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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
-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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