Aah VI, a novel, N‐glycosylated anti‐insect toxin from Androctonus australis hector scorpion venom: isolation, characterisation, and glycan structure determination

FEBS Letters

Papandréou, M.J²  Sampieri, F²  Loew, D¹  Sorokine, O¹  Rochat, H²  Hassani, O²  Mansuelle, P²  Van Dorsselaer, A¹ 

[1] UMR 7509, Laboratoire de Spectrométrie de Masse Bio-Organique associé au CNRS, Université Louis Pasteur, 1 rue B. Pascal, 67008 Strasbourg, France;UMR 6560, Université de la Méditerranée CNRS, Laboratoire de Biochimie, Ingénierie des Protéines, IFR Jean Roche, Faculté de Médecine Secteur Nord, Bd P. Dramard, 13916 Marseille Cedex 20, France

关键词: Scorpion toxin;    N-Glycosylation;    Mass spectrometry;    High-performance liquid chromatography;    Hex;    hexose;    dHex;    deoxyhexose;    HexNAc;    N-acetylhexosamine;    NeuAc;    N-acetylneuraminic acid;    ESMS;    electrospray mass spectrometry;    ESMS/MS;    electrospray tandem mass spectrometry;    ICV;    intracerebroventricular;    PEC;    pyridylethyl-cysteine;    RCM;    reduced and S-carboxymethylated;    RPE;    reduced and S-pyridyl-ethylated;    PLA2;    phospholipase A2;    RP-HPLC;    reverse-phase high-performance liquid chromatography;    LC-MS;    liquid chromatography mass spectrometry;    TFA;    trifluoroacetic acid;    Tris;    tris-(hydroxymethyl)-aminomethane;    RT;    retention time;    SIR;    single ion recording;    LD50;    lethal dose for 50% of the tested animals;   

DOI  :  10.1016/S0014-5793(98)01710-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 (LD₅₀=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.

【 授权许可】

Unknown