TY - JOUR
T1 - Structure of the O-Glycosylated Conopeptide CcTx from Conus consors Venom
AU - Hocking, H.G.
AU - Gerwig, G.J.
AU - Dutertre, S.
AU - Violette, A.
AU - Favreau, P.
AU - Stöcklin, R.
AU - Kamerling, J.P.
AU - Boelens, R.
PY - 2013
Y1 - 2013
N2 - The glycopeptide CcTx, isolated
from the venom of the piscivorous
cone snail Conus consors, belongs
to the kA-family of conopeptides.
These toxins elicit excitotoxic re-
ACHTUNGTRENUNGsponses in the prey by acting on voltage-
gated sodium channels. The structure
of CcTx, a first in the kA-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 {a-l-Galp-(1!4)-a-d-
GlcpNAc-(1!6)-[a-l-Galp-(1!2)-b-d-
Galp-(1!3)-]a-d-GalpNAc-(1!O)}, is
highlighted. A sequence comparison to
other putative members of the kAfamily
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.
AB - The glycopeptide CcTx, isolated
from the venom of the piscivorous
cone snail Conus consors, belongs
to the kA-family of conopeptides.
These toxins elicit excitotoxic re-
ACHTUNGTRENUNGsponses in the prey by acting on voltage-
gated sodium channels. The structure
of CcTx, a first in the kA-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 {a-l-Galp-(1!4)-a-d-
GlcpNAc-(1!6)-[a-l-Galp-(1!2)-b-d-
Galp-(1!3)-]a-d-GalpNAc-(1!O)}, is
highlighted. A sequence comparison to
other putative members of the kAfamily
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.
U2 - 10.1002/chem.201202713
DO - 10.1002/chem.201202713
M3 - Article
SN - 0947-6539
VL - 19
SP - 870
EP - 879
JO - Chemistry-A European Journal
JF - Chemistry-A European Journal
IS - 3
ER -