Bose U , Wang T , Zhao M , Motti CA , Hall MR , Cummins SF .

	Figure 1. Charonia tritonis attack on a Crown-of-Thorns starfish (COTS). (A) C. tritonis withdraws proboscis in preparation for attack. (B) C. tritonis uses muscular foot to immobilize COTS. (C) Two C. tritonis feeding on a COTS, proboscis of the snail on the right penetrating COTS body wall. (D) Location of the proboscis, and internal organs including buccal mass, ducts and radula in C. tritonis.
	Figure 2. Charonia tritonis salivary gland (SG) anatomy and proteomics study. (A) Cephalic region of the C. tritonis. (B) Cephalic region with full proboscis and paired SGs exposed. (C) Cephalic region with proboscis removed. (D) Isolated SG showing region of anterior lobe (AL) and posterior lobe (PL). (E) Cell smear of AL. Arrow shows prominent mucin-like globlet cell. Scale bar represents 200 μm.
	Figure 3. Proteomics analysis of Charonia tritonis anterior lobe (AL) and posterior lobe (PL) of the salivary gland (SG). (A) SDS-PAGE and Coomassie stain of extracts derived from the SG-AL and SG-PL. (B) Comparison of total proteins identified in extracts of SG-AL and SG-PL, based on Pfam analysis.
	Figure 4. Molecular characterisation of Charonia tritonis cysteine-rich venom proteins (CRVPs), arylsulfatase and metalloprotease. Schematic diagram (top) showing the general organization with signal peptide (SP) and conserved domains (blue). Sequence logo representation (below) of multiple sequence alignments for C. tritonis with other species (Supplementary Data S8). Asterisks represent site of conserved cysteine (C) residues. Region of signal peptide (yellow) and conserved domain (blue) are shown.
	Figure 5. Molecular characterization of Charonia tritonis echotoxin proteins. (A) Multiple sequence alignment of C. tritonis echotoxin and with echotoxins from other species. Genbank accession numbers for all proteins are provided in Supplementary Data S8. Shading represents high amino acid conservation and the line shows region of signal peptide based on M. echo. The Lys (K) residue and residues involved in the aromatic patch are indicated by a closed circle and asterisks, respectively. (B) Phylogenetic tree of echotoxin proteins using neighbor-joining estimation. Scale bar represents amino acid substitutions. (C) 3D structure of fragaceatoxin from sea anemone (SWISS-MODEL id: 4tsn.3.A; identity 22.68% and sequence similarity 0.32) and the predicted C. tritonis echotoxin model, shown using ribbon representation in DeepView. Analysis of Z-scores of the template protein (fragaceatoxin) and echotoxin from C. tritonis shows the geometrical features responsible for an observed negative value. Large negative values correspond to red regions in the color gradient, and light red and deep blue region represents maximum match with protein used for modelling and the experimental protein. The structure reveals up to one ligand (phosphocholine) bound to a single chain of fragaceatoxin, a single binding site is also present in the echotoxin of C. tritonis.
	Figure 6. Identification of enzymes associated with the sulfuric acid biosynthesis pathway. (A) Pathway for biosynthesis of sulfuric acid. Those enzymes identified within the anterior lobe of the Charonia tritonis salivary gland are shown as (i), (ii) and (iii). (B) Schematics showing enzymes (i), (ii) and (iii) including characteristic domains. Biosynthetic enzymes derived from C. tritonis are listed in Supplementary Data S8.

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