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J Bacteriol, March 1998, p. 1323-1330, Vol. 180, No. 5
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Sequence Diversity, Predicted Two-Dimensional Protein Structure, and Epitope Mapping of Neisserial Opa Proteins

Burkhard Malorny,1 Giovanna Morelli,1 Barica Kusecek,1 Jan Kolberg,2 and Mark Achtman1,*

Max-Planck Institut für molekulare Genetik, 14195 Berlin, Germany,1 and Department of Vaccines, National Institute of Public Health, N-0462 Oslo, Norway2

Received 11 August 1997/Accepted 16 December 1997

The sequence diversity of 45 Opa outer membrane proteins from Neisseria meningitidis, Neisseria gonorrhoeae, Neisseria sicca, and Neisseria flava indicates that horizontal genetic exchange of opa alleles has been rare between these species. A two-dimensional structural model containing four surface-exposed loops was constructed based on rules derived from porin crystal structure and on conservation of sequence homology within transmembrane beta -strands. The minimal continuous epitopes recognized by 23 monoclonal antibodies were mapped to loops 2 and 3. Some of these epitopes are localized on the bacterial cell surface, in support of the model.

* Corresponding author. Mailing address: Max-Planck Institut für molekulare Genetik, Ihnestraße 73, D-14195 Berlin, Germany. Phone: (49 30) 8413 1262. Fax: (49 30) 8413 1387. E-mail: achtman{at}mpimg-berlin-dahlem.mpg.de.




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