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Toxins 2016, 8(3), 63; doi:10.3390/toxins8030063

Characterization and Recombinant Expression of Terebrid Venom Peptide from Terebra guttata

Hunter College, City University of New York, Belfer Research Center 413 E. 69th Street, New York, NY 10021, USA
The Graduate Center, City University of New York, 365 Fifth Avenue, New York, NY 10016, USA
New York Genome Center, 101 Avenue of the Americas, New York, NY 10013, USA
The American Museum of Natural History, 79th Street at Central Park West, New York, NY 10026, USA
These authors contributed equally to this work.
Author to whom correspondence should be addressed.
Academic Editor: Stephen Mackessy
Received: 1 January 2016 / Revised: 23 February 2016 / Accepted: 23 February 2016 / Published: 3 March 2016
(This article belongs to the Special Issue Venomics, Venom Proteomics and Venom Transcriptomics)
View Full-Text   |   Download PDF [1964 KB, uploaded 3 March 2016]   |  


Venom peptides found in terebrid snails expand the toolbox of active compounds that can be applied to investigate cellular physiology and can be further developed as future therapeutics. However, unlike other predatory organisms, such as snakes, terebrids produce very small quantities of venom, making it difficult to obtain sufficient amounts for biochemical characterization. Here, we describe the first recombinant expression and characterization of terebrid peptide, teretoxin Tgu6.1, from Terebra guttata. Tgu6.1 is a novel forty-four amino acid teretoxin peptide with a VI/VII cysteine framework (C–C–CC–C–C) similar to O, M and I conotoxin superfamilies. A ligation-independent cloning strategy with an ompT protease deficient strain of E. coli was employed to recombinantly produce Tgu6.1. Thioredoxin was introduced in the plasmid to combat disulfide folding and solubility issues. Specifically Histidine-6 tag and Ni-NTA affinity chromatography were applied as a purification method, and enterokinase was used as a specific cleavage protease to effectively produce high yields of folded Tgu6.1 without extra residues to the primary sequence. The recombinantly-expressed Tgu6.1 peptide was bioactive, displaying a paralytic effect when injected into a Nereis virens polychaete bioassay. The recombinant strategy described to express Tgu6.1 can be applied to produce high yields of other disulfide-rich peptides. View Full-Text
Keywords: Terebridae; venom peptides; teretoxins; recombinant synthesis; polychaete assay; disulfide-rich peptides; Conoidea; snail venom Terebridae; venom peptides; teretoxins; recombinant synthesis; polychaete assay; disulfide-rich peptides; Conoidea; snail venom

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Moon, J.; Gorson, J.; Wright, M.E.; Yee, L.; Khawaja, S.; Shin, H.Y.; Karma, Y.; Musunri, R.L.; Yun, M.; Holford, M. Characterization and Recombinant Expression of Terebrid Venom Peptide from Terebra guttata. Toxins 2016, 8, 63.

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