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Infection and Immunity, March 1999, p. 1267-1276, Vol. 67, No. 3
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Functional Activities and Epitope Specificity of Human and Murine Antibodies against the Class 4 Outer Membrane Protein (Rmp) of Neisseria meningitidis

Einar Rosenqvist,1,* Alexis Musacchio,1,dagger Audun Aase,1 E. Arne Høiby,2 Ellen Namork,3 Jan Kolberg,1 Elisabeth Wedege,1 Alexei Delvig,1 Rolf Dalseg,1 Terje E. Michaelsen,1,4 and Jan Tommassen5

Departments of Vaccinology,1 Bacteriology,2 and Environmental Medicine,3 National Institute of Public Health, N-0403 Oslo, and Department of Pharmacognosy, Institute of Pharmacy, University of Oslo, N-0316 Oslo,4 Norway, and Department of Molecular Cell Biology and Institute of Biomembranes, University of Utrecht, 3584 CH Utrecht, The Netherlands5

Received 27 August 1998/Returned for modification 21 October 1998/Accepted 28 December 1998

Antibodies against the class 4 outer membrane protein (OMP) from Neisseria meningitidis have been purified from sera from vaccinees immunized with the Norwegian meningococcal group B outer membrane vesicle vaccine. The human sera and purified antibodies reacted strongly with the class 4 OMP in immunoblots, whereas experiments with whole bacteria showed only weak reactions, indicating that the antibodies mainly reacted with parts of the class 4 molecule that were not exposed. The purified human anti-class 4 OMP antibodies and the monoclonal antibodies (MAbs) were neither bactericidal nor opsonic against live meningococci. Three new MAbs against the class 4 OMP were generated and compared with other, previously described MAbs. Three linear epitopes in different regions of the class 4 OMP were identified by the reaction of MAbs with synthetic peptides. The MAbs showed no blocking effect on bactericidal activity of MAbs against other OMPs. However, one of the eight purified human anti-class 4 OMP antibody preparations, selected from immunoblot reactions among sera from 27 vaccinees, inhibited at high concentrations the bactericidal effect of a MAb against the class 1 OMP. However, these antibodies were not vaccine induced, as they were present also before vaccination. Therefore, this study gave no evidence that vaccination with a meningococcal outer membrane vesicle vaccine containing the class 4 OMP induces blocking antibodies. Our data indicated that the structure of class 4 OMP does not correspond to standard beta -barrel structures of integral OMPs and that no substantial portion of the OmpA-like C-terminal region of this protein is located at the surface of the outer membrane.

* Corresponding author. Mailing address: Department of Vaccinology, National Institute of Public Health, P. O. Box 4404, Torshov, N-0403 Oslo, Norway. Phone: (47) 22 04 26 19. Fax: (47) 22 04 23 01. E-mail: einar.rosenqvist{at}folkehelsa.no.

dagger Present address: Center for Genetic Engineering and Biotechnology, Department of Vaccines, C. Habana, Cuba.

Infection and Immunity, March 1999, p. 1267-1276, Vol. 67, No. 3
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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