This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow E-mail this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ASM journals
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Drogari-Apiranthitou, M.
Right arrow Articles by Dankert, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Drogari-Apiranthitou, M.
Right arrow Articles by Dankert, J.

 Previous Article  |  Next Article 

Infection and Immunity, July 2002, p. 3752-3758, Vol. 70, No. 7
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.7.3752-3758.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Complement Activation and Formation of the Membrane Attack Complex on Serogroup B Neisseria meningitidis in the Presence or Absence of Serum Bactericidal Activity

M. Drogari-Apiranthitou,1* E. J. Kuijper,1,2 N. Dekker,1 and J. Dankert1

Department of Medical Microbiology, Academic Medical Centre, University of Amsterdam, Amsterdam,1 Department of Medical Microbiology, University Medical Centre of Leiden, Leiden, The Netherlands2

Received 6 December 2001/ Returned for modification 19 January 2002/ Accepted 15 April 2002

Encapsulated meningococci are complement sensitive only in the presence of bactericidal antibodies by yet-unexplored mechanisms. The objective of this study was to investigate the involvement of major bacterial surface constituents on complement activation and membrane attack complex (MAC) formation on serogroup B meningococci in the presence or absence of antibody-dependent serum bactericidal activity (SBA). The strains used were the encapsulated H44/76, five of its variants differing in capsulation and expression of the class 1 porin (PorA), and its lipopolysaccharide (LPS)-deficient isogenic mutant (LPS-) pLAK33. Two normal sera, one with high SBA (SBA+) and one with no bactericidal activity (SBA-) against H44/76 as well as an a-{gamma}-globulinemic serum were used for sensibilization of the bacteria. C3b and iC3b deposition on H44/76, its unencapsulated variant v24, and pLAK33 was similar in SBA+ and SBA- serum, and no difference was present between the strains. MAC deposition on H44/76 was higher in SBA+ serum than in SBA- serum and the a-{gamma}-globulinemic serum. The amounts of C3b on H44/76, v24, and pLAK33 in the a-{gamma}-globulinemic serum were also not different, indicating immunoglobulin G (IgG)- and LPS-independent complement activation. H44/76 PorA(+) and its PorA(-) variant and the v24 PorA(+) and its PorA(-) variant incubated in SBA- serum induced comparable amounts of MAC, despite their different serum sensitivities. Complement formation on the surface of the bacteria occurred almost exclusively via the classical pathway, but the considerable amounts of Bb measured in the serum indicated alternative pathway activation in the fluid phase. We conclude that complement deposition on meningococci is, for the most part, independent of classical pathway IgG and is not influenced by the presence of PorA or LPS on the meningococcal surface. Addition of an anti-PorA chimeric antibody to the nonbactericidal normal serum, while promoting a dose-related bacterial lysis, did not influence the amounts of C3b, iC3b, and MAC formed on the bacterial surface. These findings support the hypothesis that proper MAC insertion rather than the quantity of MAC formed on the bacterial surface is of importance for efficient lysis of meningococci.


* Corresponding author. Mailing address: Department of Medical Microbiology, K3-113C, University of Amsterdam, Meibergdreef 15, 1105 AZ Amsterdam, The Netherlands. Phone: 31-20-5664865. Fax: 31-20-6916531. E-mail: m.apiranthitou{at}amc.uva.nl.

Editor: T. R. Kozel


Infection and Immunity, July 2002, p. 3752-3758, Vol. 70, No. 7
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.7.3752-3758.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Uria, M. J., Zhang, Q., Li, Y., Chan, A., Exley, R. M., Gollan, B., Chan, H., Feavers, I., Yarwood, A., Abad, R., Borrow, R., Fleck, R. A., Mulloy, B., Vazquez, J. A., Tang, C. M. (2008). A generic mechanism in Neisseria meningitidis for enhanced resistance against bactericidal antibodies. JEM 205: 1423-1434 [Abstract] [Full Text]  
  • Jarva, H., Ram, S., Vogel, U., Blom, A. M., Meri, S. (2005). Binding of the Complement Inhibitor C4bp to Serogroup B Neisseria meningitidis. J. Immunol. 174: 6299-6307 [Abstract] [Full Text]  
  • Ram, S., Cox, A. D., Wright, J. C., Vogel, U., Getzlaff, S., Boden, R., Li, J., Plested, J. S., Meri, S., Gulati, S., Stein, D. C., Richards, J. C., Moxon, E. R., Rice, P. A. (2003). Neisserial Lipooligosaccharide Is a Target for Complement Component C4b: INNER CORE PHOSPHOETHANOLAMINE RESIDUES DEFINE C4b LINKAGE SPECIFICITY. J. Biol. Chem. 278: 50853-50862 [Abstract] [Full Text]  
  • Sprong, T., Brandtzaeg, P., Fung, M., Pharo, A. M., Hoiby, E. A., Michaelsen, T. E., Aase, A., van der Meer, J. W. M., van Deuren, M., Mollnes, T. E. (2003). Inhibition of C5a-induced inflammation with preserved C5b-9-mediated bactericidal activity in a human whole blood model of meningococcal sepsis. Blood 102: 3702-3710 [Abstract] [Full Text]