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Monoclonal antibodies neutralizing the toxin II from Androctonus australis hector scorpion venom: usefulness of a synthetic, non‐toxic analog
Author(s) -
Devaux Christiane,
Clot-Faybesse Olivier,
Juin Marianick,
Mabrouk Kamel,
Sabatier Jean-Marc,
Rochat Hervé
Publication year - 1997
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(97)00826-0
Subject(s) - venom , toxin , scorpion , scorpion venoms , monoclonal antibody , scorpion toxin , epitope , neutralization , chemistry , antivenom , biology , antibody , biochemistry , immunology
Scorpion venom contains toxins that act on ion channels. Some are responsible for the noxious effects observed when people are stung by scorpions. The study of the neutralization of these molecules and the production of monoclonal antibodies (mAbs) should prove valuable. Toxin II from Androctonus australis hector scorpion (AahII) is one of the most potent toxins and has been well‐characterized and studied. Producing mAbs against such molecules is often difficult due to their toxicity. We used a synthetic, non‐toxic analog, (Abu) 8 ‐AahII, to obtain mAbs which recognize and neutralize the native toxin AahII. Sets of peptides spanning the entire sequence of AahII were assayed to identify the binding sites of the mAbs. The various mAbs recognized only the largest peptides (12–17 residues). They recognized peptides corresponding to different parts of the AahII sequence, suggesting that several regions of the (Abu) 8 ‐AahII sequence mimic AahII epitopes and then elicit mAbs directed against toxin.