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https://hdl.handle.net/2440/75130
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dc.contributor.author | Fry, B. | - |
dc.contributor.author | Roelants, K. | - |
dc.contributor.author | Winter, K. | - |
dc.contributor.author | Hodgson, W. | - |
dc.contributor.author | Griesman, L. | - |
dc.contributor.author | Kwok, H. | - |
dc.contributor.author | Scanlon, D. | - |
dc.contributor.author | Karas, J. | - |
dc.contributor.author | Shaw, C. | - |
dc.contributor.author | Wong, L. | - |
dc.contributor.author | Norman, J. | - |
dc.date.issued | 2010 | - |
dc.identifier.citation | Molecular Biology and Evolution, 2010; 27(2):395-407 | - |
dc.identifier.issn | 0737-4038 | - |
dc.identifier.issn | 1537-1719 | - |
dc.identifier.uri | http://hdl.handle.net/2440/75130 | - |
dc.description.abstract | The origin and evolution of venom proteins in helodermatid lizards were investigated by multidisciplinary techniques. Our analyses elucidated novel toxin types resultant from three unique domain-expression processes: 1) The first full-length sequences of lethal toxin isoforms (helofensins) revealed this toxin type to be constructed by an ancestral monodomain, monoproduct gene (beta-defensin) that underwent three tandem domain duplications to encode a tetradomain, monoproduct with a possible novel protein fold; 2) an ancestral monodomain gene (encoding a natriuretic peptide) was medially extended to become a pentadomain, pentaproduct through the additional encoding of four tandemly repeated proline-rich peptides (helokinestatins), with the five discrete peptides liberated from each other by posttranslational proteolysis; and 3) an ancestral multidomain, multiproduct gene belonging to the vasoactive intestinal peptide (VIP)/ glucagon family being mutated to encode for a monodomain, monoproduct (exendins) followed by duplication and diversification into two variant classes (exendins 1 and 2 and exendins 3 and 4). Bioactivity characterization of exendin and helokinestatin elucidated variable cardioactivity between isoforms within each class. These results highlight the importance of utilizing evolutionary-based search strategies for biodiscovery and the virtually unexplored potential of lizard venoms in drug design and discovery. | - |
dc.description.statementofresponsibility | Bryan G. Fry, Kim Roelants, Kelly Winter, Wayne C. Hodgson, Laura Griesman, Hang Fai Kwok, Denis Scanlon, John Karas, Chris Shaw, Lily Wong and Janette A. Norman | - |
dc.language.iso | en | - |
dc.publisher | Oxford Univ Press | - |
dc.rights | © The Author 2009. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution. All rights reserved. | - |
dc.source.uri | http://dx.doi.org/10.1093/molbev/msp251 | - |
dc.subject | Venom | - |
dc.subject | adaptive evolution | - |
dc.subject | molecular evolution | - |
dc.subject | protein | - |
dc.subject | toxin | - |
dc.subject | Heloderma | - |
dc.subject | byetta | - |
dc.subject | exendin | - |
dc.title | Novel venom proteins produced by differential domain-expression strategies in beaded lizards and gila monsters (genus Heloderma) | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1093/molbev/msp251 | - |
dc.relation.grant | ARC | - |
pubs.publication-status | Published | - |
Appears in Collections: | Aurora harvest Medical Sciences publications |
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