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Analysis of Conus monile venom duct

ABSTRACT: Mass Spectrometric Characterisation of Linear Conotoxins.

INSTRUMENT(S): maXis

ORGANISM(S): Conus Monile

TISSUE(S): Venom Duct, Epithelial Cell

SUBMITTER: P Balaram

LAB HEAD: P.Balaram, MBU, IISc

PROVIDER: PXD042902 | Pride | 2023-12-05

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	Mo1521-fasta.fasta	Fasta
	Mo1521-search.dat	Other
	Mo1521.mgf	Mgf
	Mo1648-fasta.fasta	Fasta
	Mo1648-search.dat	Other

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1 - 5 of 17

Publications

Cysteine-free cone snail venom peptides: Classification of precursor proteins and identification of mature peptides.

Vijayasarathy Marimuthu M Kumar Sanjeev S Das Rajdeep R Balaram Padmanabhan P

Journal of peptide science : an official publication of the European Peptide Society 20231127 4

The cysteine-free acyclic peptides present in marine cone snail venom have been much less investigated than their disulfide bonded counterparts. Precursor protein sequences derived from transcriptomic data, together with mass spectrometric fragmentation patterns for peptides present in venom duct tissue extracts, permit the identification of mature peptides. Twelve distinct gene superfamiles have been identified with precursor lengths between 64 and 158 residues. In the case of Conus monile, thr ...[more]

PMID: 38009400

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Analysis of Conus venom peptides

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2018-06-29 | PXD009006 | Pride

Analysis of Conus monile venom duct.

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Contryphan sequence diversity: Messy N-terminus processing, effects on chromatographic behaviour and mass spectrometric fragmentation.

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Analysis of C.monile venom peptides.

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Contryphan sequence diversity:Conus lividus

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Contryphan sequence diversity:Conus amadis

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Characterization of the Conus bullatus genome and its venom-duct transcriptome.

Project description:BackgroundThe venomous marine gastropods, cone snails (genus Conus), inject prey with a lethal cocktail of conopeptides, small cysteine-rich peptides, each with a high affinity for its molecular target, generally an ion channel, receptor or transporter. Over the last decade, conopeptides have proven indispensable reagents for the study of vertebrate neurotransmission. Conus bullatus belongs to a clade of Conus species called Textilia, whose pharmacology is still poorly characterized. Thus the genomics analyses presented here provide the first step toward a better understanding the enigmatic Textilia clade.ResultsWe have carried out a sequencing survey of the Conus bullatus genome and venom-duct transcriptome. We find that conopeptides are highly expressed within the venom-duct, and describe an in silico pipeline for their discovery and characterization using RNA-seq data. We have also carried out low-coverage shotgun sequencing of the genome, and have used these data to determine its size, genome-wide base composition, simple repeat, and mobile element densities.ConclusionsOur results provide the first global view of venom-duct transcription in any cone snail. A notable feature of Conus bullatus venoms is the breadth of A-superfamily peptides expressed in the venom duct, which are unprecedented in their structural diversity. We also find SNP rates within conopeptides are higher compared to the remainder of C. bullatus transcriptome, consistent with the hypothesis that conopeptides are under diversifying selection.

| S-EPMC3040727 | biostudies-literature

Venom duct origins of prey capture and defensive conotoxins in piscivorous Conus striatus.

Project description:The venom duct origins of predatory and defensive venoms has not been studied for hook-and-line fish hunting cone snails despite the pharmacological importance of their venoms. To better understand the biochemistry and evolution of injected predatory and defensive venoms, we compared distal, central and proximal venom duct sections across three specimens of C. striatus (Pionoconus) using proteomic and transcriptomic approaches. A total of 370 conotoxin precursors were identified from the whole venom duct transcriptome. Milked defensive venom was enriched with a potent cocktail of proximally expressed inhibitory α-, ω- and μ-conotoxins compared to milked predatory venom. In contrast, excitatory κA-conotoxins dominated both the predatory and defensive venoms despite their distal expression, suggesting this class of conotoxin can be selectively expressed from the same duct segment in response to either a predatory or defensive stimuli. Given the high abundance of κA-conotoxins in the Pionoconus clade, we hypothesise that the κA-conotoxins have evolved through adaptive evolution following their repurposing from ancestral inhibitory A superfamily conotoxins to facilitate the dietary shift to fish hunting and species radiation in this clade.

| S-EPMC8225645 | biostudies-literature

Novel venom peptides from the cone snail Conus pulicarius discovered through next-generation sequencing of its venom duct transcriptome.

Project description:The venom peptides (i.e., conotoxins or conopeptides) that species in the genus Conus collectively produce are remarkably diverse, estimated to be around 50,000 to 140,000, but the pace of discovery and characterization of these peptides have been rather slow. To date, only a minor fraction have been identified and studied. However, the advent of next-generation DNA sequencing technologies has opened up opportunities for expediting the exploration of this diversity. The whole transcriptome of a venom duct from the vermivorous marine snail C. pulicarius was sequenced using the 454 sequencing platform. Analysis of the data set resulted in the identification of over eighty unique putative conopeptide sequences, the highest number discovered so far from a Conus venom duct transcriptome. More importantly, majority of the sequences were potentially novel, many with unexpected structural features, hinting at the vastness of the diversity of Conus venom peptides that remains to be explored. The sequences represented at least 14 major superfamilies/types (disulfide- and non-disulfide-rich), indicating the structural and functional diversity of conotoxins in the venom of C. pulicarius. In addition, the contryphans were surprisingly more diverse than what is currently known. Comparative analysis of the O-superfamily sequences also revealed insights into the complexity of the processes that drive the evolution and diversification of conotoxins.

| S-EPMC4286325 | biostudies-literature

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