1. ¹Laboratoire des Venins et Toxines, Institut Pasteur de Tunis, Tunis Belvédère, Tunisie
2. ²CNRS FRE2737, Faculté de Pharmacie, Marseille, France
3. ³CNRS UMR 6560, Boulevard Pierre Dramard, Marseille Cedex, France
4. ⁴Faculté de Médecine de Tunis, Tunis, Tunisie

Correspondence: Dr M Naziha, PhD, Institut Pasteur de Tunis, 13, Place Pasteur-BP.74, Tunis-Belvedere 1002, Tunisie. E-mail: marrakchi_naziha@yahoo.fr

^*These authors contributed equally to this work

Received 5 April 2005; Revised 12 July 2005; Accepted 14 July 2005; Published online 3 October 2005.

Abstract

Lebestatin, a new member of the lysine-threonine-serine (KTS)-disintegrin family, was purified to homogeneity from Tunisian snake (Macrovipera lebetina) venom. It is a single-chain polypeptide composed of 41 amino acids. The amino-acid sequence of lebestatin shows that it displays a pattern of cysteines similar to other short disintegrins, but contains the sequence KTS rather than RGD in its integrin-binding loop. Lebestatin presents a high homology with obtustatin and viperistatin. Lebestatin interacts specifically with the 11 integrin. It was thus able to inhibit both adhesion and migration of PC12 and 11 integrin-expressing CHO cells (CHO-1) to type I and IV collagens. This disintegrin also affected adhesion and migration of endothelial cells and exhibited an anti-angiogenic effect in vivo when using the 8-day-old embryo chick chorioallantoic membrane model.