Characterization of novel cysteine-rich antimicrobial peptides from scorpion blood.
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.
Ehret-Sabatier
L
L
Institut de Biologie Moléculaire et Cellulaire, UPR 9022, CNRS, "Réponse Immunitaire et Développement chez les Insectes," 15, rue René Descartes, 67084 Strasbourg Cedex, France.
Loew
D
D
Goyffon
M
M
Fehlbaum
P
P
Hoffmann
J A
JA
van Dorsselaer
A
A
Bulet
P
P
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000494:pharmacology; D002851:Chromatography, High Pressure Liquid; D003545:Cysteine / Q000032:analysis*; D006458:Hemolymph / Q000737:chemistry*; D006461:Hemolysis / Q000187:drug effects; D013058:Mass Spectrometry; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D010455:Peptides; D012605:Scorpions
D000900:Anti-Bacterial Agents; D010455:Peptides; D003545:Cysteine