Table 1.
Species type | Clade | Conus species | δ-Conotoxin (ref.) | Amino acid sequence |
Worm-hunting | * * * ** * | |||
Tesseliconus | C. tessulatus | TsVIA | CAAFGSFCGL-PGLVDCCSGRCFIVCLL | |
C. eburneus | ErVIA | CAGIGSFCGL-PGLVDCCSGRCFIVCLP | ||
Fish-hunting | * * ** ** * | |||
Chelyconus | C. purpurascens | PVIA (33) | EACYAOGTFCGIKOGL- -CCSEFCLPGVCFG# | |
C. ermineus | EVIA (35) | EACYPOGTFCGIKOGL- -CCSELCLPAVCVG# | ||
Pionoconus | C. striatus | SVIE (44) | DGCSSGGTFCGIHOGL- -CCSEFCFLWCITFID | |
C. magus | MVIA (34) | DGCYNAGTFCGIROGL- -CCSEFCFLWCITFVDS# | ||
C. consors | CnVIA (34) | YECYSTGTFCGINGGL- -CCSNLCLFFVCLTFS | ||
C. aurisiacus | AVIA (34) | DGCSNAGAFCGIHOGL- -CCSEICIVWCT | ||
Mollusc-hunting | * | |||
Cylinder | C. textile | TxVIA (31) | WCKQSGEMCNLLDQN- -CCDGYCIVLVCT | |
C. gloriamaris | GmVIA (45) | VKPCRKEGQLCDPIFQN- -CCRGWNCVLFCV |
The bold-font “C”s represent the cysteine amino acids that form the disulfide bonding framework of these delta conotoxin peptides. Asterisks represent conserved (non-Cys) amino acids within δ-conotoxins from fish-hunting cone snails. Underlining indicates conserved amino acids and conservative amino acid changes (similar biochemical properties) between worm hunters and fish hunters. All amino acid sequences were determined from peptides purified from venom, with the exceptions of MVIA and AVIA, which were determined by molecular cloning of the genes encoding these peptides. # indicates an amidated C terminus. O, hydroxyproline. Each dash is for alignment of conserved amino acids.