4.7 Article

Two Novel Mosquitocidal Peptides Isolated from the Venom of the Bahia Scarlet Tarantula (Lasiodora klugi)

Journal

TOXINS
Volume 15, Issue 7, Pages -

Publisher

MDPI
DOI: 10.3390/toxins15070418

Keywords

Lasiodora klugi; insecticidal toxin; Aedes aegypti; disulfide-directed beta-hairpin; inhibitor cystine knot

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The control of diseases transmitted by Aedes aegypti mainly relies on chemical insecticides, but insecticide resistance in A. aegypti hampers the effectiveness of current control measures. To address this issue, researchers screened spider and scorpion venoms for mosquitocidal toxins, and identified two peptides from the venom of Lasiodora klugi tarantula with activity against adult A. aegypti. These peptides, named U-TRTX-Lk1a and U-TRTX-Lk2a, have the potential to serve as novel control agents for A. aegypti.
Effective control of diseases transmitted by Aedes aegypti is primarily achieved through vector control by chemical insecticides. However, the emergence of insecticide resistance in A. aegypti undermines current control efforts. Arachnid venoms are rich in toxins with activity against dipteran insects and we therefore employed a panel of 41 spider and 9 scorpion venoms to screen for mosquitocidal toxins. Using an assay-guided fractionation approach, we isolated two peptides from the venom of the tarantula Lasiodora klugi with activity against adult A. aegypti. The isolated peptides were named U-TRTX-Lk1a and U-TRTX-Lk2a and comprised 41 and 49 residues with monoisotopic masses of 4687.02 Da and 5718.88 Da, respectively. U-TRTX-Lk1a exhibited an LD50 of 38.3 pmol/g when injected into A. aegypti and its modeled structure conformed to the inhibitor cystine knot motif. U-TRTX-Lk2a has an LD50 of 45.4 pmol/g against adult A. aegypti and its predicted structure conforms to the disulfide-directed beta-hairpin motif. These spider-venom peptides represent potential leads for the development of novel control agents for A. aegypti.

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