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Title: Antibacterial and antifungal properties of alpha-helical, cationic peptides in the venom of scorpions from southern Africa
Authors: Moerman, Leentje
Bosteels, Suzanne
Noppe, Wim
Willems, Jean
Clynen, Elke
Schoofs, Liliane
Thevissen, Karin
Tytgat, Jan
Van Eldere, Johan
Van Der Walt, Jurg
Verdonck, Alfons # ×
Issue Date: Oct-2002
Publisher: Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Series Title: European Journal of Biochemistry vol:269 issue:19 pages:4799-4810
Abstract: Two novel pore-forming peptides have been isolated from the venom of the South-African scorpion Opistophtalmus carinatus. These peptides, designated opistoporin 1 and 2, differ by only one amino acid and belong to a group of alpha-helical, cationic peptides. For the first time, a comparison of the primary structures of alpha-helical pore-forming peptides from scorpion venom was undertaken. This analysis revealed that peptides in the range of 40-50 amino acids contain a typical scorpion conserved sequence S(x)3KxWxS(x)5L. An extensive study of biological activity of synthesized opistoporin 1 and parabutoporin, a pore-forming peptide previously isolated from the venom of the South-African scorpion Parabuthus schlechteri, was undertaken to investigate an eventual cell-selective effect of the peptides. Opistoporin 1 and parabutoporin were most active in inhibiting growth of Gram-negative bacteria (1.3-25 micro m), while melittin and mastoparan, two well-known cytolytic peptides, were more effective against Gram-positive bacteria in the same concentration range. In addition, the peptides showed synergistic activity with some antibiotics commonly used in therapy. Opistoporin 1 and parabutoporin had hemolytic activity intermediate between the least potent mastoparan and the highly lytic melittin. Furthermore, all peptides inhibited growth of fungi. Experiments with SYTOX green suggested that this effect is related to membrane permeabilization.
URI: 
ISSN: 0014-2956
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Faculty of Medicine - miscellaneous
Laboratory of Clinical Bacteriology and Mycology
Faculty of Medicine, Campus Kulak Kortrijk
Animal Physiology and Neurobiology Section - miscellaneous
Centre of Microbial and Plant Genetics
Toxicology and Pharmacology
Laboratory of Molecular Bacteriology (Rega Institute)
Interdisciplinary Research Facility Life Sciences, Campus Kulak Kortrijk
Department of Microbiology & Immunology - miscellaneous
Microbiology and Immunology, Campus Kulak Kortrijk
× corresponding author
# (joint) last author

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