This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Turner, D. P. J. Articles by Ala'Aldeen, D. A. A. Search for Related Content PubMed PubMed Citation Articles by Turner, D. P. J. Articles by Ala'Aldeen, D. A. A.

 Previous Article  |  Next Article 

Infection and Immunity, May 2006, p. 2957-2964, Vol. 74, No. 5
0019-9567/06/$08.00+0     doi:10.1128/IAI.74.5.2957-2964.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Characterization of MspA, an Immunogenic Autotransporter Protein That Mediates Adhesion to Epithelial and Endothelial Cells in Neisseria meningitidis

D. P. J. Turner,^* A. G. Marietou, L. Johnston, K. K. L. Ho, A. J. Rogers, K. G. Wooldridge, and D. A. A. Ala'Aldeen

Molecular Biology and Immunology Group, Institute of Infections, Immunity and Inflammation, School of Molecular Medical Sciences, University Hospital, Queen's Medical Centre, Nottingham NG7 2UH, United Kingdom

Received 21 October 2005/ Returned for modification 9 December 2005/ Accepted 1 February 2006

A novel putative autotransporter protein (NMB1998) was identified in the available genomic sequence of meningococcal strain MC58 (ET-5; ST-32). The mspA gene is absent from the genomic sequences of meningococcal strain Z2491 (ET-IV; ST-4) and the gonococcal strain FA1090. An orthologue is present in the meningococcal strain FAM18 (ET-37; ST-11), but the sequence contains a premature stop codon, suggesting that the protein may not be expressed in this strain. MspA is predicted to be a 157-kDa protein with low cysteine content, and it exhibits 36 and 33% identity to the meningococcal autotransporter proteins immunoglobulin A1 (IgA1) protease and App, respectively. Search of the Pfam database predicts the presence of IgA1 protease and autotransporter ß-barrel domains. MspA was cloned, and a recombinant protein of the expected size was expressed and after being affinity purified was used to raise rabbit polyclonal monospecific antiserum. Immunoblot studies showed that ca. 125- and 95-kDa fragments of MspA are secreted in meningococcal strain MC58, which are absent from the isogenic mutant. Secretion of MspA was shown to be modified in an AspA isogenic mutant. A strain survey showed that MspA is expressed by all ST-32 and ST-41/44 (lineage 3) strains, but none of the ST-8 (A4) strains examined. Sera from patients convalescing from meningococcal disease were shown to contain MspA-specific antibodies. In bactericidal assays, anti-MspA serum was shown to kill the homologous strain (MC58) and another ST-32 strain. Escherichia coli-expressing recombinant MspA was shown to adhere to both human bronchial epithelial cells and brain microvascular endothelial cells.

Editor: J. N. Weiser

These authors contributed equally to this work.

This article has been cited by other articles:

• Takahashi, H., Carlson, R. W., Muszynski, A., Choudhury, B., Kim, K. S., Stephens, D. S., Watanabe, H. (2008). Modification of Lipooligosaccharide with Phosphoethanolamine by LptA in Neisseria meningitidis Enhances Meningococcal Adhesion to Human Endothelial and Epithelial Cells. Infect. Immun. 76: 5777-5789 [Abstract] [Full Text]