A novel M-superfamily conotoxin with a unique motif from Conus vexillum.
Cone snails are tropical marine mollusks that envenomate prey with a complex mixture of neuropharmacologically active compounds for the purpose of feeding and defence, each evolved to act in a highly specific manner on different parts of the nervous system. Here, we report the peptide purification, molecular cloning, chemical synthesis, and functional characterization of a structurally unique toxin isolated from the venom of Conus vexillum. The novel peptide, designated Vx2, was composed of 21 amino acid residues cross-linked by 3 disulfide bonds (WIDPSHYCCCGGGCTDDCVNC). Intriguingly, its mature peptide sequence shows low level of similarity with other identified conotoxins, and its unique motif (-CCCGGGC-) was not reported in other Conus peptides. However, its signal peptide sequence shares high similarity with those of the M-superfamily conotoxins. Hence, Vx2 could be classified into a new family of the M-superfamily.
Jiang
Hui
H
Shanghai Institute of Biochemistry and Cell Biology, Shanghai Institute of Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
Wang
Cheng-Zhong
CZ
Xu
Chen-Qi
CQ
Fan
Chong-Xu
CX
Dai
Xian-Dong
XD
Chen
Ji-Sheng
JS
Chi
Cheng-Wu
CW
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D020916:Conotoxins / Q000737:chemistry* / Q000145:classification* / Q000235:genetics / Q000302:isolation & purification; D052078:Conus Snail / Q000737:chemistry* / Q000235:genetics; D018076:DNA, Complementary / Q000235:genetics; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D020916:Conotoxins; D018076:DNA, Complementary