The toxicogenomic multiverse: Convergent recruitment of proteins into animal venoms

Bryan G Fry, Kim Roelants, Donald E. Champagne, Holger Scheib, Joel D A Tyndall, Glenn Frederick King, Timo J. Nevalainen, Janette A Norman, Richard J Lewis, Raymond S. Norton, Camila Renjifo, Ricardo C. Rodríguez De La Vega

Research output: Contribution to journalReview ArticleResearchpeer-review

582 Citations (Scopus)


Throughout evolution, numerous proteins have been convergently recruited into the venoms of various animals, including centipedes, cephalopods, cone snails, fish, insects (several independent venom systems), platypus, scorpions, shrews, spiders, toxicoferan reptiles (lizards and snakes), and sea anemones. The protein scaffolds utilized convergently have included AVIT/colipase/ prokineticin, CAP, chitinase, cystatin, defensins, hyaluronidase, Kunitz, lectin, lipocalin, natriuretic peptide, peptidase S1, phospholipase A2, sphingomyelinase D, and SPRY. Many of these same venom protein types have also been convergently recruited for use in the hematophagous gland secretions of invertebrates (e.g., fleas, leeches, kissing bugs, mosquitoes, and ticks) and vertebrates (e.g., vampire bats). Here, we discuss a number of overarching structural, functional, and evolutionary generalities of the protein families from which these toxins have been frequently recruited and propose a revised and expanded working definition for venom. Given the large number of striking similarities between the protein compositions of conventional venoms and hematophagous secretions, we argue that the latter should also fall under the same definition.

Original languageEnglish
Pages (from-to)483-511
Number of pages29
JournalAnnual Review of Genomics and Human Genetics
Publication statusPublished - Sept 2009
Externally publishedYes


  • Convergence
  • Evolution
  • Phylogeny
  • Toxin

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