Tentacles of Venom: Toxic Protein Convergence in the Kingdom Animalia
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The origin and evolution of venom in many animal orders remain controversial or almost entirely uninvestigated. Here we use cDNA studies of cephalopod posterior and anterior glands to reveal a single early origin of the associated secreted proteins. Protein types recoverd were CAP (CRISP, Antigen 5 [Ag5] and Pathogenesis-related [PR-1]), chitinase, peptidase S1, PLA2 (phospholipase A2), and six novel peptide types. CAP, chitinase, and PLA2 were each recovered from a single species (Hapalochlaena maculosa, Octopus kaurna, and Sepia latimanus, respectively), while peptidase S1 transcripts were found in large numbers in all three posterior gland libraries. In addition, peptidase S1 transcripts were recovered from the anterior gland of H. maculata. We compare their molecular evolution to that of related proteins found in invertebrate and vertebrate venoms, revealing striking similarities in the types of proteins selected for toxic mutation and thus shedding light on what makes a protein amenable for use as a toxin.
KeywordsVenom Protein Phylogeny Cephalopod Convergence
This work was funded by grants to B.G.F. from the Australian Academy of Science, Australian French Association for Science & Technology, Australia & Pacific Science Foundation, Australian Research Council (DP0665971 and DP0772814, to W.C.H. and J.A.N.), CASS Foundation, Ian Potter Foundation, International Human Frontiers Science Program Organisation, and the Netherlands Organisation for Scientific Research, University of Melbourne (Faculty of Medicine and Department of Biochemistry & Molecular Biology) and a Department of Innovation, Industry & Regional Development Victoria Fellowship. This work was also funded by an Australian Government Department of Education, Science & Training/EGIDE International Science Linkages grant to B.G.F and J.A.N. Accession numbers: GenBank accession numbers for sequences obtained in this study are EU790590–EU790615.
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