Identification of OmpT as the protease that hydrolyzes the antimicrobial peptide protamine before it enters growing cells of Escherichia coli

被引:178
作者
Stumpe, S
Schmid, R
Stephens, DL
Georgiou, G
Bakker, EP
机构
[1] Univ Osnabruck, Abt Mikrobiol, D-49069 Osnabruck, Germany
[2] Univ Texas, Dept Chem Engn, Austin, TX 78712 USA
关键词
D O I
10.1128/JB.180.15.4002-4006.1998
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
引用
收藏
页码:4002 / 4006
页数:5
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