Session: Parallel session 6 - Proteogenomics and metaproteomics

Cone snail venom characterization through combined mass spectrometry, transcriptomics and proteomics

Carnivorous marine cone snails produce highly complex venoms that are used as immobilizing agents against predators and preys (fish, mollusks, or worms) [1]. Their venoms are mainly made of highly structured cysteine-rich peptides known as conotoxins [2]. In some species, subsets of conotoxins are specifically selected for predation or defense [1,3]. Accelerated characterization of venoms was achieved through venomics, a combination of mass spectrometry, proteomics and transcriptomics [3]. In this work, we applied a venomics strategy to decipher the venom of Cylinder canonicus, a molluscivorous species from Mayotte Island. Venom gland transcriptomics were performed by Illumina mRNA sequencing, then peptide venoms were sequenced through proteomics to confirm and complete transcriptomics results.



LC-MS revealed a total of 631 unique masses in Cylinder canonicus venoms, and proteo-transcriptomics uncovered 108 conotoxin sequences from 24 gene superfamilies. Additionally, comparative LC-MS of venom profiles presume the origin of Cylinder canonicus predatory venom to be produced mostly from the distal section of the venom gland. Overall, this study contributes to a better understanding of cone snails prey strategies and provides novel conotoxin sequences with potential for biodiscovery.