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Given the emerging evidence of an association between periodontal infections and systemic conditions, the search for specific methods to detect the presence of  P. gingivalis , a principal etiologic agent in chronic periodontitis, is of high importance. The aim of this study was to characterize antibodies raised against purified  P. gingivalis  HmuY protein and selected epitopes of the HmuY molecule. Since other periodontopathogens produce homologs of HmuY, we also aimed to characterize responses of antibodies raised against the HmuY protein or its epitopes to the closest homologous proteins from  Prevotella intermedia  and  Tannerella forsythia . Rabbits were immunized with purified HmuY protein or three synthetic, KLH-conjugated peptides, derived from the  P. gingivalis  HmuY protein. The reactivity of anti-HmuY antibodies with purified proteins or bacteria was determined using Western blotting and ELISA assay. First, we found homologs of  P. gingivalis  HmuY in  P. intermedia  (PinO and PinA proteins) and  T. forsythia  (Tfo protein) and identified corrected nucleotide and amino acid sequences of Tfo. All proteins were overexpressed in  E. coli  and purified using ion-exchange chromatography, hydrophobic chromatography and gel filtration. We demonstrated that antibodies raised against  P. gingivalis  HmuY are highly specific to purified HmuY protein and HmuY attached to  P. gingivalis  cells. No reactivity between  P. intermedia  and  T. forsythia  or between purified HmuY homologs from these bacteria and anti-HmuY antibodies was detected. The results obtained in this study demonstrate that  P. gingivalis  HmuY protein may serve as an antigen for specific determination of serum antibodies raised against this bacterium.

Anti-HmuY Antibodies Specifically Recognize Porphyromonas gingivalis HmuY Protein but Not Homologous Proteins in Other Periodontopathogens