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]
Citations
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Cited by
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Items 101–122 of 122
Kim, T.-G., Kim, B.-G., Jeong, D.-K., Jang, Y., Lee, J., & Yang, M. (2012) · Biotechnology and Bioprocess Engineering · doi:10.1007/s12257-011-0636-z · Cited by 6
“Porphyromonas gingivalis, a black-pigmented gramnegative anaerobe, is an oral pathogen that has been implicated in the pathogenesis of severe periodontal disease in adults [17,18].”
BackgroundKim, T.-G., Tiến, N. Q. Đ., Yang, M., Moon, J.-H., & Lee, J. (2016) · Plant Cell Tissue and Organ Culture (PCTOC) · doi:10.1007/s11240-016-1005-6 · Cited by 5
“Porphyromonas gingivalis, a blackpigmented gram-negative anaerobe, has been considered as one of the most important pathogens implicated in periodontitis (Hamada et al. 1994; Lamont and Jenkinson 1998).”
BackgroundDashper, S. G., O’brien-simpson, N. M., Bhogal, P. S., Franzmann, A. D., & Reynolds, E. C. (1998) · Australian Dental Journal · doi:10.1111/j.1834-7819.1998.tb06097.x · Cited by 5
Nakagawa, T., Nakagawa, S., Ishihara, K., Yamada, S., Machida, Y., & Okuda, K. (1995) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.1995.tb01293.x · Cited by 5
Purification and characterization of a fimbrial protein from Porphyromonas salivosa ATCC 49407
KOYATA, Y., Watanabe, K., Toyama, T., SASAKI, H., & Hamada, N. (2019) · Journal of Veterinary Medical Science · doi:10.1292/jvms.19-0067 · Cited by 4
“Fimbriae in particular have an important role in facilitating the initial interaction between the bacteria and host [3, 14, 49].”
BackgroundLambertz, J., Buhl, E. M., Apel, C., Preisinger, C., & Conrads, G. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms27010383 · Cited by 3
“Indeed, FimA fimbriae have an important role in initial biofilm formation [71] and attachment to other bacteria in oral biofilm (e.g., Actinomyces viscosus , Treponema denticola , S. oralis [72–74], F. nucleatum (present study)) and to host cells [75–77].”
Bioengineering and Analysis of Oral Mucosa Models
Golinski, P., Groeger, S. E., & Meyle, J. (2013) · Springer eBooks · doi:10.1007/978-3-7091-1586-2_15 · Cited by 2
Bagaitkar, J. (2010) · doi:10.18297/etd/60 · Cited by 1
“lm (152)), hair-like, peritrichous, adhesive, filamentous structures that project away from the cell surface and are primarily comprised of a 41 kD protein (FimA, fimbrillin) encoded by the FimA gene (153).”
Porphyromonas gingivalis Fimbriae Function as One of Virulence Factors.
Hanazawa, S., & Murakami, Y. (1996) · Nippon Saikingaku Zasshi · doi:10.3412/jsb.51.803 · Cited by 1
Al-Qarakhli, A. M. A. (2018) · ORCA Online Research @Cardiff (Cardiff University) · Cited by 1
Hajishengallis, G. (2007) · Journal of Oral Biosciences · doi:10.1016/s1349-0079(07)80009-0
Characterization of the innate response to the RagB protein of Porphyromonas gingivalis.
Hutcherson, J. A. (2015) · doi:10.18297/etd/2077
“Both are considered virulence factors that aid in adherence and invasion of tissue [62, 63].”
BackgroundSimionato, M. R. L., & Rodrigues, P. H. M. (2014)
Effects of the periodontal pathogens Porphyromonas gingivalis and Tannerella forsythia on platelets
Andrews, A. (2019) · Sheffield Hallam University · doi:10.7190/shu-thesis-00159
“The primary role of fimA is to promote bacterial adherence to oral surfaces with fimA deficient strains presenting a reduced capacity for both adherence (Hamada et al., 1994) and invasion (Njoroge et al., 1997; Weinberg et al., 1997) of oral epithelial cells.”
BackgroundOfek, I., Hasty, D. L., & Doyle, R. J. (2014) · ASM Press eBooks · doi:10.1128/9781555817800.ch12
Virulence Factors of Periodontal Pathogens and Their Specific Targets in the Oral Epithelial Barrier
Alanbari, B. F., Al-Taweel, F. B. H., & Cooper, P. R. (2026) · Al-Rafidain Journal of Medical Sciences · doi:10.54133/ajms.v10i1.2662
“P. gingivalis (ATCC 33277) is one of the most well-characterized clinically isolated bacterial strains that expresses fimbriae [17], is able to produce gingipains [18], and can invade and internalize in oral cells [19].”
Evolutionary and structural diversification of the FimA adhesin in Porphyromonas gingivalisPreprint
Nuñez-Belmar, J., Luis, V., Herrmann, F., Cárdenas, J. P., & Rivas‐Pardo, J. A. (2026) · SSRN Electronic Journal · doi:10.2139/ssrn.7288238
Takeshita, A., Murakami, Y., Yamashita, Y., Ishida, M., Fujisawa, S., Kitano, S., & Hanazawa, S. (1998) · Infection and Immunity · doi:10.1128/iai.66.9.4056-4060.1998
“Interestingly, a recent study (6) demonstrated clearly that mutation of the fimA gene, encoding fimbrillin, the major subunit of the fimbriae, prevents bacterial adherence to host cells.”
BackgroundEvolutionary diversity and structural comparison of the FimA adhesin in Porphyromonas gingivalis
Nuñez-Belmar, J., Luis, V., Herrmann, F., Cárdenas, J. P., & Rivas‐Pardo, J. A. (2026) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2026.106048
Porphyromonas gingivalis: the Role of Surface Structures in Virulence and Biofilm Development
Davey, M. E., Boisvert, H., & Arndt, A. (2011) · doi:10.1128/9781555817107.ch9
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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