Venom composition and strategies in spiders: is everything possible?

Kuhn-Nentwig, Lucia; Stöcklin, Reto; Nentwig, Wolfgang (2011). Venom composition and strategies in spiders: is everything possible? Advances in insect physiology, 40, pp. 1-86. London: Academic Press 10.1016/B978-0-12-387668-3.00001-5

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This review on all spider venom components known by the end of 2010 bases on 1618 records for venom compounds from 174 spider species (= 0.41% of all known species) belonging to 32 families (= 29% of all existing spider families). Spiders investigated for venom research are either big (many mygalomorph species, Nephilidae, Ctenidae and Sparassidae) or medically important for humans (e.g. Loxosceles or Latrodectus species). Venom research widely ignored so far the two most species-rich families (Salticidae and Linyphiidae) and strongly neglected several other very abundant families (Araneidae, Lycosidae, Theridiidae, Thomisidae and Gnaphosidae).

We grouped the known 1618 records for venom compounds into six categories: low molecular mass compounds (16 % of all compounds), acylpolyamines (11 %), linear peptides (6 %), cysteine-knotted mini-proteins (60 %), neurotoxic proteins (1 %) and enzymes (6 %). Low molecular mass compounds are known from many spider families and contain organic acids, nucleosides, nucleotides, amino acids, amines, polyamines, and some further substances, many of them acting as neurotransmitters. Acylpolyamines contain amino acids (Araneidae and Nephilidae) or not (several other families) and show a very high diversity within one species. Linear peptides, also called cytolytic, membranolytic or antimicrobial, exert a highly specific structure and are so far only known from Ctenidae, Lycosidae, Oxyopidae and Zodariidae. Cysteine-knotted mini-proteins represent the majority of venom compounds because research so far focused on them. They probably occur in most but not all spider families. Neurotoxic proteins so far are only known from theridiid spiders. Enzymes had been neglected for some time but meanwhile it becomes obvious that they play an important role in spider venoms. Sixteen enzymes either cleave polymers in the extracellular matrix or target phospholipids and related compounds in membranes.

The overall structure of these compounds is given and the function, as far as it is known, is described. Since several of these component groups are presented in one average spider venom, we discuss the known interactions and synergisms and give reasons for such a functional redundancy. We also discuss main evolutionary pathways for spider venom compounds such as high variability among components of one group, synergistic interactions between cysteine-knotted mini-proteins and other components (low molecular mass compounds and linear peptides), change of function from ion-channel acting mini-proteins to cytolytic effects and replacement of mini-proteins by linear peptides, acylpolyamines, large proteins or enzymes. We also add first phylogenetic considerations.

Item Type:	Journal Article (Original Article)
Division/Institute:	08 Faculty of Science > Department of Biology > Institute of Ecology and Evolution (IEE) > Community Ecology [discontinued]
UniBE Contributor:	Kuhn-Nentwig, Lucia Gerda, Nentwig, Wolfgang
Subjects:	500 Science > 570 Life sciences; biology 500 Science > 590 Animals (Zoology) 500 Science > 580 Plants (Botany)
ISSN:	0065-2806
Publisher:	Academic Press
Language:	English
Submitter:	Factscience Import
Date Deposited:	04 Oct 2013 14:27
Last Modified:	02 Mar 2023 23:21
Publisher DOI:	10.1016/B978-0-12-387668-3.00001-5
Web of Science ID:	000299298700001
URI:	https://boris.unibe.ch/id/eprint/9818 (FactScience: 215612)