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Volume 271, Number 47, Issue of November 22, 1996 pp. 29537-29544
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Characterization of Novel Cysteine-rich Antimicrobial Peptides from Scorpion Blood

(Received for publication, July 16, 1996, and in revised form, September 9, 1996)

Laurence Ehret-Sabatier , Damarys Loew ^§ , Max Goyffon ^¶ , Pascale Fehlbaum , Jules A. Hoffmann , Alain van Dorsselaer ^§ and Philippe Bulet

From the  Institut de Biologie Moléculaire et Cellulaire, UPR 9022, CNRS, "Réponse Immunitaire et Développement chez les Insectes," 15, rue René Descartes, 67084 Strasbourg Cedex, France, the ^§ Laboratoire de Spectrométrie de Masse Bio-Organique, URA 31, CNRS-Université Louis Pasteur, Faculté de Chimie, 1, rue Blaise Pascal, 67008 Strasbourg Cedex, France, and the ^¶ Muséum National d'Histoire Naturelle et Division de Biologie Générale et Ecologie, "Laboratoire d'Etudes et de Recherches sur les Arthropodes Irradiés," 57, rue Cuvier, 75005 Paris, France

We have isolated, from the hemolymph of unchallenged scorpions of the species Androctonus australis, three distinct antimicrobial peptides, which we have fully characterized by Edman degradation, electrospray ionization mass spectrometry, and matrix-assisted laser desorption/ionization mass spectrometry. Two are novel molecules: (i) androctonin, a 25-residue peptide with two disulfide bridges, active against both bacteria (Gram-positive and Gram-negative) and fungi and showing marked sequence homology to tachyplesins and polyphemusins from horseshoe crabs; and (ii) buthinin, a 34-residue antibacterial (Gram-positive and Gram-negative) peptide with three disulfide bridges. The third peptide contains 37 residues and three disulfide bridges and clearly belongs to the family of anti-Gram-positive insect defensins. We have synthesized androctonin and explored its activity spectrum and mode of action.

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