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Solution structure of the factor H-binding protein, a survival factor and protective antigen of Neisseria

Francesca Cantini1, Daniele Veggi, Sara Dragonetti

  • 1Magnetic Resonance Center (CERM), F50019 Sesto Fiorentino, Italy.

The Journal of Biological Chemistry
|February 7, 2009
PubMed

Insights

Factor H-binding protein from Neisseria meningitidis is crucial for bacterial survival by binding human complement factor H. Its full-length structure reveals insights for developing improved meningococcal vaccines.

Area of Science:

  • Microbiology
  • Structural Biology
  • Vaccinology

Background:

  • Factor H-binding protein (fHBP) is a Neisseria meningitidis lipoprotein essential for pathogenesis.
  • fHBP facilitates bacterial survival in human blood by inhibiting complement factor H.
  • fHBP is a key target for developing vaccines against meningococcal disease.

Purpose of the Study:

  • To determine the full-length structure of Neisseria meningitidis Factor H-binding protein.
  • To map functional sites involved in complement factor H binding and bactericidal antibody recognition.
  • To provide a structural basis for designing enhanced meningococcal vaccine candidates.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was used to determine the full-length protein structure.
  • Monoclonal antibodies were mapped to specific residues on the protein surface.
  • Functional mapping related antibody epitopes to factor H binding and bactericidal activity.

Main Results:

  • The full-length Factor H-binding protein consists of two independent structural barrels linked together.
  • Residues involved in binding human complement factor H and recognized by bactericidal antibodies were identified.
  • The structure elucidates the molecular organization of fHBP and its functional domains.

Conclusions:

  • The determined structure of full-length fHBP provides critical insights into its mechanism of immune evasion.
  • Mapping of functional sites offers a rational basis for the design of more effective meningococcal vaccines.
  • This structural information can guide the development of next-generation vaccines targeting Neisseria meningitidis.

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