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Cited by 31Invertebrate Immune Response MechanismsAntimicrobial Peptides and ActivitiesImmune Response and Inflammation

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Drosophila immunity: the Drosocin gene encodes two host defence peptides with pathogen-specific roles

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Hanson, M. A., Kondo, S., Lemaitre, B.·2022·Proceedings of the Royal Society B: Biological Sciences
DOI 10.1098/rspb.2022.0773PMC PMC9233930

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Abstract

Antimicrobial peptides (AMPs) are key to defence against infection in plants and animals. Use of AMP mutations in Drosophila has now revealed that AMPs can additively or synergistically contribute to defence in vivo . However, these studies also revealed high specificity, wherein just one AMP contributes an outsized role in combatting a specific pathogen. Here, we show the Drosocin locus ( CG10816 ) is more complex than previously described. In addition to its namesake peptide ‘Drosocin’, it encodes a second mature peptide from a precursor via furin cleavage. This peptide corresponds to the previously uncharacterized ‘Immune-induced Molecule 7’. A polymorphism (Thr52Ala) in the Drosocin precursor protein previously masked the identification of this peptide, which we name ‘Buletin’. Using mutations differently affecting Drosocin and Buletin, we show that only Drosocin contributes to Drosocin gene-mediated defence against Enterobacter cloacae . Strikingly, we observed that Buletin, but not Drosocin, contributes to the Drosocin gene-mediated defence against Providencia burhodogranariea , including an importance of the Thr52Ala polymorphism for survival. Our study reveals that the Drosocin gene encodes two prominent host defence peptides with different specificity against distinct pathogens. This finding emphasizes the complexity of the Drosophila humoral response and demonstrates how natural polymorphisms can affect host susceptibility.

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Metadata

Authors
Hanson, M. A., Kondo, S., & Lemaitre, B.
Affiliations
  • École Polytechnique Fédérale de Lausanne (CH)
  • National Institute of Genetics (JP)
  • Global Health Institute, School of Life Science, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland
Corresponding author
Hanson, M. A.
ORCID
Venue
Proceedings of the Royal Society B: Biological Sciences
Publisher
The Royal Society
Published
2022-06-22
Volume
289
Issue
1977
Pages
20220773-20220773
ISSN
  • 0080-4649 (ISSN-L)
  • 0962-8452
  • 1471-2954
DOI
10.1098/rspb.2022.0773
PMC
PMC9233930
OpenAlex
W4283317109
Cited by
31
References
1
Citations by year
2026: 6 · 2025: 4 · 2024: 10 · 2023: 7 · 2022: 4
FWCI
2.39
Type
journal article
Language
en
Open access
Licence
Locations
  • Proceedings of the Royal Society B Biological Sciences (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
Funders
  • Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (CRSII5_186397)
  • Novartis (532114)
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › Invertebrate Immune Response Mechanisms
  • Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
  • Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Keywords
drosocin, antimicrobial peptides, furin cleavage, Enterobacter cloacae, humoral immune response, host susceptibility
MeSH terms
Amino Acid Sequence, Animals, Drosophila, Drosophila melanogaster, Glycopeptides, Immunity, Innate, Antimicrobial Cationic Peptides

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