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Nonfunctional variant 3 factor H binding proteins as meningococcal vaccine candidates
Stijn van der Veen1, Steven Johnson, Ilse Jongerius
1Sir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.
Infection and Immunity
|January 1, 2014
Summary
Nonfunctional Factor H binding proteins (fHbps) from Neisseria meningitidis retain immunogenicity and elicit strong bactericidal activity. These findings support the development of novel meningococcal vaccines using these modified antigens.
Area of Science:
- Microbiology
- Immunology
- Vaccine Development
Background:
- Neisseria meningitidis causes meningitis and septicemia.
- Factor H binding protein (fHbp) is a key virulence factor and vaccine antigen.
- fHbp variants (V1, V2, V3) show limited cross-reactivity; fH binding may reduce immunogenicity.
Purpose of the Study:
- To characterize nonfunctional V3 fHbps (fHbp(T286A), fHbp(E313A)) with reduced affinity for Factor H.
- To assess the immunogenicity and bactericidal activity of these nonfunctional fHbps.
- To provide a basis for designing next-generation meningococcal vaccines.
Main Methods:
- Characterization of two nonfunctional V3 fHbp mutants with single amino acid substitutions.
- Assessment of protein folding and affinity for Factor H.
- Evaluation of immunogenicity and serum bactericidal activity in transgenic mice.
Main Results:
- Nonfunctional V3 fHbps exhibited reduced affinity for Factor H without altered protein folding.
- No significant differences in anti-V3 fHbp antibody titers were observed between wild-type and nonfunctional fHbps.
- Nonfunctional V3 fHbps induced equivalent or enhanced serum bactericidal activity compared to wild-type fHbp.
Conclusions:
- Nonfunctional V3 fHbps are immunogenic and elicit potent bactericidal responses.
- These findings support the use of nonfunctional fHbps in next-generation meningococcal vaccines.
- Targeted modification of fHbp can yield effective vaccine candidates without compromising immunogenicity.
