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Cited by 124Oral microbiology and periodontitis researchBiochemical and Structural CharacterizationMicrobial infections and disease research

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

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Hamada, N, Watanabe, K, Sasakawa, C, Yoshikawa, M, Yoshimura, F, Umemoto, T·1994·Infection and Immunity
DOI 10.1128/iai.62.5.1696-1704.1994PMC PMC186386
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Abstract

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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Crossref · 10.1128/iai.62.5.1696-1704.1994

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Metadata

Authors
Hamada, N., Watanabe, K., Sasakawa, C., Yoshikawa, M., Yoshimura, F., & Umemoto, T.
Affiliations
Kanagawa Dental University (JP)
ORCID
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
DOI
10.1128/iai.62.5.1696-1704.1994
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
Licence
journals.asm.org/non-commercial-tdm-license (tdm)
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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