Premium
Aah VI, a novel, N ‐glycosylated anti‐insect toxin from Androctonus australis hector scorpion venom: isolation, characterisation, and glycan structure determination
Author(s) -
Hassani O,
Loew D,
Van Dorsselaer A,
Papandréou M.J,
Sorokine O,
Rochat H,
Sampieri F,
Mansuelle P
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01710-4
Subject(s) - venom , scorpion , edman degradation , glycan , toxin , neurotoxin , biology , amino acid , antivenom , biochemistry , chemistry , peptide sequence , glycoprotein , gene
Aah VI was isolated from the venom of the North African scorpion, Androctonus australis hector . It is the first glycosylated neurotoxin from scorpion venom to be described. It was not toxic to mice, when injected intracerebroventricularly at a dose of 1.2 μg per animal. However, it had typical activity in Blatella germanica cockroaches resulting in gradual paralysis and very low toxicity (LD 50 =8.5 μg/g of animal). It consists of 66 amino acid residues and is heterogeneously N ‐glycosylated at a single site, on asparagine 9, of the Asn‐Gly‐Thr sequence. The potential N ‐glycosylation site was deduced from automatic Edman degradation and amino acid analysis, and glycan heterogeneity was evidenced by ESMS. Determination of the N ‐glycan structures (dHex, Hex and HexNAc) was assessed by nanoESMS/MS with picomolar amounts of sample. Current knowledge of N ‐glycan structure and composition suggests that the glycan structures are derived from a common core.