1. Structure and bioactivity of an insecticidal trans-defensin from assassin bug venom.
- Author
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Walker AA, Chin YK, Guo S, Jin J, Wilbrink E, Goudarzi MH, Wirth H, Gordon E, Weirauch C, and King GF
- Subjects
- Animals, Models, Molecular, Recombinant Proteins chemistry, Recombinant Proteins metabolism, Insect Proteins chemistry, Insect Proteins metabolism, Humans, Heteroptera chemistry, Heteroptera metabolism, Insecticides chemistry, Insecticides pharmacology, Drosophila melanogaster metabolism, Defensins chemistry, Defensins pharmacology, Arthropod Venoms chemistry, Arthropod Venoms metabolism, Amino Acid Sequence
- Abstract
Disulfide-rich peptides such as defensins play diverse roles in immunity and ion channel modulation, as well as constituting the bioactive components of many animal venoms. We investigated the structure and bioactivity of U-RDTX-Pp19, a peptide previously discovered in venom of the assassin bug Pristhesancus plagipennis. Recombinant Pp19 (rPp19) was found to possess insecticidal activity when injected into Drosophila melanogaster. A bioinformatic search revealed that domains homologous to Pp19 are produced by assassin bugs and diverse other arthropods. rPp19 co-eluted with native Pp19 isolated from P. plagipennis, which we found is more abundant in hemolymph than venom. We solved the three-dimensional structure of rPp19 using 2D
1 H NMR spectroscopy, finding that it adopts a disulfide-stabilized structure highly similar to known trans-defensins, with the same cystine connectivity as human α-defensin (I-VI, II-IV, and III-V). The structure of Pp19 is unique among reported structures of arthropod peptides., Competing Interests: Declaration of interests The authors declare no competing interests., (Copyright © 2024 Elsevier Inc. All rights reserved.)- Published
- 2024
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