Deep venomics of the Pseudonaja genus reveals inter- and intra-specific variation

Reeks, Timothy, Lavergne, Vincent, Sunagar, Kartik, Jones, Alun, Undheim, Eivind, Dunstan, Nathan, Fry, Bryan and Alewood, Paul F. (2016) Deep venomics of the Pseudonaja genus reveals inter- and intra-specific variation. Journal of Proteomics, 133 20-32. doi:10.1016/j.jprot.2015.11.019

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Author Reeks, Timothy
Lavergne, Vincent
Sunagar, Kartik
Jones, Alun
Undheim, Eivind
Dunstan, Nathan
Fry, Bryan
Alewood, Paul F.
Title Deep venomics of the Pseudonaja genus reveals inter- and intra-specific variation
Formatted title
Deep venomics of the Pseudonaja genus reveals inter- and intra-specific variation
Journal name Journal of Proteomics   Check publisher's open access policy
ISSN 1874-3919
Publication date 2016-02-05
Year available 2015
Sub-type Article (original research)
DOI 10.1016/j.jprot.2015.11.019
Open Access Status File (Author Post-print)
Volume 133
Start page 20
End page 32
Total pages 44
Place of publication Amsterdam, Netherlands
Publisher Elsevier
Language eng
Formatted abstract
Australian elapid venom remains an under-investigated resource of novel bioactive peptides. In this study, the venom gland transcriptomes and proteomes of the Australian western brown snakes, Pseudonaja aspidorhyncha and Pseudonaja nuchalis, were compared to Pseudonaja textilis. A deep venomics strategy incorporating high throughput 454 pyrosequencing gave a total of 200,911 raw reads for the three venoms. Subsequent annotation identified 5716 transcripts from 20 different toxin families with inter-specific variation between species observed in eight of the less abundant families. Integration of each venom proteome with the corresponding annotated reads identified 65 isoforms from six toxin families; high sequence coverage highlighted subtle differences between sequences and intra and inter-specific variation between species. High quality MS/MS data identified unusual glycoforms with natriuretic peptides from P. aspidorhyncha and P. nuchalis containing O-linked trisaccharides with high homology to the glycosylated region of TNPc. Molecular evolutionary assessments indicated the accelerated evolution of all toxin families with the exception of both natriuretic peptides and P. aspidorhyncha PLA2s that were found to be evolutionarily constrained under purifying selection pressures. This study has revealed a wide range of novel peptide sequences from six bioactive peptide families and highlights the subtle differences between toxins in these closely related species.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2016 Collection
School of Biological Sciences Publications
Institute for Molecular Bioscience - Publications
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Created: Wed, 09 Dec 2015, 18:25:19 EST by Susan Allen on behalf of Institute for Molecular Bioscience