Journal
INFECTION AND IMMUNITY
Volume 77, Issue 2, Pages 764-769Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/IAI.01191-08
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Funding
- National Institute of Allergy and Infectious Diseases [RO1 AI046464, RO1 AI054544]
- National Center for Research Resources [CO6 RR-16226]
- NIH
- Novartis Vaccines and Diagnostics
- Sanofi Pasteur
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Complement factor H (fH), a molecule that downregulates complement activation, binds to Neisseria meningitidis and increases resistance to serum bactericidal activity. We investigated the species specificity of fH binding and the effect of human fH on downregulating rat ( relevant for animal models) and rabbit ( relevant for vaccine evaluation) complement activation. Binding to N. meningitidis was specific for human fH ( low for chimpanzee fH and not detected with fH from lower primates). The addition of human fH decreased rat and rabbit C3 deposition on the bacterial surface and decreased group C bactericidal titers measured with rabbit complement 10- to 60-fold in heat-inactivated sera from human vaccinees. Administration of human fH to infant rats challenged with group B strain H44/76 resulted in an fH dose-dependent increase in CFU/ml of bacteria in blood 8 h later (P < 0.02). At the highest fH dose, 50 mu g/rat, the geometric mean number of CFU per ml was higher than that in control animals (1,050 versus 43 [P < 0.005]). The data underscore the importance of binding of human fH for survival of N. meningitidis in vitro and in vivo. The species specificity of binding of human fH adds another mechanism toward our understanding of why N. meningitidis is strictly a human pathogen.
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