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Originally published In Press as doi:10.1074/jbc.M802503200 on May 14, 2008

J. Biol. Chem., Vol. 283, Issue 29, 20342-20349, July 18, 2008
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The LptA Protein of Escherichia coli Is a Periplasmic Lipid A-binding Protein Involved in the Lipopolysaccharide Export Pathway*

An X. Tran{ddagger}, M. Stephen Trent§, and Chris Whitfield, Recipient of a Tier 1 Canada Research Chair{ddagger}1

From the {ddagger}Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario N1G 2W1, Canada and the §Department of Biochemistry and Molecular Biology, Medical College of Georgia, Augusta, Georgia 30912

The LptA protein of Escherichia coli has been implicated in the transport of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. Here we provide evidence that LptA binds structurally diverse LPS substrates in vitro and demonstrate that it interacts specifically with the lipid A domain of LPS. These results are consistent with LptA playing a chaperone role in the transport of LPS across the periplasm and have implications for possible assembly models.


Received for publication, April 1, 2008 , and in revised form, May 12, 2008.

* This work was supported, in whole or in part, by National Institutes of Health Grants RO1-AI064184 and RO1-AI076322 (to M. S. T.). This work was also supported by a grant from the Canadian Institutes of Health Research (to C. W.). 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.

1 To whom correspondence should be addressed: Dept. of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario N1G 2W1, Canada. Tel.: 519-824-4120, ext. 53361; Fax: 519-837-1802; E-mail: cwhitfie{at}uoguelph.ca.


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