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Conus Peptides
Conus peptides, biodiversity-based discovery and exogenomics

The 700 different predatory cone snails (genus Conus) have evolved complex venoms, each species with it's own distinct set of 100 to 200 biologically active venom peptides. These are specified by a small number of gene superfamilies that rapidly diversify as speciation occurs. Most conopeptides are multiply disulfide cross-linked, with peptides in a superfamily having a characteristic disulfide framework, resulting in generally similar structures, but diverging function. Conopeptides have direct therapeutic applications - at least five are in clinical trials, and one (Prialt) has been approved as a drug for severe pain. Many conopeptides have exquisite targeting selectivity, and have the potential to be diagnostic ligands for a particular molecular isoform of an ion channel or receptor (the majority of conopeptide targets fall into these categories). The rapid diversification observed in conopeptide genes may be a general feature of all genes used by organisms to interact with other organisms in their environment. Across megadiverse taxa, each individual species has it's own complement of predators, prey and competitors; those genes whose products are used to mediate the biotic interactions of that particular species should thus be rapidly diversifying, if compared to homologous genes of other species. For conopeptides, an integrated approach to discovery that incorporates phylogenetics has been highly successful for identifying peptides with differing subtype-specificity.
Olivera BM. J Biol Chem. 2006 Aug 11; [Epub ahead of print]


Phylogenetic tree. The relationship of C. magus to other species is shown in the phylogenetic tree based on 16S sequences. The red branches show species in the subgenus Pionoconus, the purple branch is a
fish-hunter in Chelyconus. The green branch shows a mollusc hunter (C. aulicus). The uncolored branches are worm-hunting species, that specialize on amphinomid polychaetes; these express α-conopeptides in the α4/3 subfamily.
Baldomero M. Olivera. JBC Papers in Press. Published on August 11, 2006 as Manuscript R600020200

 


Baldomero M. Olivera. JBC Papers in Press. Published on August 11, 2006 as Manuscript R600020200

 


Baldomero M. Olivera. JBC Papers in Press. Published on August 11, 2006 as Manuscript R600020200

 


Talley T.T., et al. JBC Papers in Press. Published on June 27, 2006 as Manuscript M602969200

 

α-Conotoxin OmIA binding to AChBP. Concentration response curves were determined for α-
conotoxin OmIA displacement of radioligand binding to AChBP from Lymnaea stagnalis and Aplysia
californica as described in Experimental Procedures. A, competition with [125I] α-bungarotoxin. B,
competition with [3H] epibatidine. Calculated Kds are shown in Table I. n = 6 for all experiments.
Talley T.T., et al. JBC Papers in Press. Published on June 27, 2006 as Manuscript M602969200

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