Open AccessPurification, characterization and molecular modelling of two toxin‐like proteins from the Androctonus australis Hector venom
Author(s) -
SrairiAbid Najet,
Mansuelle Pascal,
Mejri Thouraya,
Karoui Habib,
Rochat Hervé,
Sampieri François,
El Ayeb Mohamed
Publication year - 2000
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.2000.01632.x
Subject(s) - venom , edman degradation , scorpion , toxin , scorpion venoms , biology , amino acid , biochemistry , peptide sequence , chemistry , gene
Two toxin‐like proteins (AahTL1 and AahTL3) were purified from the venom of the scorpion Androctonus australis Hector (Aah). AahTL1 and AahTL3 are the first non toxic proteins cross‐reacting with AahI toxins group which indicates that these proteins can be used as a model of vaccins. In order to study structure‐function relationships, their complete amino‐acid sequences (66 residues) were determined, by automated Edman degradation. They show more than 50% of similarity with both AahI and AahIII antimammal toxins. Three‐dimensional structural models of AahTL1 and AahTL3 constructed by homology suggest that the two proteins are structurally similar to antimammal scorpion α‐toxins specific to voltage dependent Na + channels. The models showed also that amino‐acid changes between potent Aah toxins and both AahTL1 and AahTL3 disrupt the electrostatic potential gradient at their surface preventing their interaction with the receptor, which may explain their non toxicity.