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Journal of Endotoxin Research, Vol. 11, No. 1, 57-61 (2005)
DOI: 10.1177/09680519050110010101

Purification and characterization of deacylated and/or palmitoylated lipid A species unique to Salmonella enterica serovar Typhimurium

Kiyoshi Kawasaki

Department of Microbiology, University of Washington, Seattle, Washington, USA, kawa{at}nih.go.jp

Robert K. Ernst

Department of Medicine, University of Washington, Seattle, Washington, USA

Samuel I. Miller

Department of Microbiology, University of Washington, Seattle, Washington, USA, Department of Genome Sciences, University of Washington, Seattle, Washington, USA

The Salmonella enterica serovar Typhimurium virulence gene products PhoP/PhoQ sense host microenvironments to regulate the expression of a lipid A 3-O-deacylase, PagL, and a lipid A palmitoyltransferase, PagP. Therefore, deacylation and/or palmitoylation of lipid A could occur in Salmonellae adapted to host environments. The PhoP/PhoQ-regulated modification of lipid A alters host recognition and signaling, and may play an important role in host defense against Salmonellae infection. Here we report the purification and characterization of modified lipid A species. Deacylated lipid A, deacylated and palmitoylated lipid A, and palmitoylated lipid A species were generated in Escherichia coli cells heterologously expressing salmonellae PagL and/or PagP, and then purified by sequential thin-layer chromatography. The purified lipid A species showed m/z values that correspond to single lipid A species on mass spectrometry analysis. The modified lipid A species showed reduced ability to induce cellular signaling through Toll-like receptor 4, suggesting a specific function of the lipid A modifications in the pathogenesis of salmonellae infection.

Key Words: Deacylated lipid A • palmitoylated lipid A • Salmonella enterica serovar Typhimurium


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