Molecular cloning and characterization of the gene encoding 53 kD outer membrane protein of Porphyromonas gingivalis.

The pga53 gene which encoded the antigenic 53 kD outer membrane protein (Ag53) was isolated from a genomic DNA library of Porphyromonas gingivalis FDC381 by using an Ag53-immunized rabbit serum. Determination of its complete nucleotide sequence revealed that the precursor of Ag53 had a 50 amino-acid putative signal sequence and the mature protein of 448 amino acids. The deduced amino acid sequence after a 50 amino-acid putative signal sequence was in complete agreement with the first 20 N-terminal amino acids of purified Ag53. Analysis of the deduced amino acid sequence revealed the presence of a highly hydrophilic proline-rich region at the C-terminal of Ag53. The deduced amino acid sequence showed 29.9% homology with that of a 72 kD cell-surface protein in P. gingivalis. Southern hybridization revealed that pga53 was specific to several P. gingivalis strains and that P. gingivalis strains which did not possess Ag53 had genes homologous to pga53.