Weaponization of a Hormone: Convergent Recruitment of Hyperglycemic Hormone into the Venom of Arthropod Predators
Undheim, EAB
Grimm, LL
Low, CF
Morgenstern, D
Herzig, V
Zobel-Thropp, P
Pineda, SS
Habib, R
Dziemborowicz, S
Fry, BG
Nicholson, GM
Binford, GJ
Mobli, M
King, GF
- Publication Type:
- Journal Article
- Citation:
- Structure, 2015, 23 (7), pp. 1283 - 1292
- Issue Date:
- 2015-07-09
Closed Access
Filename | Description | Size | |||
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1-s2.0-S0969212615001811-main.pdf | Published Version | 2.16 MB | Adobe PDF |
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Full metadata record
Field | Value | Language |
---|---|---|
dc.contributor.author | Undheim, EAB | en_US |
dc.contributor.author | Grimm, LL | en_US |
dc.contributor.author | Low, CF | en_US |
dc.contributor.author | Morgenstern, D | en_US |
dc.contributor.author | Herzig, V | en_US |
dc.contributor.author | Zobel-Thropp, P | en_US |
dc.contributor.author | Pineda, SS | en_US |
dc.contributor.author | Habib, R | en_US |
dc.contributor.author | Dziemborowicz, S | en_US |
dc.contributor.author | Fry, BG | en_US |
dc.contributor.author |
Nicholson, GM |
en_US |
dc.contributor.author | Binford, GJ | en_US |
dc.contributor.author | Mobli, M | en_US |
dc.contributor.author | King, GF | en_US |
dc.date.available | 2015-05-04 | en_US |
dc.date.issued | 2015-07-09 | en_US |
dc.identifier.citation | Structure, 2015, 23 (7), pp. 1283 - 1292 | en_US |
dc.identifier.issn | 0969-2126 | en_US |
dc.identifier.uri | http://hdl.handle.net/10453/117822 | |
dc.description.abstract | © 2015 Elsevier Ltd. Summary Arthropod venoms consist primarily of peptide toxins that are injected into their prey with devastating consequences. Venom proteins are thought to be recruited from endogenous body proteins and mutated to yield neofunctionalized toxins with remarkable affinity for specific subtypes of ion channels and receptors. However, the evolutionary history of venom peptides remains poorly understood. Here we show that a neuropeptide hormone has been convergently recruited into the venom of spiders and centipedes and evolved into a highly stable toxin through divergent modification of the ancestral gene. High-resolution structures of representative hormone-derived toxins revealed they possess a unique structure and disulfide framework and that the key structural adaptation in weaponization of the ancestral hormone was loss of a C-terminal α helix, an adaptation that occurred independently in spiders and centipedes. Our results raise a new paradigm for toxin evolution and highlight the value of structural information in providing insight into protein evolution. | en_US |
dc.relation.ispartof | Structure | en_US |
dc.relation.isbasedon | 10.1016/j.str.2015.05.003 | en_US |
dc.subject.classification | Biophysics | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Spiders | en_US |
dc.subject.mesh | Diptera | en_US |
dc.subject.mesh | Nerve Tissue Proteins | en_US |
dc.subject.mesh | Spider Venoms | en_US |
dc.subject.mesh | Evolution, Molecular | en_US |
dc.subject.mesh | Phylogeny | en_US |
dc.subject.mesh | Amino Acid Sequence | en_US |
dc.subject.mesh | Protein Structure, Secondary | en_US |
dc.subject.mesh | Molecular Sequence Data | en_US |
dc.subject.mesh | Protein Stability | en_US |
dc.subject.mesh | Arthropod Proteins | en_US |
dc.title | Weaponization of a Hormone: Convergent Recruitment of Hyperglycemic Hormone into the Venom of Arthropod Predators | en_US |
dc.type | Journal Article | |
utslib.citation.volume | 7 | en_US |
utslib.citation.volume | 23 | en_US |
utslib.for | 1115 Pharmacology and Pharmaceutical Sciences | en_US |
utslib.for | 0601 Biochemistry and Cell Biology | en_US |
utslib.for | 03 Chemical Sciences | en_US |
utslib.for | 06 Biological Sciences | en_US |
utslib.for | 08 Information and Computing Sciences | en_US |
pubs.embargo.period | Not known | en_US |
pubs.organisational-group | /University of Technology Sydney | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science | |
pubs.organisational-group | /University of Technology Sydney/Strength - CHT - Health Technologies | |
pubs.organisational-group | /University of Technology Sydney/Students | |
utslib.copyright.status | closed_access | |
pubs.issue | 7 | en_US |
pubs.publication-status | Published | en_US |
pubs.volume | 23 | en_US |
Abstract:
© 2015 Elsevier Ltd. Summary Arthropod venoms consist primarily of peptide toxins that are injected into their prey with devastating consequences. Venom proteins are thought to be recruited from endogenous body proteins and mutated to yield neofunctionalized toxins with remarkable affinity for specific subtypes of ion channels and receptors. However, the evolutionary history of venom peptides remains poorly understood. Here we show that a neuropeptide hormone has been convergently recruited into the venom of spiders and centipedes and evolved into a highly stable toxin through divergent modification of the ancestral gene. High-resolution structures of representative hormone-derived toxins revealed they possess a unique structure and disulfide framework and that the key structural adaptation in weaponization of the ancestral hormone was loss of a C-terminal α helix, an adaptation that occurred independently in spiders and centipedes. Our results raise a new paradigm for toxin evolution and highlight the value of structural information in providing insight into protein evolution.
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