Structure and bioactivity of an insecticidal trans-defensin from assassin bug venom.

Autor:	Walker AA; Institute for Molecular Bioscience, The University of Queensland, St Lucia, QLD 4072, Australia; Centre of Excellence for Innovations in Protein and Peptide Science, St Lucia, QLD 4072, Australia. Electronic address: a.walker@imb.uq.edu.au., Chin YK; Institute for Molecular Bioscience, The University of Queensland, St Lucia, QLD 4072, Australia; Centre for Advanced Imaging, The University of Queensland, St Lucia, QLD 4072, Australia., Guo S; Institute for Molecular Bioscience, The University of Queensland, St Lucia, QLD 4072, Australia., Jin J; Institute for Molecular Bioscience, The University of Queensland, St Lucia, QLD 4072, Australia., Wilbrink E; Institute for Molecular Bioscience, The University of Queensland, St Lucia, QLD 4072, Australia; Fontys University of Applied Sciences, Eindhoven 5612 AR, the Netherlands., Goudarzi MH; Institute for Molecular Bioscience, The University of Queensland, St Lucia, QLD 4072, Australia; Centre of Excellence for Innovations in Protein and Peptide Science, St Lucia, QLD 4072, Australia., Wirth H; Institute for Molecular Bioscience, The University of Queensland, St Lucia, QLD 4072, Australia; Centre of Excellence for Innovations in Protein and Peptide Science, St Lucia, QLD 4072, Australia., Gordon E; Department of Entomology, University of California Riverside, Riverside, CA 92521, USA., Weirauch C; Department of Entomology, University of California Riverside, Riverside, CA 92521, USA., King GF; Institute for Molecular Bioscience, The University of Queensland, St Lucia, QLD 4072, Australia; Centre of Excellence for Innovations in Protein and Peptide Science, St Lucia, QLD 4072, Australia. Electronic address: glenn.king@imb.uq.edu.au.
Jazyk:	angličtina
Zdroj:	Structure (London, England : 1993) [Structure] 2024 Sep 05; Vol. 32 (9), pp. 1348-1357.e4. Date of Electronic Publication: 2024 Jun 17.
DOI:	10.1016/j.str.2024.05.016
Abstrakt:	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.)
Databáze:	MEDLINE
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