LC-MS/MS of blue ring octopus and the southern sand octopus salivary gland extracts

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 ring 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 1,563 of 2,466 clusters 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 measurements. Phylogenetic analysis of the putative toxin serine proteases revealed a similar suite of diverse proteins present in both species. Venom composition 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. Dispersal factors particularly hyaluronidase, were disproportionately high in H. maculosa. Chitinase was abundant in both species and is believed to facilitate envenomation in chitinous/crustacean prey. 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.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Octopodiformes

TISSUE(S): Salivary Gland Cell, Salivary Gland

SUBMITTER: Ira Cooke  

LAB HEAD: Jan Strugnell

PROVIDER: PXD003897 | Pride | 2022-02-28

REPOSITORIES: Pride