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Journal of Bacteriology, August 1998, p. 4002-4006, Vol. 180, No. 15
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Identification of OmpT as the Protease That Hydrolyzes the Antimicrobial Peptide Protamine before It Enters Growing Cells of Escherichia coli

Stefan Stumpe,1,dagger Roland Schmid,1 Daren L. Stephens,2 George Georgiou,2 and Evert P. Bakker1,*

Abteilung Mikrobiologie, Universität Osnabrück, D-49069 Osnabrück, Germany,1 and Department of Chemical Engineering, The University of Texas at Austin, Austin, Texas 78712-10622

Received 8 September 1997/Accepted 27 May 1998

The influence of extracytoplasmic proteases on the resistance of Escherichia coli to the antimicrobial peptide protamine was investigated by testing strains with deletions in the protease genes degP, ptr, and ompT. Only Delta ompT strains were hypersusceptible to protamine. This effect was abolished by plasmids carrying ompT. Both at low and at high Mg2+ concentrations, ompT+ strains cleared protamine from the medium within a few minutes. By contrast, at high Mg2+ concentrations, protamine remained present for at least 1 h in the medium of an ompT strain. These data indicate that OmpT is the protease that degrades protamine and that it exerts this function at the external face of the outer membrane.

* Corresponding author. Mailing address: Abteilung Mikrobiologie, Universität Osnabrück, Barbarastraße 11, D-49069 Osnabrück, Germany. Phone: 49-541-9692855. Fax: 49-541-9692870. E-mail: bakker_e{at}sfbbio1.biologie.uni-osnabrueck.de.

dagger Present address: Institut für Molekulare Biotechnologie, Abteilung Strukturbiologie/Kristallographie, Arbeitsgruppe Physikalische DNA-Analytik, 07745 Jena, Germany.

Journal of Bacteriology, August 1998, p. 4002-4006, Vol. 180, No. 15
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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