Combined transcriptomic and proteomic analysis of the posterior salivary gland from the southern blue-ringed octopus and the southern sand octopus

Whitelaw, Brooke Lauren, Strugnell, Jan M., Faou, Pierre, da Fonseca, Rute R., Hall, Nathan, Norman, Mark, Finn, Julian, and Cooke, Ira Robin (2016) Combined transcriptomic and proteomic analysis of the posterior salivary gland from the southern blue-ringed octopus and the southern sand octopus. Journal of Proteome Research, 15 (9). pp. 3284-3297.

[img] PDF (Published Version) - Published Version
Restricted to Repository staff only

View at Publisher Website: http://dx.doi.org/10.1021/acs.jproteome....
 
10
2


Abstract

This study provides comprehensive proteomic profiles from the venom producing posterior salivary glands of octopus (superorder Octopodiformes) species. A combined transcriptomic and proteomic approach was used to identify 1,703 proteins from the posterior salivary gland of the southern blue-ringed octopus, Hapalochlaena maculosa and 1,300 proteins from the posterior salivary gland of the southern sand octopus, Octopus kaurna. The two proteomes were broadly similar, clustering of proteins into orthogroups revealed 937 that were shared between species. Serine proteases were particularly diverse and abundant in both species. Other abundant proteins included a large number of secreted proteins many of which had no known conserved domains, or homology to proteins with known function. Based on homology to known venom proteins, 23 putative toxins were identified in H. maculosa and 24 in O. kaurna. These toxins span nine protein families: CAP (cysteine rich secretory proteins, antigen 5, parthenogenesis related), chitinase, carboxylesterase, DNase, hyaluronidase, metalloprotease, phospholipase, serine protease and tachykinin. Serine proteases were responsible for 70.9% and 86.3% of putative toxin expression in H. maculosa and O. kaurna respectively as determined using intensity based absolute quantification (iBAQ) measurements. Phylogenetic analysis of the putative toxin serine proteases revealed a similar suite of diverse proteins present in both species. Posterior salivary gland composition of H. maculosa and O. kaurna differ in several key aspects. While O. kaurna expressed the proteinaceous neurotoxin, tachykinin, this was absent from H. maculosa, perhaps reflecting the acquisition of a potent non-proteinaceous neurotoxin, tetrodotoxin (TTX) produced by bacteria in the salivary glands of that species. The dispersal factor, hyaluronidase was particularly abundant in H. maculosa. Chitinase was abundant in both species and is believed to facilitate envenomation in chitinous prey such as crustaceans. Cephalopods represent a largely unexplored source of novel proteins distinct from all other venomous taxa and are of interest for further inquiry as novel proteinaceous toxins derived from venoms may contribute to pharmaceutical design.

Item ID: 44750
Item Type: Article (Research - C1)
ISSN: 1535-3907
Keywords: Cephalopod, venom, proteogenomics, omics, transcriptomics, proteomics, venomics, tandem mass spectrometry, Hapalochlaena maculosa, Octopus kaurna
Funders: La Trobe University (LTU)
Projects and Grants: LTU Understanding Disease Research Focus Area small project grant
Date Deposited: 03 Aug 2016 03:03
FoR Codes: 06 BIOLOGICAL SCIENCES > 0601 Biochemistry and Cell Biology > 060102 Bioinformatics @ 100%
SEO Codes: 97 EXPANDING KNOWLEDGE > 970106 Expanding Knowledge in the Biological Sciences @ 100%
Downloads: Total: 2
More Statistics

Actions (Repository Staff Only)

Item Control Page Item Control Page