The Neurotoxic Mode of Action of Venoms from the Spider Family Theraphosidae

Herzig, Volker and King, Glenn F. (2013). The Neurotoxic Mode of Action of Venoms from the Spider Family Theraphosidae. In Wolfgang Nentwig (Ed.), Spider Ecophysiology (pp. 203-215) Heidelberg, Germany: Springer-Verlag. doi:10.1007/978-3-642-33989-9_15

Author Herzig, Volker
King, Glenn F.
Title of chapter The Neurotoxic Mode of Action of Venoms from the Spider Family Theraphosidae
Title of book Spider Ecophysiology
Place of Publication Heidelberg, Germany
Publisher Springer-Verlag
Publication Year 2013
Sub-type Research book chapter (original research)
DOI 10.1007/978-3-642-33989-9_15
Open Access Status
Year available 2012
ISBN 9783642339882
Editor Wolfgang Nentwig
Chapter number 15
Start page 203
End page 215
Total pages 14
Total chapters 37
Language eng
Formatted Abstract/Summary
Spiders from the family Theraphosidae are typically generalist predators of both invertebrates and vertebrates. Due to their large size and popularity in the pet trade, obtaining large amounts of a diverse range of theraphosid venoms is easier than for any other spider family. This explains why ~25 % of all spider toxins described to date originate from theraphosids even though they account for only 2 % of the taxonomic diversity of spiders. The main components of theraphosid venoms are neurotoxic peptides (cysteine-rich mini-proteins) that act on ion channels in the central or peripheral nervous system in order to induce rapid paralysis and/or death of prey. Their venoms also contain toxins that inhibit proteolytic degradation and enzymes that aid in the spread of other venom components. Some compounds in theraphosid venoms cause pain in vertebrates, making them useful for predator deterrence. Most theraphosid venom peptides contain three disulfide bonds that form an inhibitor cystine knot motif, which endows these toxins with extreme chemical and thermal stability, as well as resistance to proteolytic degradation. These properties, as well as their high potency and selectivity for particular molecular targets, have made some theraphosid venom peptides valuable as pharmacological tools and as leads for therapeutics and bioinsecticides.
Keyword Animal physiology
Animal biochemistr
Animal ecology
Q-Index Code B1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Book Chapter
Collections: Non HERDC
Institute for Molecular Bioscience - Publications
Version Filter Type
Citation counts: Scopus Citation Count Cited 11 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Tue, 12 Aug 2014, 00:59:13 EST by Susan Allen on behalf of Institute for Molecular Bioscience