JAC Advance Access originally published online on September 6, 2002
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Journal of Antimicrobial Chemotherapy (2002) 50, 461-467
© 2002 The British Society for Antimicrobial Chemotherapy
Proteases in Escherichia coli and Staphylococcus aureus confer reduced susceptibility to lactoferricin B
1 Department of Medical Microbiology, University Hospital of North Norway; 2 Department of Microbiology, University of Tromsø, Norway
Received 12 November 2001; returned 21 January 2002; revised 14 June 2002; accepted 21 June 2002
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.
* Correspondence address. H. Ulvatne Marthinsen, Department of Medical Microbiology, PO Box 56, N-9038 University Hospital of North Norway, Norway. Tel: +47-77-62-82-65; Fax: +47-77-62-70-15; E-mail: hilde.ulvatne{at}rito.no
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