Identification and characterization of human immunoglobulin G Fc receptors of Fusobacterium nucleatum.

Several human pathogens express components which can bind to the Fc portion of immunoglobulins. This study was undertaken to characterize the human immunoglobulin G (IgG) Fc-binding activity of Fusobacterium nucleatum, a suspected pathogen involved in periodontal diseases. Fc-binding activity was detected using whole-cell, cell envelope and outer membrane fractions, and it was found to be associated with polypeptides of 40 kDa and 42 kDa, respectively. Amino terminal sequencing of these components revealed them to be homologous to the bacterial porin encoded by fomA gene. Further sequencing of internal peptide fragments obtained by CNBr cleavage suggested that these two proteins are probably isoforms. In summary, we show that a porin-like protein on the surface of F. nucleatum can bind the Fc fragment of the human immunoglobulin G, and this protein may act as a virulence factor to facilitate this bacterium in evading host immune surveillance system.