The Toxicogenomic Multiverse: Convergent Recruitment of Proteins Into Animal Venoms

Fry, Bryan G., Roelants, Kim, Champagne, Donald E., Scheib, Holger, Tyndall, Joel D. A., King, Glenn F., Nevalainen, Timo J., Norman, Janette A., Lewis, Richard J., Norton, Raymond S., Renjifo, Camila and Rodriguez de la Vega, Ricardo C. (2009) The Toxicogenomic Multiverse: Convergent Recruitment of Proteins Into Animal Venoms. Annual Review of Genomics and Human Genetics, 10 483-511. doi:10.1146/annurev.genom.9.081307.164356

Author Fry, Bryan G.
Roelants, Kim
Champagne, Donald E.
Scheib, Holger
Tyndall, Joel D. A.
King, Glenn F.
Nevalainen, Timo J.
Norman, Janette A.
Lewis, Richard J.
Norton, Raymond S.
Renjifo, Camila
Rodriguez de la Vega, Ricardo C.
Title The Toxicogenomic Multiverse: Convergent Recruitment of Proteins Into Animal Venoms
Journal name Annual Review of Genomics and Human Genetics   Check publisher's open access policy
ISSN 1527-8204
ISBN 978-0-8243-3710-0
Publication date 2009-09
Year available 2009
Sub-type Article (original research)
DOI 10.1146/annurev.genom.9.081307.164356
Volume 10
Start page 483
End page 511
Total pages 29
Editor Aravinda Chakravatrti
Place of publication California, USA
Publisher Annual Reviews
Collection year 2010
Language eng
Subject C1
970106 Expanding Knowledge in the Biological Sciences
110106 Medical Biochemistry: Proteins and Peptides (incl. Medical Proteomics)
Abstract 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.
Q-Index Code C1
Q-Index Status Confirmed Code

Document type: Journal Article
Sub-type: Article (original research)
Collections: 2010 Higher Education Research Data Collection
Institute for Molecular Bioscience - Publications
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Citation counts: TR Web of Science Citation Count  Cited 222 times in Thomson Reuters Web of Science Article | Citations
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Created: Tue, 09 Feb 2010, 14:19:33 EST by Susan Allen on behalf of Institute for Molecular Bioscience