The Relationship between Mutations in Gene-Specific Domains of Salivary Fibronectin (cFn) and Dynamin-2 (Dynm-2) and the Development of Porphyromonas gingivalis-Initiated Periodontitis

Periodontitis is a chronic inflammatory disease characterized by the destruction of supporting structures teeth. Its high prevalence and negative effects on quality life make it one current problems in dentistry. Porphyromonas gingivalis (P. gingivalis) predominant periodontal pathogen that expresses number virulence factors involved pathogenesis periodontitis. P. fimbriae are critical factor interaction between organism host tissue. They promote both bacterial adhesion invasion into target sites. Fimbriae capable binding to human saliva components, extracellular matrix proteins, commensal bacteria, as well firmly cellular integrin α5β1. After attachment α5β1-integrin, captured pseudopodia, which makes invagination through an actin-mediated pathway possible. It has been proven event also requires participation cell dynamin, actin fibers, microtubules lipid rafts. Work emerged investigating mutations proline-rich terminal domain (PRD) their impact development. Salivary antimicrobial peptides early protective against microbial attack. Of great interest fibronectin (FN) main competitor fimbriae. The FN can interact with cells three different regions: central cell-binding (CCBD), COOH heparin-binding (Hep2), type III connecting segment (IIICS), including CS1 region (Yamada, 1991). CCBD major cell-adhesion contains Arg–Gly–Asp (RGD) motif recognized members receptor family, a5b1, primary many types. work focuses identifying relationship development periodontitis presence domains salivary proteins such (cFN) dynamin-2 (DYNM2).