Disease relevance of fimA

• Regulation of the Porphyromonas gingivalis fimA (Fimbrillin) gene [1].
• We previously reported that P. gingivalis with type II fimA was strongly associated with adult periodontitis [2].
• In this study, we have cloned a new type (type V) of fimA from dental plaque samples [3].
• BACKGROUND: Porphyromonas gingivalis is considered to be one of the most important pathogens in periodontal disease and its fimA genes have been classified into six variants (types I through V and Ib) [4].
• A total of 188 Porphyromonas gingivalis strains isolated from 13 periodontal pockets of 8 periodontitis patients were investigated by means of restriction fragment length polymorphism (RFLP) analysis using the fimA gene as a pobe [5].

High impact information on fimA

• Chromatin immunoprecipitation assays and electrophoretic mobility shift assays identify and confirm that FimR binds to the promoter region of the first gene in the fimA cluster [6].
• Furthermore, P. gingivalis strain HW24D1 with type II fimA adhered to cells and invaded them more than strains with other fimA genotypes [2].
• The fimA genes encoding fimbrillin (FimA), a subunit protein of fimbriae, have been classified into five types, types I to V, based on nucleotide sequences [2].
• In common with many bacterial virulence genes, the fimbrillin (fimA) gene of Porphyromonas gingivalis is modulated in response to environmental fluctuation [1].
• Expression of subunit protein, fimbrillin, was observed in eukaryotic cells growing in vitro following transfection with pcDNA3/fimA [7].

Chemical compound and disease context of fimA

• Relationship of periodontal bacteria and Porphyromonas gingivalis fimA variations with phenytoin-induced gingival overgrowth [8].
• Immunochemical specificity of lipopolysaccharide and the molecular property of the gene encoding the fimbrilin (fimA) of Porphyromonas gingivalis strains were examined using 'fimbriated' strains 381 and HG564 and 'non-fimbriated' strains 381FL and W50 [9].

Biological context of fimA

• We used a novel approach, targeted salivary gland (TSG) immunization, using plasmid pcDNA3/fimA, coding for Porphyromonas gingivalis fimbriae [7].
• Restriction fragment length polymorphism analysis of the fimbrillin locus, fimA, of Porphyromonas gingivalis [10].
• Inactivation of the Porphyromonas gingivalis fimA gene blocks periodontal damage in gnotobiotic rats [11].
• Fimbrial production by Porphyromonas gingivalis was inactivated by insertion-duplication mutagenesis, using the cloned gene for the P. gingivalis major fimbrial subunit protein, fimA. by several criteria, this insertion mutation rendered P. gingivalis unable to produce fimbrilin or an intact fimbrial structure [11].
• Primers to the following genes were employed: the fimbrial gene (fimA) of P. gingivalis, the 16S rRNA gene of Pr. intermedia and the leukotoxin-A (lktA) gene of A. actinomycetemcomitans [12].

Anatomical context of fimA

• However, adherence to and invasion of KB cells was not detected with the P. gingivalis fimA mutants, DPG3 and MPG1 [13].
• Adhesion to and invasion of epithelial cells by the periodontopathogen Porphyromonas gingivalis is promoted by the major fimbriae, encoded by fimA [14].
• Fimbria encoded by the gene fimA is considered one of the main factors in the colonization of the oral cavity by Porphyromonas gingivalis [15].
• Several studies have provided clinical evidence that FimA clonal variation may contribute to the periodontopathogenicity of Porphyromonas gingivalis (P.g.). We studied the gene expression profiling of the macrophage-like human cell line U937 after infection of two types of P.g. (fimA type I; Pg-I and fimA type II; Pg-II) using microarray [16].
• Specific binding region within fimbrial subunit protein (fimbrilin) from Porphyromonas gingivalis strain 381 was studied in cultured human gingival fibroblasts [17].

Associations of fimA with chemical compounds

• Insert DNA from the recombinant clones did not contain homology to the P. gingivalis fimA gene, encoding fimbrillin, the subunit protein of fimbriae, but showed various degrees of homology to certain cysteine protease-hemagglutinin genes [18].
• Type II fimA organisms caused the most significant induction of serum sialic acid, as well as other infectious symptoms, followed by types Ib, IV and V [19].
• Heating for 5 min at 100 degrees C in sodium dodecyl sulfate was necessary to denature the fimbriae into their constituent protein (fimbrilin) monomers with a reduced content of beta-sheet structure [20].

Other interactions of fimA

• Conclusion: Infection of P. gingivalis with prtC+/fimA+ and A. actinomycetemcomitans with lktA+ correlates with periodontal destruction of CP in Chinese. Nonetheless P. gingivalis fimA, prtC genes and A. actinomycetemcomitans lktA gene are closely associated with periodontal destruction, while A. actinomycetemcomitans fap gene is not [21].
• This property was dependent, in part, on the strain 381 fimA, ppk, and usp genes [22].
• Both the arginine-specific cysteine proteinase (Arg-gingipain) and lysine-specific cysteine proteinase (Lys-gingipain) activity of the P. gingivalis fimA type I strain were significantly higher than those of the fimA type II strains [23].

Analytical, diagnostic and therapeutic context of fimA

• Expression of fimbriae on the surface of the fimA mutant and the wild-type strain, ATCC 33277, were investigated by electron microscopy [24].
• We previously examined the distribution of P. gingivalis in terms of fimA genotypes in periodontitis patients using a fimA type-specific PCR assay [3].
• CONCLUSIONS: BOP in initially type I positive sites showed little improvement with treatment, and the combined persistence of fimA type I and T. forsythensis seemed to be involved in this poor treatment outcome [25].
• Moreover, 26 P. gingivalis isolates were analysed by sequence analysis of the fimA gene [26].
• The present study demonstrated the potential of P. gingivalis fimA type I as a predictor of persistent BOP after treatment [25].

References