Inhibition of evoked neurotransmitter release from rat hippocampus by a polypeptide toxin isolated from the marine snail Conus distans☆

Saxena, Vijay; Partoens, P.; Block, Jan De; Coen, Edmond; Vauquelin, Georges; Potter, W.P. De

doi:10.1016/0197-0186(92)90127-d

Cited by 8 publications

(3 citation statements)

References 26 publications

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“…Conus distans venom has not been analyzed extensively; to date, only two polypeptide toxins, 25.5 kDa and 24 kDa, respectively, were isolated and identified, but their peptide sequences were not reported (Saxena et al 1992, Partoens et al 1996. These two venom components were reported to affect the uptake of Ca in bovine chromaffin cells; the 25.5 kDa-component increases the initial rate of Ca uptake but it does not inhibit the stimulationevoked uptake, whereas the 24 kDa-component produces the complementary effects.…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of a novel excitatory peptide from Conus distans venom that defines a novel gene superfamily of conotoxins

Chen

Garrett²,

Watkins

et al. 2008

Toxicon

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An excitatory peptide, di16a, with 49 amino acids and ten cysteine residues was purified and characterized from the venom of Conus distans. Five AA residues were modified: one γ-carboxyglutamate (Gla), and four hydroxyproline (Hyp) residues. A cDNA clone encoding the precursor for the peptide was characterized; the peptide has a novel cysteine framework and a distinctive signal sequence that differs from any other conotoxin superfamily. The peptide was chemically synthesized and folded, and synthetic and native materials were shown to co-elute. Injection of the synthetic peptide causes a hyperexcitable phenotype in mice greater than three weeks of age at lower doses, and lethargy at higher doses. The peptide defines both a previouslyuncharacterized gene superfamily of conopeptides, and a new Cys pattern with three vicinal Cys residues.

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Section: Discussionmentioning

confidence: 99%

Purification and characterization of a novel excitatory peptide from Conus distans venom that defines a novel gene superfamily of conotoxins

Chen

Garrett²,

Watkins

et al. 2008

Toxicon

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“…To better understand when venom gland compartmentalisation might have evolved in cone snails, we studied the venom of the earliest diverging extant Conidae, Conus distans , from the Fraterconus subgenus [ 9 , 14 ]. The venom of this species is little studied, with previous assay-guided efforts only identifying proteins between 24 kDa and 25.5 kDa that blocked calcium influx associated with neurotransmitter release in the hippocampus of rats and bovine chromaffin cells [ 15 , 16 ] and a novel excitatory peptide, DiXIXA, possessing a rare triple cysteine motif [ 17 ].…”

Section: Introductionmentioning

confidence: 99%

Venomics Reveals a Non-Compartmentalised Venom Gland in the Early Diverged Vermivorous Conus distans

Prashanth

Dutertre

Kumar

et al. 2022

Toxins

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The defensive use of cone snail venom is hypothesised to have first arisen in ancestral worm-hunting snails and later repurposed in a compartmentalised venom duct to facilitate the dietary shift to molluscivory and piscivory. Consistent with its placement in a basal lineage, we demonstrate that the C. distans venom gland lacked distinct compartmentalisation. Transcriptomics revealed C. distans expressed a wide range of structural classes, with inhibitory cysteine knot (ICK)-containing peptides dominating. To better understand the evolution of the venom gland compartmentalisation, we compared C. distans to C. planorbis, the earliest diverging species from which a defence-evoked venom has been obtained, and fish-hunting C. geographus from the Gastridium subgenus that injects distinct defensive and predatory venoms. These comparisons support the hypothesis that venom gland compartmentalisation arose in worm-hunting species and enabled repurposing of venom peptides to facilitate the dietary shift from vermivory to molluscivory and piscivory in more recently diverged cone snail lineages.

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“…Although larger protein components are present in the cone snail venoms, only a few have been biochemically characterized and none have been reported to contain Gla (28)(29)(30)(31)(32). Recently, a 30 kDa calcium-dependent substrate-specific protease, Tex31, was identified in the venom of Conus textile (33).…”

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confidence: 99%

A Single γ-Carboxyglutamic Acid Residue in a Novel Cysteine-Rich Secretory Protein without Propeptide^,

et al. 2006

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Gamma-glutamyl carboxylase catalyzes the modification of specific glutamyl residues to gamma-carboxyglutamyl (Gla) residues in precursor proteins that possess the appropriate gamma-carboxylation recognition signal within the propeptide region. We describe the immunopurification and first biochemical characterization of an invertebrate high molecular weight Gla-containing protein with homologues in mammals. The protein, named GlaCrisp, was isolated from the venom of the marine cone snail Conus marmoreus. GlaCrisp gave intense signals in Western blot experiments employing the Gla-specific antibody M3B, and the presence of Gla was chemically confirmed by amino acid analysis after alkaline hydrolysis. Characterization of a full-length cDNA clone encoding GlaCrisp deduced a precursor containing an N-terminal signal peptide but, unlike other Gla-containing proteins, no apparent propeptide. The predicted mature protein of 265 amino acid residues showed considerable sequence similarity to the widely distributed cysteine-rich secretory protein family and closest similarity (65% identity) to the recently described substrate-specific protease Tex31. In addition, two cDNA clones encoding the precursors of two isoforms of GlaCrisp were identified. The predicted precursor isoforms differed at three amino acid positions (-6, 9, and 25). Analysis by Edman degradation and nanoelectrospray ionization mass spectrometry, before and after methyl esterfication, identified a Gla residue at amino acid position 9 in GlaCrisp. This is the first example of a Gla-containing protein without an obvious gamma-carboxylation recognition site. The results define a new class of Gla proteins and support the notion that gamma-carboxylation of glutamyl residues is phylogenetically older than blood coagulation and the vertebrate lineage.

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Inhibition of evoked neurotransmitter release from rat hippocampus by a polypeptide toxin isolated from the marine snail Conus distans☆

Cited by 8 publications

References 26 publications

Purification and characterization of a novel excitatory peptide from Conus distans venom that defines a novel gene superfamily of conotoxins

Purification and characterization of a novel excitatory peptide from Conus distans venom that defines a novel gene superfamily of conotoxins

Venomics Reveals a Non-Compartmentalised Venom Gland in the Early Diverged Vermivorous Conus distans

A Single γ-Carboxyglutamic Acid Residue in a Novel Cysteine-Rich Secretory Protein without Propeptide^,

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Inhibition of evoked neurotransmitter release from rat hippocampus by a polypeptide toxin isolated from the marine snail Conus distans☆

Cited by 8 publications

References 26 publications

Purification and characterization of a novel excitatory peptide from Conus distans venom that defines a novel gene superfamily of conotoxins

Purification and characterization of a novel excitatory peptide from Conus distans venom that defines a novel gene superfamily of conotoxins

Venomics Reveals a Non-Compartmentalised Venom Gland in the Early Diverged Vermivorous Conus distans

A Single γ-Carboxyglutamic Acid Residue in a Novel Cysteine-Rich Secretory Protein without Propeptide,

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Product

Resources

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A Single γ-Carboxyglutamic Acid Residue in a Novel Cysteine-Rich Secretory Protein without Propeptide^,