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Infection and Immunity, March 2007, p. 1364-1372, Vol. 75, No. 3
0019-9567/07/$08.00+0     doi:10.1128/IAI.01424-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Proteomic Analysis of Outer Membranes and Vesicles from Wild-Type Serogroup B Neisseria meningitidis and a Lipopolysaccharide-Deficient Mutant{triangledown} ,{dagger}

Jeannette N. Williams,1 Paul J. Skipp,2 Holly E. Humphries,1 Myron Christodoulides,1 C. David O'Connor,2 and John E. Heckels1*

Molecular Microbiology Group, Division of Infection Inflammation and Repair, University of Southampton Medical School, Southampton, United Kingdom,1 Centre for Proteomic Research, School of Biological Sciences, University of Southampton, Southampton, United Kingdom2

Received 5 September 2006/ Returned for modification 12 October 2006/ Accepted 30 November 2006

Current experimental vaccines against serogroup B Neisseria meningitidis are based on meningococcal outer membrane (OM) proteins present in outer membrane vesicles (OMV) in which toxic lipopolysaccharide is depleted by detergent extraction. Knowledge of the composition of OM and OMV is essential for developing new meningococcal vaccines based on defined antigens. In the current study, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and nanocapillary liquid chromatography-tandem mass spectrometry were used to investigate the proteomes of OM and OMV from meningococcal strain MC58 and OM from a lipopolysaccharide-deficient mutant. The analysis of OM revealed a composition that was much more complex than the composition that has been reported previously; a total of 236 proteins were identified, only 6.4% of which were predicted to be located in the outer membrane. The most abundant proteins included not only the well-established major OM proteins (PorA, PorB, Opc, Rmp, and Opa) but also other proteins, such as pilus-associated protein Q (PilQ) and a putative macrophage infectivity protein. All of these proteins were also present in OMV obtained by extraction of the OM with deoxycholate. There were markedly increased levels of some additional proteins in OM from the lipopolysaccharide-deficient mutant, including enzymes that contribute to the tricarboxylic acid cycle. In all the preparations, the proteins not predicted to have an OM location were predominantly periplasmic or cytoplasmic or had an unknown location, and relatively few cytoplasmic membrane proteins were detected. However, several proteins that have previously been identified as potential vaccine candidates were not detected in either OM preparations or in OMV. These results have important implications for the development and use of vaccines based on outer membrane proteins.

* Corresponding author. Mailing address: Molecular Microbiology Group, Division of Infection Inflammation and Repair, University of Southampton Medical School, Mailpoint 814, Southampton General Hospital, Southampton SO16 6YD, United Kingdom. Phone: 44 2380 796974. Fax: 44 2380 796992. E-mail: jeh{at}soton.ac.uk.

{triangledown} Published ahead of print on 11 December 2006.

Editor: J. N. Weiser

{dagger} Supplemental material for this article may be found at http://iai.asm.org/.

Infection and Immunity, March 2007, p. 1364-1372, Vol. 75, No. 3
0019-9567/07/$08.00+0     doi:10.1128/IAI.01424-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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