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Infection and Immunity, January 2001, p. 607-612, Vol. 69, No. 1
Department of Microbiology, Hellenic Pasteur
Institute, Athens 115 21, Greece,1 and
Moredun Research Institute, International Research Centre,
Pentlands Science Park, Penicuik, Midlothian EH26 OPZ, United
Kingdom2
Received 2 August 2000/Returned for modification 18 September
2000/Accepted 12 October 2000
Protective monoclonal antibodies (MAbs) to the major outer membrane
protein (MOMP) of species of the family Chlamydiaceae, which is the primary vaccine candidate antigen, recognize nonlinear epitopes conferred by the oligomeric conformation of the molecule. Protective MAbs failed to recognize oligomeric MOMP of the variant strain LLG, which bears amino acid substitutions in variable segments (VSs) 1, 2, and 4, and competed with monomer-specific MAbs mapping to
these VSs in reference strain 577. The results suggest that multiple
sites located in the three VSs contribute to the epitope of protective MAbs.
0019-9567/01/$04.00+0 DOI: 10.1128/IAI.69.1.607-612.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Identification of Protective Epitopes by Sequencing
of the Major Outer Membrane Protein Gene of a Variant Strain of
Chlamydia psittaci Serotype 1 (Chlamydophila
abortus)
*
Corresponding author. Mailing address: Hellenic Pasteur
Institute, 127 Vassilissis Sofias Ave., 115 21 Athens, Greece. Phone and fax: (301) 64 78 873. E-mail: evretou{at}netor.gr.
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