ArticlePloS one2012
Porphyromonas gingivalis FimA fimbriae: fimbrial assembly by fimA alone in the fim gene cluster and differential antigenicity among fimA genotypes.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed, 52 citations in OpenAlex.
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- Salivary Porphyromonas gingivalis predicts outcome in oral squamous cell carcinomas: a cohort study.BMC oral health · 2021Article
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- Structure of polymerized type V pilin reveals assembly mechanism involving protease-mediated strand exchange.Nature microbiology · 2020Article
- A Putative Type V Pilus Contributes to Bacteroides thetaiotaomicron Biofilm Formation Capacity.Journal of bacteriology · 2019Article
- Recombinant fimbriae protein of Porphyromonas gingivalis induces an inflammatory response via the TLR4/NF‑κB signaling pathway in human peripheral blood mononuclear cells.International journal of molecular medicine · 2019Article
- Frequency of Porphyromonas gingivalis fimA in smokers and nonsmokers after periodontal therapy.Journal of applied oral science : revista FOB · 2019Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The periodontal pathogen Porphyromonas gingivalis colonizes largely through FimA fimbriae, composed of polymerized FimA encoded by fimA. fimA exists as a single copy within the fim gene cluster (fim cluster), which consists of seven genes: fimX, pgmA and fimA-E. Using an expression vector, fimA alone was inserted into a mutant from which the whole fim cluster was deleted, and the resultant complement exhibited a fimbrial structure. Thus, the genes of the fim cluster other than fimA were not essential for the assembly of FimA fimbriae, although they were reported to influence FimA protein expression. It is known that there are various genotypes for fimA, and it was indicated that the genotype was related to the morphological features of FimA fimbriae, especially the length, and to the pathogenicity of the bacterium. We next complemented the fim cluster-deletion mutant with fimA genes cloned from P. gingivalis strains including genotypes I to V. All genotypes showed a long fimbrial structure, indicating that FimA itself had nothing to do with regulation of the fimbrial length. In FimA fimbriae purified from the complemented strains, types I, II, and III showed slightly higher thermostability than types IV and V. Antisera of mice immunized with each purified fimbria principally recognized the polymeric, structural conformation of the fimbriae, and showed low cross-reactivity among genotypes, indicating that FimA fimbriae of each genotype were antigenically different. Additionally, the activity of a macrophage cell line stimulated with the purified fimbriae was much lower than that induced by Escherichia coli lipopolysaccharide.
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