Isolation and characterisation of conomap-Vt, a D-amino acid containing excitatory peptide from the venom of a vermivorous cone snail

Dutertre, S., Lumsden, N. G., Alewood, P. F. and Lewis, R. J. (2006) Isolation and characterisation of conomap-Vt, a D-amino acid containing excitatory peptide from the venom of a vermivorous cone snail. Febs Letters, 580 16: 3860-3866. doi:10.1016/j.febslet.2006.06.011


Author Dutertre, S.
Lumsden, N. G.
Alewood, P. F.
Lewis, R. J.
Title Isolation and characterisation of conomap-Vt, a D-amino acid containing excitatory peptide from the venom of a vermivorous cone snail
Journal name Febs Letters   Check publisher's open access policy
ISSN 0014-5793
Publication date 2006
Sub-type Article (original research)
DOI 10.1016/j.febslet.2006.06.011
Volume 580
Issue 16
Start page 3860
End page 3866
Total pages 7
Editor Felix Wieland
Patricia McCabe
Tine Walma
Place of publication Amsterdam
Publisher Elsevier Science Bv
Collection year 2006
Language eng
Subject C1
780103 Chemical sciences
320305 Medical Biochemistry - Proteins and Peptides
Abstract Cone snail venom is a rich source of bioactives, in particular small disulfide rich peptides that disrupt synaptic transmission. Here, we report the discovery of conomap-Vt (Conp-Vt), an unusual linear tetradecapeptide isolated from Conus vitulinus venom. The sequence displays no homology to known conopeptides, but displays significant homology to peptides of the MATP (myoactive tetradecapeptide) family, which are important endogenous neuromodulators in molluscs, annelids and insects. Conp-Vt showed potent excitatory activity in several snail isolated tissue preparations. Similar to ACh, repeated doses of Conp-Vt were tachyphylactic. Since nicotinic and muscarinic antagonists failed to block its effect and Conp-Vt desensitised tissue remained responsive to ACh, it appears that Conp-Vt contractions were non-cholinergic in origin. Finally, biochemical studies revealed that Conp-Vt is the first member of the MATP family with a D-amino acid. Interestingly, the isomerization of L-Phe to D-Phe enhanced biological activity, suggesting that this post-translational modified conopeptide may have evolved for prey capture. (c) 2006 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
Keyword Cone Snail
Conotoxin
Venom Peptide
Post-translational Modification
Molusc Selective Bioactive
Biochemistry & Molecular Biology
Biophysics
Cell Biology
Eisenia-foetida
Platypus Venom
Tetradecapeptide
Residue
Neuropeptides
Isomerization
Contraction
Conotoxins
Contryphan
Earthworm
Q-Index Code C1
Institutional Status UQ

 
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Created: Wed, 15 Aug 2007, 08:52:17 EST