Citation

Hocking HG, Gerwig GJ, Dutertre S, Violette A, Favreau P, Stöcklin R, Kamerling JP, Boelens R. Chemistry (Weinheim) 2013; 19(3): 870-879.

Affiliation

NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht (Netherlands), Fax: (+31) 30-253-7623. h.hocking@tum.de.

Copyright

(Copyright © 2013, John Wiley and Sons)

DOI

10.1002/chem.201202713

PMID

23281027

Abstract

The glycopeptide CcTx, isolated from the venom of the piscivorous cone snail Conus consors, belongs to the κA-family of conopeptides. These toxins elicit excitotoxic responses in the prey by acting on voltage-gated sodium channels. The structure of CcTx, a first in the κA-family, has been determined by high-resolution NMR spectroscopy together with the analysis of its O-glycan at Ser7. A new type of glycopeptide O-glycan core structure, here registered as core type 9, containing two terminal L-galactose units {α-L-Galp-(1→4)-α-D-GlcpNAc-(1→6)-[α-L-Galp-(1→2)-β-D-Galp-(1→3)-]α-D-GalpNAc-(1→O)}, is highlighted. A sequence comparison to other putative members of the κA-family suggests that O-linked glycosylation might be more common than previously thought. This observation alone underlines the requirement for more careful and in-depth investigations into this type of post-translational modification in conotoxins.

Language: en