Details

Autor(en) / Beteiligte

• Cociancich, S.
• Goyffon, M.
• Bontems, F.
• Bulet, P.
• Bouet, F.
• Menez, A.
• Hoffmann, J.

Titel

Purification and Characterization of a Scorpion Defensin, a 4kDa Antibacterial Peptide Presenting Structural Similarities with Insect Defensins and Scorpion Toxins

Ist Teil von

• Biochemical and biophysical research communications, 1993-07, Vol.194 (1), p.17-22

Ort / Verlag

San Diego, CA: Elsevier Inc

Erscheinungsjahr

1993

Quelle

Elsevier Journal Backfiles on ScienceDirect (DFG Nationallizenzen)

Beschreibungen/Notizen

• Insect defensins are a group of inducible small-sized antibacterial peptides with three intramolecular disulfide bridges. NMR studies have recently shown that they share striking structural similarities with scorpion toxins. We have investigated in a scorpion species, Leiurus quinquestriatus, the potential presence of antibacterial molecules and report the isolation and structural characterization of a novel insect defensin homologue, which we refer to as scorpion defensin. This peptide shows a remarkably high degree of sequence homology with a defensin recently characterized in a species belonging to the ancient insect order of the Odonata with which it defines a novel ancient subclass of defensins. The scorpion defensin has in common with the scorpion toxins a consensus sequence Cys-[...]-Cys-Xaa-Xaa-Xaa-Cys-[...]-Gly-Xaa-Cys-[...]-Cys-Xaa-Cys present in all scorpion toxins characterized so far.