PXD004804

PXD004804 is an original dataset announced via ProteomeXchange.

Title	Assassin bug (Pristhesancus plagipennis) venom proteome
Description	Assassin bugs (Hemiptera: Heteroptera: Reduviidae) are venomous insects that prey on invertebrates. Assassin bug venom has features in common with venoms from other animals, such as paralysing and lethal activity when injected, and a molecular composition that includes disulfide-rich peptide neurotoxins. Uniquely, this venom also has strong liquefying activity that has been hypothesised to facilitate feeding through the narrow channel of the proboscis—a structure inherited from sap- and phloem-feeding phytophagous hemipterans and adapted during the evolution of Heteroptera into a fang and feeding structure. However, further understanding of the function of assassin bug venom is impeded by the lack of proteomic studies detailing its molecular composition. In addition, the lack of knowledge regarding venoms of predaceous reduviids limits our understanding of how the venoms of the blood-feeding kissing bugs (Reduviidae: Triatominae) evolved to facilitate hematophagy. By using a combined transcriptomic/proteomic approach we show that the venom proteome of the harpactorine assassin bug Pristhesancus plagipennis includes a complex suite of >100 proteins comprising disulfide-rich peptides, CUB-domain proteins, cystatins, putative cytolytic toxins, triabin-like protein, odorant binding protein, serine proteases, catabolic enzymes, putative nutrient-binding proteins, plus eight families of proteins without homology to characterised proteins. Serine proteases, CUB domain proteins and other novel proteins in the 10–16 kDa mass range, as well as putative cytolytic toxins, were the most abundant venom components. Thus, in addition to putative neurotoxins, assassin bug venom includes a high proportion of enzymatic and cytolytic venom components well suited to tissue liquefaction. While some protein families such as lipocalin/triabins occur in the venoms of both predaceous and blood-feeding reduviids, the composition of venoms in these two groups differs markedly. These results provide insights into the venom evolution in the insect suborder Heteroptera.
HostingRepository	PRIDE
AnnounceDate	2017-11-14
AnnouncementXML	Submission_2017-11-14_01:21:31.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Andrew Walker
SpeciesList	scientific name: Pristhesancus sp. 00004635; NCBI TaxID: 1276473;
ModificationList	No PTMs are included in the dataset
Instrument	TripleTOF 5600

Revision	Datetime	Status	ChangeLog Entry
0	2016-08-15 03:23:06	ID requested
⏵ 1	2017-11-14 01:21:32	announced

Walker AA, Madio B, Jin J, Undheim EA, Fry BG, King GF, (Hemiptera: Reduviidae). Mol Cell Proteomics, 16(4):552-566(2017) [pubmed]

curator keyword: Biological

submitter keyword: assassin bug, venom, Reduviidae, Heteroptera

Glenn F. King
contact affiliation	Institute for Molecular Bioscience, The University of Queensland, St Lucia, Queensland 4072, Australia
contact email	glenn.king@imb.uq.edu.au
lab head
Andrew Walker
contact affiliation	University of Queensland
contact email	a.walker@uq.edu.au
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2017/11/PXD004804

PRIDE project URI

• PRIDE
  1. PXD004804
     1. Label: PRIDE project
     2. Name: Assassin bug (Pristhesancus plagipennis) venom proteome