The Serine Phosphatase SerB of Porphyromonas gingivalis Suppresses IL-8 Production by Dephosphorylation of NF-κB RelA/p65

• DOI: 10.1371/journal.ppat.1003326
• Publication Date: 2013-04-18T21:04:26Z
• Authors: Hiroki Takeuchi; Takanori Hirano; Sarah E. Whitmore; Ichijiro Morisaki; Atsuo Amano; Richard J. Lamont
• Keywords: Dephosphorylation

Porphyromonas gingivalis is a major pathogen in severe and chronic manifestations of periodontal disease, which one the most common infections humans. A central feature P. pathogenicity dysregulation innate immunity at gingival epithelial interface, including suppression IL-8 production by cells. NF-κB transcriptional regulator that controls important aspects immune responses, RelA/p65 homodimers regulate transcription IL8. Phosphorylation p65 subunit protein on serine 536 residue affects nuclear translocation target genes. Here we show SerB, haloacid dehalogenase (HAD) family phosphatase secreted gingivalis, produced intracellularly can specifically dephosphorylate S536 mutant lacking SerB was impaired dephosphorylation S536, ectopically expressed bound to co-localized with cytoplasm. Ectopic expression also resulted reduced TNF-α-stimulated In contrast, p105/50 unaffected SerB. Co-expression constitutively active (S536D) relieved inhibition translocation. Both activity IL8 promoter were diminished Deletion truncation mutants HAD-family enzyme motifs unable p65, inhibit or abrogate transcription. Specific consequent translocation, provides molecular basis for bacterial strategy manipulate host inflammatory pathways repress mucosal surfaces.