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. 2010 May 7;9(5):2292-301.
doi: 10.1021/pr901032r.

Proteomic analysis provides insights on venom processing in Conus textile

Lemmuel L Tayo  1 , Bingwen Lu, Lourdes J Cruz, John R Yates 3rd
Affiliations

Proteomic analysis provides insights on venom processing in Conus textile

Lemmuel L Tayo et al. J Proteome Res. .

Abstract

Conus species of marine snails deliver a potent collection of toxins from the venom duct via a long proboscis attached to a harpoon tooth. Conotoxins are known to possess powerful neurological effects and some have been developed for therapeutic uses. Using mass-spectrometry based proteomics, qualitative and quantitative differences in conotoxin components were found in the proximal, central and distal sections of the Conus textile venom duct suggesting specialization of duct sections for biosynthesis of particular conotoxins. Reversed phase HPLC followed by Orbitrap mass spectrometry and data analysis using SEQUEST and ProLuCID identified 31 conotoxin sequences and 25 post-translational modification (PTM) variants with King-Kong 2 peptide being the most abundant. Several previously unreported variants of known conopeptides were found and this is the first time that HyVal is reported for a disulfide rich Conus peptide. Differential expression along the venom duct, production of PTM variants, alternative proteolytic cleavage sites, and venom processing enroute to the proboscis all appear to contribute to enriching the combinatorial pool of conopeptides and producing the appropriate formulation for a particular hunting situation. The complementary tools of mass spectrometry-based proteomics and molecular biology can greatly accelerate the discovery of Conus peptides and provide insights on envenomation and other biological strategies of cone snails.

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Figures

Figure 1
Figure 1
Chromatograms of Conus textile venom from three sections of the duct
Figure 2
Figure 2
Distribution of conotoxins in the venom duct.. The radula sac contains about 30 hollow chitinous harpoons at different stages of formation. (Photo courtesy of Prof. Gil S. Jacinto and Katrina S. Luzon of UP Marine Science Institute.)
Figure 3
Figure 3
Alternative cleavage sites on the propeptide of Tx3a and three resulting conotoxins. Note: Z represents PyroGlu, HyV is a hydroxylated valine and C* is an amidated Cys residue.
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