Porphyromonas gingivalis has been implicated as a major pathogen associated with chronic periodontitis. To extend our knowledge of post-translational protein glycosylation in P. gingivalis, a proteomic analysis involving two-dimensional polyacrylamide gel electrophoresis combined with carbohydrate staining and mass spectrometry was performed. Four novel glycoproteins, PGN0743, PGN0876, PGN1513 and PGN0729, in P. gingivalis ATCC 33277 were identified. These four identified glycoproteins possess a range of biochemical activities and cellular localization. PGN0743 contains a sequence motif identifying it as a FKBP-type cis-trans isomerase, which has activity usually associated with chaperone functions. PGN0876 and PGN1513 contain tetratricopeptide repeat domains that mediate protein-protein interactions. PGN0729 encodes the outer membrane protein 41 precursor, which was previously identified as Pgm6, and is homologous to the OmpA protein in Escherichia coli. Several different types of glycoprotein were identified, suggesting that P. gingivalis possesses a general mechanism for protein glycosylation. PGN0743-deficient and PGN0876-deficient mutants were constructed to examine the role(s) of the two identified glycoproteins. Both mutants showed a decreased growth rate under nutrient-limited conditions and reduced biofilm formation activity. These results suggest that the novel glycoproteins PGN0743 and PGN0876 play an important role in the growth and colonization of P. gingivalis.
© 2012 John Wiley & Sons A/S.