Plectreurys tristis venome: A proteomic and transcriptomic analysis

Research Article

J Venom Res 
(2014), Vol 5, 33-47

Published online: 20 September 2014

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Pamela A Zobel-Thropp a*, Emily Z Thomas a, Cynthia L David b, Linda A Breci b and Greta J Binford a

Department of Biology, Lewis & Clark College, Portland, OR 97219, USA

Arizona Proteomics Consortium, University of Arizona, Tucson, AZ 85721, USA

*Correspondence to: Pamela Zobel-Thropp, E-mail: (PAZT), Greta Binford, (GB), Tel: +503 768 7653, Fax: +503 768 7658

Received: 22 April 2014; Revised: 29 August 2014; Accepted: 15 September 2014

© Copyright The Author(s). First Published by Library Publishing Media. This is an open access article, published under the terms of the Creative Commons Attribution Non-Commercial License ( This license permits non-commercial use, distribution and reproduction of the article, provided the original work is appropriately acknowledged with correct citation details.


Spider venoms are complex cocktails rich in peptides, proteins and organic molecules that collectively act to immobilize prey. Venoms of the primitive hunting spider, Plectreurys tristis, have numerous neurotoxic peptides called “plectoxins” (PLTX), a unique acylpolyamine called bis(agmatine)oxalamide, and larger unidentified protein components. These spiders also have unconventional multi-lobed venom glands. Inspired by these unusual characteristics and their phylogenetic position as Haplogynes, we have partially characterized the venome of P. tristis using combined transcriptomic and proteomic methods. With these analyses we found known venom neurotoxins U1-PLTX-Pt1a, U3-PLTX-Pt1a, and we discovered new groups of potential neurotoxins, expanding the U1– and w-PLTX families and adding U4-through U9-PLTX as six new groups. The venom also contains proteins that are homologs of astacin metalloproteases that, combined with venom peptides, make up 94% of components detected in crude venom, while the remaining 6% is a single undescribed protein with unknown function. Other proteins detected in the transcriptome were found to be members of conserved gene families and make up 20% of the transcripts. These include cDNA sequences that match venom proteins from Mesobuthus and Hottentotta scorpions, Loxosceles and Dysdera spiders, and also salivary and secreted peptide sequences from Ixodes, Amblyomma and Rhipicephalus ticks. Finally, we show that crude venom has neurotoxic effects and an effective paralytic dose on crickets of 3.3µg/gm.

KEYWORDS: Spider,venom, astacin metalloprotease, neurotoxin, PD50, cDNA library, Orbitrap mass spectrometry