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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,{dagger} and D. A. A. Ala'Aldeen{dagger}

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.

* Corresponding author. Mailing address: Division of Microbiology & Infectious Diseases, University Hospital, Queen's Medical Centre, Nottingham NG7 2UH, United Kingdom. Phone: (44) 115 8230753. Fax: (44) 115 970 9233. E-mail: david.turner{at}nottingham.ac.uk.

Editor: J. N. Weiser

{dagger} These authors contributed equally to this work.

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.



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