Role of the RprY Response Regulator in P. gingivalis Community Development and Virulence

In this study we examined cross phosphorylation of RprY on tyrosine residues and its importance for RprY function. We show that RprY reacts with phosphotyrosine antibodies, and a tyrosine (Y) resi due at position 41 is predicted to be solvent accessible. Loss of RprY increased the level of heterotypic community development withStreptococcus gordonii, and the community ‐suppressive function of RprY required Y41. Expression of the Mfa1 fimbrial adhesin was increased in therprY mutant and in the mutant complemented withrprY containing a Y41F mutation. In a microscale thermophoresis assay, recombinant RprY protein bound to the promoter region ofmfa1, and binding was diminished in RprY with a Y41F substitution. RprY was required for virulence ofP. gingivalis in a murine model of alveolar bone loss. Transcriptional profiling indicated that RprY can control the expression of genes encoding the type IX secretion system (T9SS) machinery and virulence factors secreted through the T9SS, including the gingipain proteases and peptidylarginine deiminase (PPAD). Collectively, these results establish the RprY response regulator as a component of the tyrosine phosphorylation regulon inP. gingivalis, which can independently control heterotypic community development through the Mfa1 fimbriae, and virulence through the T9SS.

Source: Molecular Oral Microbiology - September 15, 2020 Category: Microbiology Authors: Daonan Shen, John D. Perpich, Kendall S. Stocke, Lan Yakoumatos, Zackary R. Fitzsimonds, Chengcheng Liu, Daniel P. Miller, Richard J. Lamont Tags: ORIGINAL ARTICLE Source Type: research