Virulence factors of Porphyromonas gingivalis are modified by polyphenol oxidase and asparaginase.

Porphyromonas gingivalis is a well-adapted pathogen of the periodontal pocket distinguished by its wide array of proteolytic activities and its ability to adhere to multiple substrata in the oral cavity. Microbial proteins with binding functions (such as adhesins and enzymes) very often contain critical tyrosine residues, supported by one or more asparagines in the binding cleft. This study investigates the reduction in adhesiveness and in proteolytic activity after treating P. gingivalis with the tyrosine- and asparagine-targeting enzymes polyphenol oxidase (PPO) and asparaginase (ASG). Cysteine protease activity was reduced by pretreatment with both enzymes, while the trypsin-like activity was affected only by PPO. Adhesion to buccal epithelial cells, laminin and fibronectin as well as hemagglutination was reduced by one or both of the enzymes. PPO, but not ASG, reduced the coaggregation of P. gingivalis with Actinomyces naeslundii. Treatment with these enzymes might provide an alternative to traditional antimicrobial strategies.