The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
Construction and characterization of a fimA mutant of Porphyromonas gingivalis
Open accessAbstract
Although fimbriae of Porphyromonas gingivalis have been implicated as playing a major role in adherence to gingival tissue surfaces, no conclusive genetic evidence has yet been obtained. The fimA gene, the determinant for the major fimbrial subunit protein, was cloned and sequenced (D. P. Dickinson, M. A. Kubiniec, F. Yoshimura, and R. J. Genco, J. Bacteriol. 170:1658-1665, 1988). We undertook to inactivate the fimA gene by a homologous recombination technique and examined the fimA mutant for changes in surface properties, including production of fimbriae, adherence to human gingival fibroblasts and epithelial cells, hemagglutinating activity, and surface hydrophobicity. To inactivate the fimA gene, we disrupted a fimA clone by insertion of a DNA segment containing an erythromycin resistance (Emr) gene. This was then delivered into P. gingivalis ATCC 33277 from an Escherichia coli K-12 strain, SM10 lambda pir, by using a mobilizable suicide vector, pGP704; recombination at the fimA locus led to the isolation of a fimA mutant. Disruption of the fimA locus and disappearance of FimA production were confirmed by Southern hybridization with a fimA-specific DNA probe and Western immunoblotting with a monoclonal antibody against the FimA protein, respectively. The fimA mutant constructed failed to express long (0.5- to 1.0-micron) fimbriae from the bacterial surface and had a diminished adhesive capacity to tissue-cultured human gingival fibroblasts and epithelial cells. Observation of the bacteria adhering to human gingival fibroblasts by scanning electron microscopy revealed that the wild-type strain had dramatic local changes in the appearance of the microvilli at the point of contact with large bacterial clumps, whereas the fimA mutant did not. In contrast, neither the hemagglutinating activity nor the surface hydrophobicity was changed in the fimA mutant. These data thus constitute the first direct genetic evidence demonstrating that the FimA protein of P. gingivalis is essential for the interaction of the organism with human gingival tissue cells through a function(s) encoded by the fimA gene.
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“Cell surface hydrophobicity is another key factor contributing to bacterial biofilm formation, including oral bacteria such as P. gingivalis and F. nucleatum [51,52].”
From Analysis of Chemical Structure and Antibiofilm Properties of Exopolysaccharides from Lactiplantibacillus plantarum EIR/IF-1 Postbiotics (2022) · cites this paper as [51]
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Cites
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Implantation of Bacteroides gingivalis in Nonhuman Primates Initiates Progression of Periodontitis
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Life Below the Gum Line: Pathogenic Mechanisms ofPorphyromonas gingivalis
Lamont, R. J., & Jenkinson, H. F. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.4.1244-1263.1998 · Cited by 964
“naeslundii; and fibrinogen, fibronectin, and lactoferrin (7, 9, 76, 88, 105, 128, 136, 162, 252, 255, 274).”
Porphyromonas gingivalis: An Overview of Periodontopathic Pathogen below the Gum Line
How, K. Y., Song, K. P., & Chan, K. G. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.00053 · Cited by 858
“It constitues an important component of the bacterial outer membrane (Hamada et al., 1994).”
Virulence factors of Porphyromonas gingivalis
Holt, S. C., Kesavalu, L. N., Walker, S. G., & Genco, C. A. (1999) · Periodontology 2000 · doi:10.1111/j.1600-0757.1999.tb00162.x · Cited by 644
Groeger, S., & Meyle, J. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00208 · Cited by 473
Generation of inflammatory stimuli: how bacteria set up inflammatory responses in the gingiva
Madianos, P. N., Bobetsis, Y. A., & Kinane, D. F. (2005) · Journal Of Clinical Periodontology · doi:10.1111/j.1600-051x.2005.00821.x · Cited by 310
Metadata
- Authors
- Hamada, N., Watanabe, K., Sasakawa, C., Yoshikawa, M., Yoshimura, F., & Umemoto, T.
- Affiliations
- Kanagawa Dental University (JP)
- Venue
- Infection and Immunity
- Publisher
- American Society for Microbiology
- Published
- 1994-05
- Volume
- 62
- Issue
- 5
- Pages
- 1696-1704
- ISSN
- 0019-9567 (ISSN-L)
- 1098-5522
- PMC
- PMC186386
- OpenAlex
- W2111125148
- Cited by
- 124
- References
- 45
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 2 · 2023: 1 · 2022: 1 · 2019: 5 · 2018: 2 · 2017: 1 · 2016: 2 · 2015: 4 · 2014: 4 · 2013: 3 · 2012: 2
- FWCI
- 13.33
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Infection and Immunity (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Dentistry › Periodontics › Oral microbiology and periodontitis research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Life Sciences › Immunology and Microbiology › Microbiology › Microbial infections and disease research
- Keywords
- Porphyromonas gingivalis, fimA gene, fimbriae, bacterial adhesion, gingival fibroblasts, gingival epithelial cells, homologous recombination, gene disruption, erythromycin resistance, hemagglutination, surface hydrophobicity, periodontal pathogens, host-bacteria interactions
- MeSH terms
- Bacterial Adhesion, Bacterial Proteins, Fibroblasts, Gingiva, Hemagglutination, Humans, Mutation, Fimbriae, Bacterial, Porphyromonas gingivalis, Fimbriae Proteins
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