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J. Biol. Chem., Vol. 280, Issue 9, 8248-8259, March 4, 2005
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¶
From the
Department of Molecular Microbiology, Utrecht University, Padualaan 8, Utrecht 3584 CH, The Netherlands, the Netherlands Vaccine Institute, P. O. Box 457, Bilthoven 3720 AL, The Netherlands, the ||Laboratory of Immunotherapy, University Medical Center, P. O. Box 85090, Utrecht 3508 AB, The Netherlands, and the **Laboratory of Organic-Analytical Chemistry, National Institute of Public Health and the Environment, P. O. Box 1, Bilthoven 3720 BA, The Netherlands
Lipopolysaccharide (LPS) is one of the main constituents of the Gram-negative bacterial outer membrane. It usually consists of a highly variable O-antigen, a less variable core oligosaccharide, and a highly conserved lipid moiety, designated lipid A. Several bacteria are capable of modifying their lipid A architecture in response to external stimuli. The outer membrane-localized lipid A 3-O-deacylase, encoded by the pagL gene of Salmonella enterica serovar Typhimurium, removes the fatty acyl chain from the 3 position of lipid A. Although a similar activity was reported in some other Gram-negative bacteria, the corresponding genes could not be identified. Here, we describe the presence of pagL homologs in a variety of Gram-negative bacteria. Although the overall sequence similarity is rather low, a conserved domain could be distinguished in the C-terminal region. The activity of the Pseudomonas aeruginosa and Bordetella bronchiseptica pagL homologs was confirmed upon expression in Escherichia coli, which resulted in the removal of an R-3-hydroxymyristoyl group from lipid A. Upon deacylation by PagL, E. coli lipid A underwent another modification, which was the result of the activity of the endogenous palmitoyl transferase PagP. Furthermore, we identified a conserved histidine-serine couple as active site residues, suggesting a catalytic mechanism similar to serine hydrolases. The biological function of PagL remains unclear. However, because PagL homologs were found in both pathogenic and nonpathogenic species, PagL-mediated deacylation of lipid A probably does not have a dedicated role in pathogenicity.
Received for publication, December 17, 2004
* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
¶ To whom correspondence should be addressed: Dept. of Molecular Microbiology, Utrecht University, Padualaan 8, Utrecht 3584 CH, The Netherlands. Tel.: 31-30-253-2592; Fax: 31-30-253-2837; E-mail: j.j.g.geurtsen{at}bio.uu.nl.
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