Insecticidal activity of a recombinant knottin peptide from Loxosceles intermedia venom and recognition of these peptides as a conserved family in the genus

Matsubara, F. H., Meissner, G. O., Herzig, V., Justa, H. C., Dias, B. C. L., Trevisan-Silva, D., Gremski, L. H., Gremski, W., Senff-Ribeiro, A., Chaim, O. M., King, G. F. and Veiga, S. S. (2017) Insecticidal activity of a recombinant knottin peptide from Loxosceles intermedia venom and recognition of these peptides as a conserved family in the genus. Insect Molecular Biology, 26 1: 25-34. doi:10.1111/imb.12268


Author Matsubara, F. H.
Meissner, G. O.
Herzig, V.
Justa, H. C.
Dias, B. C. L.
Trevisan-Silva, D.
Gremski, L. H.
Gremski, W.
Senff-Ribeiro, A.
Chaim, O. M.
King, G. F.
Veiga, S. S.
Title Insecticidal activity of a recombinant knottin peptide from Loxosceles intermedia venom and recognition of these peptides as a conserved family in the genus
Formatted title
Insecticidal activity of a recombinant knottin peptide from Loxosceles intermedia venom and recognition of these peptides as a conserved family in the genus
Journal name Insect Molecular Biology   Check publisher's open access policy
ISSN 1365-2583
0962-1075
Publication date 2017-02-01
Year available 2016
Sub-type Article (original research)
DOI 10.1111/imb.12268
Open Access Status Not yet assessed
Volume 26
Issue 1
Start page 25
End page 34
Total pages 10
Place of publication Chichester, West Sussex, United Kingdom
Publisher Wiley-Blackwell Publishing
Language eng
Formatted abstract
Loxosceles intermedia venom comprises a complex mixture of proteins, glycoproteins and low molecular mass peptides that act synergistically to immobilize envenomed prey. Analysis of a venom-gland transcriptome from L. intermedia revealed that knottins, also known as inhibitor cystine knot peptides, are the most abundant class of toxins expressed in this species. Knottin peptides contain a particular arrangement of intramolecular disulphide bonds, and these peptides typically act upon ion channels or receptors in the insect nervous system, triggering paralysis or other lethal effects. Herein, we focused on a knottin peptide with 53 amino acid residues from L. intermedia venom. The recombinant peptide, named U2-sicaritoxin-Li1b (Li1b), was obtained by expression in the periplasm of Escherichia coli. The recombinant peptide induced irreversible flaccid paralysis in sheep blowflies. We screened for knottin-encoding sequences in total RNA extracts from two other Loxosceles species, Loxosceles gaucho and Loxosceles laeta, which revealed that knottin peptides constitute a conserved family of toxins in the Loxosceles genus. The insecticidal activity of U2-SCTX-Li1b, together with the large number of knottin peptides encoded in Loxosceles venom glands, suggests that studies of these venoms might facilitate future biotechnological applications of these toxins.
Keyword Bioinsecticide
Brown spider
Inhibitor cystine knot
Knottin
Loxosceles
Venom
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
Institute for Molecular Bioscience - Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 1 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 1 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Tue, 17 Jan 2017, 10:28:32 EST by System User on behalf of Learning and Research Services (UQ Library)