Affiliation:
1. Department of Oral Immunology and Infectious Diseases, University of Louisville School of Dentistry, Louisville, Kentucky, USA
Abstract
Periodontal diseases are among the most common infections of humans and are also associated with systemic inflammatory conditions. Colonization and pathogenicity of
P. gingivalis
are regulated by signal transduction pathways based on protein tyrosine phosphorylation and dephosphorylation. Here, we identify and characterize a novel component of the tyrosine (de)phosphorylation axis: a polymerase and histindinol phosphatase (PHP) family enzyme. This tyrosine phosphatase, designated Php1, was required for
P. gingivalis
community development with other oral bacteria, and in the absence of Php1 activity
P. gingivalis
was unable to cause disease in a mouse model of periodontitis. This work provides significant insights into the protein tyrosine (de)phosphorylation network in
P. gingivalis
, its adaptation to heterotypic communities, and its contribution to colonization and virulence.
Publisher
American Society for Microbiology
Cited by
19 articles.
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