1. Epitope Mapping of a Bactericidal Monoclonal Antibody against the Factor H Binding Protein of Neisseria meningitidis
- Author
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Maurizio Comanducci, Claudio Donati, Giacomo Romagnoli, Daniele Veggi, Mariagrazia Pizza, Rino Rappuoli, Laura Santini, Silvana Savino, Marzia Monica Giuliani, Maria Scarselli, Federica Di Marcello, Sara Dragonetti, Lucia Banci, and Francesca Cantini
- Subjects
Models, Molecular ,Protein Conformation ,medicine.drug_class ,Molecular Sequence Data ,Neisseria meningitidis ,Monoclonal antibody ,Epitope ,Bacterial Proteins ,Structural Biology ,medicine ,Amino Acid Sequence ,Nuclear Magnetic Resonance, Biomolecular ,Molecular Biology ,Antigens, Bacterial ,Linear epitope ,biology ,Binding protein ,Antibodies, Monoclonal ,biology.organism_classification ,Antibodies, Bacterial ,Molecular biology ,Meningococcal Infections ,Epitope mapping ,Biochemistry ,biology.protein ,Neisseria ,Antibody ,Sequence Alignment ,Epitope Mapping ,Conformational epitope - Abstract
The factor H binding protein (fHbp) is a 27-kDa membrane-anchored lipoprotein of Neisseria meningitidis that allows the survival of the bacterium in human plasma; it is also a major component of a universal vaccine against meningococcus B. In this study, we used nuclear magnetic resonance spectroscopy, mutagenesis, and in silico modeling to map the epitope recognized by MAb502, a bactericidal monoclonal antibody elicited by fHbp. The data show that the antibody recognizes a conformational epitope within a well-defined area of the immunodominant C-terminal domain of the protein that is formed by two loops connecting different beta-strands of a beta-barrel and a short alpha-helix brought in spatial proximity by the protein folding. The identification of the protective epitopes of fHbp is an important factor for understanding the mechanism(s) of an effective immune response and provides valuable guidelines for designing variants of the protein able to induce broadly protective immunity.
- Published
- 2009
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