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The Toxicogenomic Multiverse: Convergent Recruitment of Proteins Into Animal Venoms


Fry, BG; Roelants, K; Champagne, DE; Scheib, H; Tyndall, JDA; King, GF; Nevalainen, TJ; Norman, JA; Lewis, RJ; Norton, RS; Renjifo, C; de la Vega, RCR
2009
ANNUAL REVIEW OF GENOMICS AND HUMAN GENETICS
S
10
483-511
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 salve 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 over-arching 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.
ANNUAL REVIEWS
PLATELET-AGGREGATION INHIBITOR; ADULT FEMALE MOSQUITO; SALIVARY-GLAND TRANSCRIPTS; TICK ORNITHODOROS-MOUBATA; BUG RHODNIUS-PROLIXUS; GATED ION CHANNELS; STONEFISH SYNANCEJA-HORRIDA; HISTAMINE-BINDING PROTEINS; FLY LUTZOMYIA-LONGIPALPIS; SHREW BLARINA-BREVICAUDA
10.1146/annurev.genom.9.081307.164356
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Creation Date 2009-01-01 12:00:00