Conotoxins and the posttranslational modification of secreted gene products

@article{Buczek2005ConotoxinsAT,
  title={Conotoxins and the posttranslational modification of secreted gene products},
  author={O. Buczek and G. Bulaj and B. Olivera},
  journal={Cellular and Molecular Life Sciences CMLS},
  year={2005},
  volume={62},
  pages={3067-3079}
}
Abstract.The venoms of predatory cone snails (genus Conus) have yielded a complex library of about 50–100,000 bioactive peptides, each believed to have a specific physiological target (although peptides from different species may overlap in their target specificity). Conus has evolved the equivalent of a drug development strategy that combines the accelerated evolution of toxin sequences with an unprecedented degree of posttranslational modification. Some Conus venom peptide families are the… Expand
Various Conotoxin Diversifications Revealed by a Venomic Study of Conus flavidus*
TLDR
This study revealed that conotoxin-encoding transcripts are diversified by hypermutation, fragment insertion/deletion, and mutation-induced premature termination, and that a single mRNA species can produce multiple toxin products through alternative post-translational modifications and alternative cleavages of the translated precursor. Expand
Glycosylation of Conotoxins
TLDR
The potential application of specific conotoxins as neuropharmalogical agents and chemical probes requires a full characterization of the relevant peptides, including the structure of the carbohydrate part, and the currently existing knowledge of O-glycosylation of conotoxin is described. Expand
Specialisation of the venom gland proteome in predatory cone snails reveals functional diversification of the conotoxin biosynthetic pathway.
TLDR
Proteomic interrogations on the Conus venom gland led to the identification of novel glandular proteins of potential importance for toxin synthesis and secretion, and the presence of a multitude of isoforms of protein disulfide isomerase (PDI), the enzyme catalyzing the formation and isomerization of the native disulfides bond is demonstrated. Expand
PPIase is associated with the diversity of conotoxins from cone snail venom glands.
TLDR
The results suggest that PPIase may modify conotoxins containing prolines and play an important role in the process of peptide folding and modification in venom glands and contribute to conotoxin diversity. Expand
Post-translationally modified conopeptides: Biological activities and pharmacological applications
TLDR
This review focuses on ∼ 60 representative post-translationally modified conopeptides that were isolated from Conus venoms, and reveals post-translational modifications of specific amino acids, other than the more common disulfide crosslinking and C-terminal amidation. Expand
Conus Peptides: Biodiversity-based Discovery and Exogenomics*
  • B. Olivera
  • Biology, Medicine
  • Journal of Biological Chemistry
  • 2006
TLDR
The interdisciplinary paradigm that has evolved for the systematic discovery of Conus venom peptides, if applied more broadly, should prove fruitful for generally exploring chemical diversity from the animal biodiversity that surrounds us. Expand
Identification of six novel T-1 conotoxins from Conus pulicarius by molecular cloning
TLDR
A simple and fast strategy of gaining novel disulfide-rich conotoxins via molecular cloning is presented and the detailed sequence analysis will pave the way for the future functional characterization of toxin-receptor interaction. Expand
Contryphan Genes and Mature Peptides in the Venom of Nine Cone Snail Species by Transcriptomic and Mass Spectrometric Analysis.
TLDR
The widespread occurrence of contryphan genes and mature peptides in the venom of diverse cone snails is suggestive of their potential biological significance. Expand
Mass Spectral Identification of Vc1.1 and Differential Distribution of Conopeptides in the Venom Duct of Conus victoriae. Effect of Post-Translational Modifications and Disulfide Isomerisation on Bioactivity
Molluscs of the genus Conus (cone shells) are carnivorous, feeding on marine worms, small fish and other marine molluscs. They capture their prey by injecting venom containing hundreds of neurallyExpand
Purification and characterization of a novel excitatory peptide from Conus distans venom that defines a novel gene superfamily of conotoxins.
TLDR
An excitatory peptide, di16a, with 49 amino acids and 10 cysteine residues was purified and characterized from the venom of Conus distans, defining both a previously uncharacterized gene superfamily of conopeptides, and a new Cys pattern with three vicinal Cys residues. Expand
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
This study demonstrates for the first time that specialization of gene expression, processing, and secretion of conotoxins occurs in different regions of the venom duct. Expand
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