期刊
ANNUAL REVIEW OF GENOMICS AND HUMAN GENETICS
卷 10, 期 -, 页码 483-511出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev.genom.9.081307.164356
关键词
toxin; phylogeny; evolution; convergence
资金
- Australian Academy of Science
- Austrilian French Association for Science and Technology
- Australia and Pacific Science Foundation
- CASS Foundation
- Herman Slade Foundation
- University of Melbourne (Faculty of Medicine and Department of Biochemistry)
- Department of Innovation, Industry, and Regional Development Victoria Fellowship
- Australian Research Council Grants
- Australian Government Department of Education, Science, and Training/EGIDE
- International Science Linkages
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.
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