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Journal of Bacteriology, December 2009, p. 7243-7252, Vol. 191, No. 23
0021-9193/09/$08.00+0     doi:10.1128/JB.00688-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

A Protein Important for Antimicrobial Peptide Resistance, YdeI/OmdA, Is in the Periplasm and Interacts with OmpD/NmpC{triangledown}

M. Carolina Pilonieta,1,{dagger} Kimberly D. Erickson,1,{dagger} Robert K. Ernst,2 and Corrella S. Detweiler1*

Department of Molecular, Cellular, and Developmental Biology, University of Colorado at Boulder, Boulder, Colorado 80309,1 University of Maryland-Baltimore, Department of Microbial Pathogenesis, School of Dentistry, Baltimore, Maryland 212012

Received 27 May 2009/ Accepted 10 September 2009

Antimicrobial peptides (AMPs) kill or prevent the growth of microbes. AMPs are made by virtually all single and multicellular organisms and are encountered by bacteria in diverse environments, including within a host. Bacteria use sensor-kinase systems to respond to AMPs or damage caused by AMPs. Salmonella enterica deploys at least three different sensor-kinase systems to modify gene expression in the presence of AMPs: PhoP-PhoQ, PmrA-PmrB, and RcsB-RcsC-RcsD. The ydeI gene is regulated by the RcsB-RcsC-RcsD pathway and encodes a 14-kDa predicted oligosaccharide/oligonucleotide binding-fold (OB-fold) protein important for polymyxin B resistance in broth and also for virulence in mice. We report here that ydeI is additionally regulated by the PhoP-PhoQ and PmrA-PmrB sensor-kinase systems, which confer resistance to cationic AMPs by modifying lipopolysaccharide (LPS). ydeI, however, is not important for known LPS modifications. Two independent biochemical methods found that YdeI copurifies with OmpD/NmpC, a member of the trimeric β-barrel outer membrane general porin family. Genetic analysis indicates that ompD contributes to polymyxin B resistance, and both ydeI and ompD are important for resistance to cathelicidin antimicrobial peptide, a mouse AMP produced by multiple cell types and expressed in the gut. YdeI localizes to the periplasm, where it could interact with OmpD. A second predicted periplasmic OB-fold protein, YgiW, and OmpF, another general porin, also contribute to polymyxin B resistance. Collectively, the data suggest that periplasmic OB-fold proteins can interact with porins to increase bacterial resistance to AMPs.

* Corresponding author. Mailing address: Department of Molecular, Cellular, and Developmental Biology, 347 UCB, University of Colorado at Boulder, Boulder, CO 80309. Phone: (303) 735-2956. Fax: (303) 492-7744. E-mail: detweile{at}colorado.edu

{triangledown} Published ahead of print on 18 September 2009.

{dagger} M.C.P. and K.D.E. contributed equally to this study.

Journal of Bacteriology, December 2009, p. 7243-7252, Vol. 191, No. 23
0021-9193/09/$08.00+0     doi:10.1128/JB.00688-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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