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Identification of cptA, a PmrA-Regulated Locus Required for Phosphoethanolamine Modification of the Salmonella enterica Serovar Typhimurium Lipopolysaccharide Core

R. Tamayo,^1, B. Choudhury,² A. Septer,³ M. Merighi,³ R. Carlson,² and J. S. Gunn^3*

Department of Microbiology and Immunology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Dr., MC 7758, San Antonio, Texas 78229-3900,¹ Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602,² Department of Molecular Virology, Immunology and Medical Genetics, Department of Medicine, Division of Infectious Diseases, and The Center for Microbial Interface Biology, Ohio State University, Columbus, Ohio 43210³

Received 15 December 2004/ Accepted 8 February 2005

In response to the in vivo environment, the Salmonella enterica serovar Typhimurium lipopolysaccharide (LPS) is modified. These modifications are controlled in part by the two-component regulatory system PmrA-PmrB, with the addition of 4-aminoarabinose (Ara4N) to the lipid A and phosphoethanolamine (pEtN) to the lipid A and core. Here we demonstrate that the PmrA-regulated STM4118 (cptA) gene is necessary for the addition of pEtN to the LPS core. pmrC, a PmrA-regulated gene necessary for the addition of pEtN to lipid A, did not affect core pEtN addition. Although imparting a similar surface charge modification as Ara4N, which greatly affects polymyxin B resistance and murine virulence, neither pmrC nor cptA plays a dramatic role in antimicrobial peptide resistance in vitro or virulence in the mouse model. Therefore, factors other than surface charge/electrostatic interaction contribute to resistance to antimicrobial peptides such as polymyxin B.

Current address: Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111.

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