Buzz Kill: Function and Proteomic Composition of Venom from the Giant Assassin Fly Dolopus genitalis (Diptera: Asilidae)

A A Walker; J Dobson; J Jin; S D Robinson; Volker Herzig; I Vetter; G F King; B G Fry

doi:10.3390/toxins10110456

Back

Buzz Kill: Function and Proteomic Composition of Venom from the Giant Assassin Fly Dolopus genitalis (Diptera: Asilidae)

Journal article

Open access

Peer reviewed

Buzz Kill: Function and Proteomic Composition of Venom from the Giant Assassin Fly Dolopus genitalis (Diptera: Asilidae)

A A Walker, J Dobson, J Jin, S D Robinson, Volker Herzig, I Vetter, G F King and B G Fry

Toxins, Vol.10(11), 456

2018

DOI: https://doi.org/10.3390/toxins10110456

Files and links (2)

pdf

PDF - Published Version (Open Access)2.51 MBDownload View

Published VersionPDF - Published Version (Open Access)CC BY V4.0, Open Access

url

https://doi.org/10.3390/toxins10110456View

Published Version

Abstract

venom

peptide

defensin

Asilidae

Diptera

insect venom

Asilidin

inhibitor cystine knot

extra-oral digestion

Assassin flies (Diptera: Asilidae) inject paralysing venom into insect prey during hunting, but their venoms are poorly characterised in comparison to those produced by spiders, scorpions, or hymenopteran insects. Here we investigated the composition of the venom of the giant Australian assassin fly Dolopus genitalis using a combination of insect microinjection assays, calcium imaging assays of mammalian sensory neurons, proteomics and transcriptomics. Injection of venom into blowflies (Lucilia cuprina) produced rapid contractile paralysis (PD50 at 1 min = 3.1 μg per fly) followed by death, and also caused immediate activation of mouse dorsal root ganglion neurons (at 50 ng/μL). These results are consistent with venom use for both prey capture and predator deterrence. Paragon searches of tandem mass spectra of venom against a translated thoracic gland RNA-Seq database identified 122 polypeptides present in the venom, including six linear and 21 disulfide-rich peptides. Some of these disulfide-rich peptides display sequence homology to peptide families independently recruited into other animal venoms, including inhibitor cystine knots, cystine-stabilised α/β defensins, Kazal peptides, and von Willebrand factors. Numerous enzymes are present in the venom, including 35 proteases of the S1 family, proteases of the S10, C1A, M12A, M14, and M17 families, and phosphatase, amylase, hydrolase, nuclease, and dehydrogenase-like proteins. These results highlight convergent molecular evolution between the assassin flies and other venomous animals, as well as the unique and rich molecular composition of assassin fly venom.

Details

Title: Buzz Kill: Function and Proteomic Composition of Venom from the Giant Assassin Fly Dolopus genitalis (Diptera: Asilidae)
Authors: A A Walker (Author) - University of Queensland
J Dobson (Author) - University of Queensland
J Jin (Author) - University of Queensland
S D Robinson (Author) - University of Queensland
Volker Herzig (Author) - University of Queensland
I Vetter (Author) - University of Queensland
G F King (Author) - University of Queensland
B G Fry (Author) - University of Queensland
Publication details: Toxins, Vol.10(11), 456
Publisher: MDPI AG
Date published: 2018
DOI: 10.3390/toxins10110456
ISSN: 2072-6651
Copyright note: Copyright © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
Organisation Unit: School of Science and Engineering - Legacy; University of the Sunshine Coast, Queensland; School of Science, Technology and Engineering; Centre for Bioinnovation
Language: English
Record Identifier: 99450977602621
Output Type: Journal article

Metrics

41 File views/ downloads

74 Record Views

12 Times Cited - Web of Science

InCites Highlights

These are selected metrics from InCites Benchmarking & Analytics tool, related to this output

Web Of Science research areas: Food Science & Technology; Toxicology

UN Sustainable Development Goals (SDGs)

This output has contributed to the advancement of the following goals:

Source: InCites