ArticleThe protein journal2017
Oxidative Folding of Conopeptides Modified by Conus Protein Disulfide Isomerase.
Article in The protein journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- Multi-omics characterization of toxin expression and producing organs in the predatory gastropods Monoplex corrugatus and Stramonita haemastoma.BMC genomics · 2026Article
- Redox-Active Conopeptide Li520 Has Evolved to Catalyze Oxidative Folding of Conotoxins.ACS omega · 2024Article
- Article
- Usage of Cell-Free Protein Synthesis in Post-Translational Modification of μ-Conopeptide PIIIA.Marine drugs · 2023Article
- Application-Oriented Marine Isomerases in Biocatalysis.Marine drugs · 2020Review
- Conotoxin Diversity in the Venom Gland Transcriptome of the Magician's Cone,Marine drugs · 2019Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Protein disulfide isomerase is a type of enzyme that catalyses the oxidation, isomerization and reduction of disulfide bonds. Conotoxins that containing disulfide bonds are likely substrates of protein disulfide isomerise. Here, we cloned 12 protein disulfide isomerise genes from 12 different cone snail species that inhabited the sea near Sanya in China. The full-length amino acid sequences of these protein disulfide isomerase genes share a high degree of homology, including the same -CGHC- active site sequence and -RDEL- endoplasmic reticulum retention signal. To obtain enough conus protein disulfide isomerase for functional studies, we constructed the expression vector pET28a-sPDI. Conus protein disulfide isomerase was successfully expressed using Escherichia coli expression system and purified using chromatography method of affinity chromatography. The recombinant conus protein disulfide isomerase showed the ability to catalyse disulfide bond formation and rearrangement in the lysozyme enzyme activity assay. The role of conus protein disulfide isomerase in the in vitro oxidative folding of conotoxins was investigated using synthetic linear conotoxin lt14a, a peptide composed of 13 amino acids. It was confirmed by high performance liquid chromatography and mass spectrometry analysis that conus protein disulfide isomerase can catalyse the disulfide bond formation of linear lt14a. Then, conus protein disulfide isomerase was acted as a fusion partner during the production of engineered peptidyl-prolyl cis-trans isomerase and lt14a derived from cone snails. It was shown that peptidyl-prolyl cis-trans isomerase and conotoxin lt14a are successfully expressed in a highly soluble form by fusion with conus protein disulfide isomerase. Thus, conus protein disulfide isomerase functions not only as an enzyme that catalyses oxidative process but also a fusion partner in recombinant conotoxin expression.
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Registered trials
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