In Vitro Antimicrobial Properties of Recombinant ASABF, an Antimicrobial Peptide Isolated from the Nematode Ascaris suum
- 1 October 2000
- journal article
- research article
- Published by American Society for Microbiology in Antimicrobial Agents and Chemotherapy
- Vol. 44 (10) , 2701-2705
- https://doi.org/10.1128/aac.44.10.2701-2705.2000
Abstract
ASABF is a CSαβ-type antimicrobial peptide that contains four intramolecular disulfide bridges (Y. Kato and S. Komatsu, J. Biol. Chem. 271:30493–30498, 1996). In the present study, a recombinant ASABF was produced by using a yeast expression system, and its antimicrobial activity was characterized in detail. The recombinant ASABF was active against all gram-positive bacteria tested (7 of 7; minimum bactericidal concentration [MBC], 0.03 to 1 μg/ml) exceptLeuconostoc mesenteroides, some gram-negative bacteria (8 of 14; MBC, >0.5 μg/ml), and some yeasts (3 of 9; MBC >3 μg/ml). Slight hemolytic activity (4.2% at 100 μg/ml) against human erythrocytes was observed only under low-ionic-strength conditions. Less than 1 min of contact was enough to kill Staphylococcus aureus ATCC 6538P. The bactericidal activity against S. aureus was inhibited by salts.Keywords
This publication has 22 references indexed in Scilit:
- Insect ImmunityJournal of Biological Chemistry, 1999
- Plant defense peptidesBiopolymers, 1998
- Solution structure of drosomycin, the first inducible antifungal protein from insectsProtein Science, 1997
- Subtilases: The superfamily of subtilisin-like serine proteasesProtein Science, 1997
- Characterization of Novel Cysteine-rich Antimicrobial Peptides from Scorpion BloodJournal of Biological Chemistry, 1996
- Plant Defensins: Novel Antimicrobial Peptides as Components of the Host Defense SystemPlant Physiology, 1995
- Isolation and characterisation of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and SaxifragaceaeFEBS Letters, 1995
- Refined three-dimensional solution structure of insect defensin AStructure, 1995
- Purification and Characterization of a Scorpion Defensin, a 4kDa Antibacterial Peptide Presenting Structural Similarities with Insect Defensins and Scorpion ToxinsBiochemical and Biophysical Research Communications, 1993
- 1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecinFEBS Letters, 1990