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JAC Advance Access published online on September 6, 2002
Journal of Antimicrobial Chemotherapy, doi:10.1093/jac/dkf156
© 2002 by The British Society for Antimicrobial Chemotherapy
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© 2002 The British Society for Antimicrobial Chemotherapy

Original Paper

Proteases in Escherichia coli and Staphylococcus aureus confer reduced susceptibility to lactoferricin B

Hilde Ulvatne 1*, Hanne Husom Haukland 1, Ørjan Samuelsen 2, Manuela Krämer 2, Lars H. Vorland 1

1 Department of Medical Microbiology, University Hospital of North Norway; Department of Microbiology, University of Tromsø, Norway
2 Department of Medical Microbiology, University Hospital of North Norway

* Corresponding author. E-mail: hilde.ulvatne{at}rito.no.

Received 12 November 2001 ; revised 14 June 2002 ; accepted 21 June 2002

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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