The toxicogenomic multiverse: convergent recruitment of proteins into animal venoms.
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 A(2), 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.
Fry
Bryan G
BG
Department of Biochemistry and Molecular Biology, Bio21 Institute, University of Melbourne, Melbourne 3010 Australia. bgf@unimelb.edu.au
Roelants
Kim
K
Champagne
Donald E
DE
Scheib
Holger
H
Tyndall
Joel D A
JD
King
Glenn F
GF
Nevalainen
Timo J
TJ
Norman
Janette A
JA
Lewis
Richard J
RJ
Norton
Raymond S
RS
Renjifo
Camila
C
de la Vega
Ricardo C Rodríguez
RC
D000220:Adaptation, Biological; D000818:Animals; D016678:Genome; D006801:Humans; D010802:Phylogeny; D011506:Proteins / Q000235:genetics*; D043922:Toxicogenetics; D014688:Venoms / Q000235:genetics* / Q000633:toxicity*
D011506:Proteins; D014688:Venoms