Abstract

Centipedes are among the oldest extant venomous predators on the planet. Armed with a pair of modified, venom-bearing limbs, they are an important group of predatory arthropods and are infamous for their ability to deliver painful stings. Despite this, very little is known about centipede venom and its composition. Advances in analytical tools, however, have recently provided the first detailed insights into the composition and evolution of centipede venoms. This has revealed that centipede venom proteins are highly diverse, with 61 phylogenetically distinct venom protein and peptide families. A number of these have been convergently recruited into the venoms of other animals, providing valuable information on potential underlying causes of the occasionally serious complications arising from human centipede envenomations. However, the majority of venom protein and peptide families bear no resemblance to any characterised protein or peptide family, highlighting the novelty of centipede venoms. This review highlights recent discoveries and summarises the current state of knowledge on the fascinating venom system of centipedes.

Highlights

  • Class Chilopoda, or centipedes, represents one of the four major myriapod lineages (Arthropoda; Myriapoda)

  • In addition to β-pore-forming toxins (β-PFTx) and centiCAPs, proteomic analyses show that novel proteins containing a low-density lipoprotein receptor Class A repeat (LDLA) domain are a major constituent of centipede venoms [26,29]

  • Despite being among the most ancient extant venomous animals, little is currently known about the evolution, ecology, and molecular and pharmacological diversity of centipede venoms

Read more

Summary

Introduction

Class Chilopoda, or centipedes, represents one of the four major myriapod lineages (Arthropoda; Myriapoda). Several morphological characters unite the members of Chilopoda, of which the most obvious is the modification of the first pair of walking legs into venomous appendages known as poison claws, toxicognaths, maxillipeds, or more correctly forcipules [1]. These are used to capture a wide variety of prey, including insects, spiders, crustaceans, snails, amphibians, reptiles, and even mammals; scutigeromorphs feed primarily by ambushing and chasing down prey, while the other orders seem to rely on opportunistic encounters [2]. This review aims to summarize current knowledge on centipede venoms and provide an updated nomenclatorial framework for organisation and naming of centipede toxins

Venom Apparatus
Molecular and Pharmacological Diversity
Molecular and Pharmacological Diversity—Enzymes
Metalloproteases
Serine Proteases
Glycoside Hydrolases
Phospholipase A2
Other Enzymes
Centipede β-Pore-Forming Toxins
CAP Proteins
LDLA Domain-Containing Proteins
Other Non-Enzymatic Proteins
Molecular and Pharmacological Diversity—Peptides
Molecular Diversity of Centipede Venom Peptides
Pharmacological Diversity of Centipede Venom Peptides
Clinical Importance of Centipede Stings
Conclusions
Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call