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Originally published In Press as doi:10.1074/jbc.M509026200 on August 25, 2005

J. Biol. Chem., Vol. 280, Issue 43, 35961-35966, October 28, 2005
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MsbA Is Not Required for Phospholipid Transport in Neisseria meningitidis*

Boris Tefsen1, Martine P. Bos2, Frank Beckers, Jan Tommassen3, and Hans de Cock

From the Department of Molecular Microbiology and Institute of Biomembranes, Utrecht University, 3584 CH Utrecht, The Netherlands

The outer membrane of Gram-negative bacteria contains phospholipids and lipopolysaccharide (LPS) in the inner and outer leaflet, respectively. Little is known about the transport of the phospholipids from their site of synthesis to the outer membrane. The inner membrane protein MsbA of Escherichia coli, which is involved in the transport of LPS across the inner membrane, has been reported to be involved in phospholipid transport as well. Here, we have reported the construction and the characterization of a Neisseria meningitidis msbA mutant. The mutant was viable, and it showed a retarded growth phenotype and contained very low amounts of LPS. However, it produced an outer membrane, demonstrating that phospholipid transport was not affected by the mutation. Notably, higher amounts of phospholipids were produced in the msbA mutant than in its isogenic parental strain, provided that capsular biosynthesis was also disrupted. Although these results confirmed that MsbA functions in LPS transport, they also demonstrated that it is not required for phospholipid transport, at least not in N. meningitidis.


Received for publication, August 16, 2005

* 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 Supported by the Research Council for Earth and Life Sciences with financial aid from the Netherlands Organization for Scientific Research.

2 Supported by the Netherlands Research Council for Chemical Sciences with financial aid from the Netherlands Technology Foundation.

3 To whom correspondence should be addressed: Dept. of Molecular Microbiology and Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands. Tel.: 31-30-2532999; Fax: 31-30-2513655; E-mail: J.P.M.Tommassen{at}bio.uu.nl.


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