Journal of Molecular Evolution

, Volume 68, Issue 4, pp 311–321

Tentacles of Venom: Toxic Protein Convergence in the Kingdom Animalia


DOI: 10.1007/s00239-009-9223-8

Cite this article as:
Fry, B.G., Roelants, K. & Norman, J.A. J Mol Evol (2009) 68: 311. doi:10.1007/s00239-009-9223-8


The origin and evolution of venom in many animal orders remain controversial or almost entirely uninvestigated. Here we use cDNA studies of cephalopod posterior and anterior glands to reveal a single early origin of the associated secreted proteins. Protein types recoverd were CAP (CRISP, Antigen 5 [Ag5] and Pathogenesis-related [PR-1]), chitinase, peptidase S1, PLA2 (phospholipase A2), and six novel peptide types. CAP, chitinase, and PLA2 were each recovered from a single species (Hapalochlaena maculosa, Octopus kaurna, and Sepia latimanus, respectively), while peptidase S1 transcripts were found in large numbers in all three posterior gland libraries. In addition, peptidase S1 transcripts were recovered from the anterior gland of H. maculata. We compare their molecular evolution to that of related proteins found in invertebrate and vertebrate venoms, revealing striking similarities in the types of proteins selected for toxic mutation and thus shedding light on what makes a protein amenable for use as a toxin.


Venom Protein Phylogeny Cephalopod Convergence 

Copyright information

© Springer Science+Business Media, LLC 2009

Authors and Affiliations

  1. 1.Department of Biochemistry and Molecular Biology, Venomics Research Laboratory, Bio21 Molecular Science and Biotechnology InstituteUniversity of MelbourneParkvilleAustralia
  2. 2.Biology DepartmentVrije Universiteit Brussel (VUB)BrusselsBelgium
  3. 3.Sciences DepartmentMuseum VictoriaMelbourneAustralia

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