Open AccessInvolvement of integrins in fimbriae‐mediated binding and invasion by Porphyromonas gingivalis
Author(s) -
Yilmaz Özlem,
Watanabe Kiyoko,
Lamont Richard J.
Publication year - 2002
Publication title -
cellular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.542
H-Index - 138
eISSN - 1462-5822
pISSN - 1462-5814
DOI - 10.1046/j.1462-5822.2002.00192.x
Subject(s) - porphyromonas gingivalis , fimbria , integrin , paxillin , biology , focal adhesion , cell adhesion , tyrosine phosphorylation , microbiology and biotechnology , phosphorylation , receptor , cell , biochemistry , genetics , escherichia coli , bacteria , gene
Summary Interaction between the major fimbriae of Porphyromonas gingivalis and gingival epithelial cells is important for bacterial adhesion and invasion. In this study, we identified integrins as an epithelial cell cognate receptor for P. gingivalis fimbriae. Immunoprecipitation and direct binding assays revealed a physical association between recombinant fimbrillin and β 1 integrins. In vitro adhesion and invasion assays demonstrated inhibition of binding and invasion of P. gingivalis by β 1 integrin antibodies. In contrast, invasion of a fimbriae‐deficient mutant of P. gingivalis was not affected by integrin antibodies. Infection of gingival epithelial cells with wild‐type P. gingivalis induced tyrosine phosphorylation of the 68 kDa focal adhesion protein paxillin, whereas the fimbriae‐deficient mutant failed to evoke similar changes. Interestingly, activation of paxillin was not accompanied by an increase in the phosphorylation of focal adhesion kinase (FAK). These results provide evidence that P. gingivalis fimbriae promote adhesion to gingival epithelial cells through interaction with β 1 integrins, and this association represents a key step in the induction of the invasive process and subsequent cell responses to P. gingivalis infection.