Next Article in Journal
Daboia (Vipera) palaestinae Envenomation in 123 Horses: Treatment and Efficacy of Antivenom Administration
Previous Article in Journal
Development of Sensitive and Reliable UPLC-MS/MS Methods for Food Analysis of Emerging Mycotoxins in China Total Diet Study
Article Menu
Issue 3 (March) cover image

Export Article

Open AccessArticle
Toxins 2019, 11(3), 167;

The Dual Prey-Inactivation Strategy of Spiders—In-Depth Venomic Analysis of Cupiennius salei

Institute of Ecology and Evolution, University of Bern, Baltzerstrasse 6, CH-3012 Bern, Switzerland
Proteomics and Mass Spectrometry Core Facility, Department for BioMedical Research (DBMR), University of Bern, Freiburgstrasse 15, CH-3010 Bern, Switzerland
Institut National Polytechnique Félix Houphouet-Boigny, BP 1093 Yamoussoukro, Cote d’Ivoire
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Received: 5 March 2019 / Accepted: 14 March 2019 / Published: 19 March 2019
(This article belongs to the Section Animal Venoms)
PDF [7260 KB, uploaded 19 March 2019]


Most knowledge of spider venom concerns neurotoxins acting on ion channels, whereas proteins and their significance for the envenomation process are neglected. The here presented comprehensive analysis of the venom gland transcriptome and proteome of Cupiennius salei focusses on proteins and cysteine-containing peptides and offers new insight into the structure and function of spider venom, here described as the dual prey-inactivation strategy. After venom injection, many enzymes and proteins, dominated by α-amylase, angiotensin-converting enzyme, and cysteine-rich secretory proteins, interact with main metabolic pathways, leading to a major disturbance of the cellular homeostasis. Hyaluronidase and cytolytic peptides destroy tissue and membranes, thus supporting the spread of other venom compounds. We detected 81 transcripts of neurotoxins from 13 peptide families, whereof two families comprise 93.7% of all cysteine-containing peptides. This raises the question of the importance of the other low-expressed peptide families. The identification of a venom gland-specific defensin-like peptide and an aga-toxin-like peptide in the hemocytes offers an important clue on the recruitment and neofunctionalization of body proteins and peptides as the origin of toxins. View Full-Text
Keywords: in depth transcriptomics; proteomics; venom; enzymes; neurotoxins; α-amylase in depth transcriptomics; proteomics; venom; enzymes; neurotoxins; α-amylase

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Supplementary material


Share & Cite This Article

MDPI and ACS Style

Kuhn-Nentwig, L.; Langenegger, N.; Heller, M.; Koua, D.; Nentwig, W. The Dual Prey-Inactivation Strategy of Spiders—In-Depth Venomic Analysis of Cupiennius salei. Toxins 2019, 11, 167.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Toxins EISSN 2072-6651 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top