PMID:12356789
| Citation |
Ulvatne, H, Haukland, HH, Samuelsen, Ø, Krämer, M and Vorland, LH (2002) Proteases in Escherichia coli and Staphylococcus aureus confer reduced susceptibility to lactoferricin B. J. Antimicrob. Chemother. 50:461-7 |
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| Abstract |
Lactoferricin B is a cationic antimicrobial peptide derived from the N-terminal part of bovine lactoferrin. The effect of bacterial proteases on the antibacterial activity of lactoferricin B towards Escherichia coli and Staphylococcus aureus was investigated using various protease inhibitors and protease-deficient E. coli mutants. Sodium-EDTA, a metalloprotease inhibitor, was the most efficient inhibitors in both species, but combinations of sodium-EDTA with other types of protease inhibitor gave a synergic effect. The results indicate that several groups of proteases are involved in resistance to lactoferricin B in both E. coli and S. aureus. We also report that genetic inactivation of the heat shock-induced serine protease DegP increased the susceptibility to lactoferricin B in E. coli, suggesting that this protease, at least, is involved in reduced susceptibility to lactoferricin B. |
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| Keywords |
Animals; Cattle; Drug Resistance, Bacterial/physiology; Endopeptidases/metabolism; Escherichia coli/drug effects; Escherichia coli/enzymology; Escherichia coli/isolation & purification; Humans; Lactoferrin/analogs & derivatives; Lactoferrin/pharmacology; Protease Inhibitors/pharmacology; Staphylococcus aureus/drug effects; Staphylococcus aureus/enzymology; Staphylococcus aureus/isolation & purification |
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