ArticleProceedings of the National Academy of Sciences of the United States of America2014
A disulfide tether stabilizes the block of sodium channels by the conotoxin μO§-GVIIJ.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 43 citations in OpenAlex.
- Conotoxins Targeting Voltage-Gated Sodium Ion Channels.Pharmacological reviews · 2024Review
- Predatory and Defensive Strategies in Cone Snails.Toxins · 2024Review
- Trifunctional Saxitoxin Conjugates for Covalent Labeling of Voltage-Gated Sodium Channels.Chembiochem : a European journal of chemical biology · 2023Article
- Pain-causing stinging nettle toxins target TMEM233 to modulate NaNature communications · 2023Article
- Strategies for Heterologous Expression, Synthesis, and Purification of Animal Venom Toxins.Frontiers in bioengineering and biotechnology · 2021Review
- Venom-Derived Peptides Inhibiting Voltage-Gated Sodium and Calcium Channels in Mammalian Sensory Neurons.Advances in experimental medicine and biology · 2021Article
- Venom-Derived Peptide Modulators of Cation-Selective Channels: Friend, Foe or Frenemy.Frontiers in pharmacology · 2019Review
- Comparison of Strategies to Overcome Drug Resistance: Learning from Various Kingdoms.Molecules (Basel, Switzerland) · 2018Review
- Voltage-gated sodium channel β subunits: The power outside the pore in brain development and disease.Neuropharmacology · 2018Review
- µ-Conotoxins Modulating Sodium Currents in Pain Perception and Transmission: A Therapeutic Potential.Marine drugs · 2017Review
- Generation of therapeutic immunoconjugates via Residue-Specific Conjugation Technology (RESPECT) utilizing a native cysteine in the light chain framework of Oryctolagus cuniculus.Cancer biology & therapy · 2017Article
- Structural Basis for the Inhibition of Voltage-gated Sodium Channels by Conotoxin μO§-GVIIJ.The Journal of biological chemistry · 2016Article
- Article
- Evaluation of recombinant monoclonal antibody SVmab1 binding to NaF1000Research · 2016Article
- The hitchhiker's guide to the voltage-gated sodium channel galaxy.The Journal of general physiology · 2016Review
- Conotoxins That Could Provide Analgesia through Voltage Gated Sodium Channel Inhibition.Toxins · 2015Review
- Optimized deep-targeted proteotranscriptomic profiling reveals unexplored Conus toxin diversity and novel cysteine frameworks.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Insights into the origins of fish hunting in venomous cone snails from studies of Conus tessulatus.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Α- and β-subunit composition of voltage-gated sodium channels investigated with μ-conotoxins and the recently discovered μO§-conotoxin GVIIJ.Journal of neurophysiology · 2015Article
- Conotoxin gene superfamilies.Marine drugs · 2014Review
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Authors and funding
19 authors at 5 institutions in 3 countries.
Funding
Abstract
A cone snail venom peptide, μO§-conotoxin GVIIJ from Conus geographus, has a unique posttranslational modification, S-cysteinylated cysteine, which makes possible formation of a covalent tether of peptide to its target Na channels at a distinct ligand-binding site. μO§-conotoxin GVIIJ is a 35-aa peptide, with 7 cysteine residues; six of the cysteines form 3 disulfide cross-links, and one (Cys24) is S-cysteinylated. Due to limited availability of native GVIIJ, we primarily used a synthetic analog whose Cys24 was S-glutathionylated (abbreviated GVIIJSSG). The peptide-channel complex is stabilized by a disulfide tether between Cys24 of the peptide and Cys910 of rat (r) NaV1.2. A mutant channel of rNaV1.2 lacking a cysteine near the pore loop of domain II (C910L), was >10(3)-fold less sensitive to GVIIJSSG than was wild-type rNaV1.2. In contrast, although rNaV1.5 was >10(4)-fold less sensitive to GVIIJSSG than NaV1.2, an rNaV1.5 mutant with a cysteine in the homologous location, rNaV1.5[L869C], was >10(3)-fold more sensitive than wild-type rNaV1.5. The susceptibility of rNaV1.2 to GVIIJSSG was significantly altered by treating the channels with thiol-oxidizing or disulfide-reducing agents. Furthermore, coexpression of rNaVβ2 or rNaVβ4, but not that of rNaVβ1 or rNaVβ3, protected rNaV1.1 to -1.7 (excluding NaV1.5) against block by GVIIJSSG. Thus, GVIIJ-related peptides may serve as probes for both the redox state of extracellular cysteines and for assessing which NaVβ- and NaVα-subunits are present in native neurons.
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