science.org/doi/10.1126/science.adg5725. 
  11. ↑ 11.0 11.1 Hanson, Mark Austin; Lemaitre, Bruno; Unckless, Robert L. (2019). "Dynamic evolution of antimicrobial peptides underscores trade-offs between immunity and ecological fitness" (in en). Frontiers in Immunology 10: 2620. doi:10.3389/fimmu.2019.02620. ISSN 1664-3224. PMID 31781114. 
  12. ↑ "Antimicrobial peptides in Drosophila: structures, activities and gene regulation". Chemical Immunology and Allergy 86: 1–21. 17 February 2019. doi:10.1159/000086648. ISBN 978-3-8055-7862-2. PMID 15976485. 
  13. ↑ "Antimicrobial peptides keep insect endosymbionts under control". Science 334 (6054): 362–5. October 2011. doi:10.1126/science.1209728. PMID 22021855. Bibcode: 2011Sci...334..362L. 
  14. ↑ "Antimicrobial peptides increase tolerance to oxidant stress in Drosophila melanogaster". The Journal of Biological Chemistry 286 (8): 6211–8. February 2011. doi:10.1074/jbc.M110.181206. PMID 21148307. 
  15. ↑ "An Antiviral Role for Antimicrobial Peptides during the Arthropod Response to Alphavirus Replication". J Virol 87 (8): 4272–80. 2013. doi:10.1128/JVI.03360-12. PMID 23365449. 
  16. ↑ "Dnr1 mutations cause neurodegeneration in Drosophila by activating the innate immune response in the brain". Proceedings of the National Academy of Sciences of the United States of America 110 (19): E1752-60. May 2013. doi:10.1073/pnas.1306220110. PMID 23613578. Bibcode: 2013PNAS..110E1752C. 
  17. ↑ "Antimicrobial peptides modulate long-term memory". PLOS Genetics 14 (10): e1007440. October 2018. doi:10.1371/journal.pgen.1007440. PMID 30312294. 



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