Novel alpha D-conopeptides and their precursors identified by cDNA cloning define the D-conotoxin superfamily

Loughnan, Marion L., Nicke, Annette, Lawrence, Nicole and Lewis, Richard J. (2009) Novel alpha D-conopeptides and their precursors identified by cDNA cloning define the D-conotoxin superfamily. Biochemistry, 48 17: 3717-3729. doi:10.1021/bi9000326


Author Loughnan, Marion L.
Nicke, Annette
Lawrence, Nicole
Lewis, Richard J.
Title Novel alpha D-conopeptides and their precursors identified by cDNA cloning define the D-conotoxin superfamily
Formatted title
Novel αD-conopeptides and their precursors identified by cDNA cloning define the D-conotoxin superfamily
Journal name Biochemistry   Check publisher's open access policy
ISSN 0006-2960
1520-4995
1943-295X
ISBN 978-3-527-33465-0
Publication date 2009-05-05
Year available 2014
Sub-type Article (original research)
DOI 10.1021/bi9000326
Open Access Status
Volume 48
Issue 17
Start page 3717
End page 3729
Total pages 13
Editor Richard N. Armstrong
Place of publication Washington , DC, U.S.A.
Publisher American Chemical Society
Language eng
Subject C1
970106 Expanding Knowledge in the Biological Sciences
1101 Medical Biochemistry and Metabolomics
110106 Medical Biochemistry: Proteins and Peptides (incl. Medical Proteomics)
Abstract alpha D-Conotoxins are peptide inhibitors of nicotinic acetylcholine receptors (nAChRs) first described from Conus vexillum (alpha D-VxXIIA-C and renamed here to alpha D-VxXXA, alpha D-VxXXB, and alpha D-VxXXC). In this study, we report cDNA sequences encoding D-superfamily conopeptides identified in the Clade XII Conidae Conus vexillum, Conus capitaneus, Conus mustelinus, and Conus miles, together with partial sequences of corresponding peptides from this family. The D-superfamily signal peptide sequences display greater heterogeneity than reported for other conotoxin superfamilies. Phylogenetic analysis of the relationships among alpha D-conotoxin precursors reveals two distinct groups containing either an EMM or AVV signal peptide sequence motif. Homodimer and heterodimer combinations of predicted mature toxin sequences likely account for the partial amino acid sequences and mass values observed for several of the native dimeric peptide components identified in C. capitaneus, C. miles, and C. mustelinus venom. The discovery of the precursors and several novel conotoxins from different species defines this large conotoxin family and expands our understanding of sequence diversification mechanisms in Conus species.
Formatted abstract
αD-Conotoxins are peptide inhibitors of nicotinic acetylcholine receptors (nAChRs) first described from Conus vexillum (αD-VxXIIA−C and renamed here to αD-VxXXA, αD-VxXXB, and αD-VxXXC). In this study, we report cDNA sequences encoding D-superfamily conopeptides identified in the Clade XII Conidae Conus vexillum, Conus capitaneus, Conus mustelinus, and Conus miles, together with partial sequences of corresponding peptides from this family. The D-superfamily signal peptide sequences display greater heterogeneity than reported for other conotoxin superfamilies. Phylogenetic analysis of the relationships among αD-conotoxin precursors reveals two distinct groups containing either an EMM or AVV signal peptide sequence motif. Homodimer and heterodimer combinations of predicted mature toxin sequences likely account for the partial amino acid sequences and mass values observed for several of the native dimeric peptide components identified in C. capitaneus, C. miles, and C. mustelinus venom. The discovery of the precursors and several novel conotoxins from different species defines this large conotoxin family and expands our understanding of sequence diversification mechanisms in Conus species.
Keyword Nicotinic acetylcholine-receptor
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: 2010 Higher Education Research Data Collection
ERA 2012 Admin Only
Institute for Molecular Bioscience - Publications
 
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Created: Thu, 03 Sep 2009, 18:14:52 EST by Mr Andrew Martlew on behalf of Institute for Molecular Bioscience