TY  - JOUR
PY  - 2009//
TI  - The Toxicogenomic Multiverse: Convergent Recruitment of Proteins Into Animal Venoms
JO  - Annual review of genomics and human genetics
A1  - Fry, Bryan G.
A1  - Roelants, Kim
A1  - Champagne, Donald E.
A1  - Scheib, Holger
A1  - Tyndall, Joel D. A.
A1  - King, Glenn F.
A1  - Nevalainen, Timo J.
A1  - Norman, Janette A.
A1  - Lewis, Russell J.
A1  - Norton, Raymond S.
A1  - Renjifo, Camila
A1  - Rodríguez de la Vega, RC
SP  - 483
EP  - 511
VL  - 10
IS  - 
N2  - 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. <p />  <p>Language: en</p>
LA  - en
SN  - 1527-8204
UR  - http://dx.doi.org/10.1146/annurev.genom.9.081307.164356
ID  - ref1
ER  -