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Infection and Immunity, September 2006, p. 5085-5094, Vol. 74, No. 9
0019-9567/06/$08.00+0     doi:10.1128/IAI.00293-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Opacity-Associated Adhesin Repertoire in Hyperinvasive Neisseria meningitidis{dagger}

Martin J. Callaghan,1 Keith A. Jolley,2 and Martin C. J. Maiden2*

University Department of Paediatrics, University of Oxford, Level 4, John Radcliffe Hospital, Headington, Oxford OX3 9DU, United Kingdom,1 Department of Zoology, Peter Medawar Building for Pathogen Research, University of Oxford, South Parks Road, Oxford OX1 3SY, United Kingdom2

Received 22 February 2006/ Returned for modification 18 April 2006/ Accepted 8 June 2006

The opacity (Opa) proteins mediate a variety of interactions between the bacterium Neisseria meningitidis and its human host. These interactions are thought to be of central importance in both the asymptomatic colonization of the nasopharynx and the sporadic occurrence of meningococcal disease. The receptor specificities of a limited number of Opa protein variants have been explored, but the high level of amino acid sequence diversity among variants has complicated the assignment of specific roles to individual Opa variants or combinations of variants. In addition, the distribution of Opa protein variants among diverse meningococci, information that is potentially informative for studies of Opa function, is poorly understood. A systematic survey of the genetic diversity in the four opa gene loci in each of 77 meningococcal isolates was undertaken. These isolates were representative of the seven hyperinvasive meningococcal clonal complexes that caused the majority of meningococcal disease over the last 50 years. Consistent with previous studies, a high level of sequence diversity was observed among the opa genes and the proteins that they encoded; however, particular sets of Opa protein variants were consistently associated with each of the clonal complexes over time periods often spanning decades and during global spread. These observations were consistent with the postulate that particular combinations of Opa proteins confer fitness advantages to individual clonal complexes and have implications for studies of Opa function and the inclusion of Opa proteins in novel meningococcal vaccines.

* Corresponding author. Mailing address: Department of Zoology, Peter Medawar Building for Pathogen Research, University of Oxford, South Parks Road, Oxford OX1 3SY, United Kingdom. Phone: 44 1865 271284. Fax: 44 1865 271284. E-mail: martin.maiden{at}zoo.ox.ac.uk.

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

Editor: J. N. Weiser

Infection and Immunity, September 2006, p. 5085-5094, Vol. 74, No. 9
0019-9567/06/$08.00+0     doi:10.1128/IAI.00293-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Bilek, N., Ison, C. A., Spratt, B. G. (2009). Relative Contributions of Recombination and Mutation to the Diversification of the opa Gene Repertoire of Neisseria gonorrhoeae. J. Bacteriol. 191: 1878-1890 [Abstract] [Full Text]  
  • Callaghan, M. J., Buckee, C., McCarthy, N. D., Ibarz Pavon, A. B., Jolley, K. A., Faust, S., Gray, S. J., Kaczmarski, E. B., Levin, M., Kroll, J. S., Maiden, M. C. J., Pollard, A. J. (2008). Opa Protein Repertoires of Disease-Causing and Carried Meningococci. J. Clin. Microbiol. 46: 3033-3041 [Abstract] [Full Text]  


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