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

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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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Background
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Background
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Background
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Background
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BackgroundMethod
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Method
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Result
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Background
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Background
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Background
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Background
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Differential expression and adherence of Porphyromonas gingivalis FimA genotypes
Zheng, C., Wu, J., & Xie, H. (2011) · Molecular Oral Microbiology · doi:10.1111/j.2041-1014.2011.00626.x · Cited by 35
“gingivalis strains and also with previous reports (Hamada et al., 1994; Lin et al., 2006) supporting a critical role of FimA in promoting the attachment of P.”
Result
Identification of Escherichia coli Genes That Are Specifically Expressed in a Murine Model of Septicemic Infection
Khan, M. A., & Isaacson, R. E. (2002) · Infection and Immunity · doi:10.1128/iai.70.7.3404-3412.2002 · Cited by 35
“mutations were introduced into i484 as described previously (12).”
Method
Purification and characterization of a novel secondary fimbrial protein from Porphyromonas gingivalis strain 381
Arai, M., Hamada, N., & Umemoto, T. (2000) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(00)00459-6 · Cited by 34
In Vitro Models That Support Adhesion Specificity in Biofilms of Oral Bacteria
Ellen, R. P., Lépine, G., & Nghiem, P.-M. (1997) · Advances in Dental Research · doi:10.1177/08959374970110011401 · Cited by 34
Immune response of macrophages from young and aged mice to the oral pathogenic bacterium Porphyromonas gingivalis
Shaik-Dasthagirisaheb, Y. B., Kantarcı, A., & Gibson, F. C. (2010) · Immunity & Ageing · doi:10.1186/1742-4933-7-15 · Cited by 32
“Focusing on chemokine expression, we observed that Pg DPG3 stimulated BMM also to produce MIP-1 a as compared with unchallenged control, like TNF-a , these levels were significantly less than that observed with wild type Pg challenge (Figure 2C).”
MethodInfluential
Cytokine production induced by a 67‐kDa fimbrial protein from Porphyromonas gingivalis
Hamada, N., Watanabe, K., Arai, M., Hiramine, H., & Umemoto, T. (2002) · Oral Microbiology and Immunology · doi:10.1034/j.1399-302x.2002.170311.x · Cited by 31
Isolation and characterization of transposon-induced mutants of deficient in fimbriation
Watanabe-Kato, T., Hayashi, J., Terazawa, Y., Hoover, C. I., Nakayama, K., Eiko, H. I. B. I., Kawakami, N., Ikeda, T., Nakamura, H., Noguchi, T., et al. (1998) · Microbial Pathogenesis · doi:10.1006/mpat.1997.0170 · Cited by 31
Identification of bistable populations of Porphyromonas gingivalis that differ in epithelial cell invasion
Suwannakul, S., Stafford, G. P., Whawell, S. A., & Douglas, C. W. I. (2010) · Microbiology · doi:10.1099/mic.0.038075-0 · Cited by 29
“However, there have also been reports that strains with identical fimbriation characteristics vary in their invasive ability (Dorn et al., 2000; Duncan et al., 1993; Hamada et al., 1994; Eick et al., 2006), indicating uncertainty about Abbreviations: AMC, 7-amido-4-methylcoumarin; B-Arg-AMC, aNbenzoyl-L-arginine-7-ami…”
Background
Identification of glyceraldehyde-3-phosphate dehydrogenase of epithelial cells as a second molecule that binds toPorphyromonas gingivalisfimbriae
Sojar, H. T., & Genco, R. J. (2005) · FEMS Immunology & Medical Microbiology · doi:10.1016/j.femsim.2005.01.006 · Cited by 29
“gingivalis have been shown to have diminished capacity for adherence to oral epithelial cells in in vitro assays [5].”
Background
Fimbriae and the hemagglutinating adhesin HA-Ag2 mediate adhesion of Porphyromonas gingivalis to epithelial cells
Dû, L. L., Pellen‐Mussi, P., Chandad, F., Mouton, C., & Bonnaure‐Mallet, M. (1997) · Infection and Immunity · doi:10.1128/iai.65.9.3875-3881.1997 · Cited by 28
“(11), who showed that the FimA protein of P.”
Background
Analysis of Chemical Structure and Antibiofilm Properties of Exopolysaccharides from Lactiplantibacillus plantarum EIR/IF-1 Postbiotics
Karaca, B., Haliscelik, O., Gursoy, M., Kiran, F., Loimaranta, V., Söderling, E., & Gursoy, U. K. (2022) · Microorganisms · doi:10.3390/microorganisms10112200 · Cited by 26
Hemin-binding protein 35 (HBP35) plays an important role in bacteria–mammalian cells interactions in Porphyromonas gingivalis
Hiratsuka, K., Kiyama-Kishikawa, M., & Abiko, Y. (2010) · Microbial Pathogenesis · doi:10.1016/j.micpath.2010.01.001 · Cited by 22
Porphyromonas gingivalis fimbriae are pro-inflammatory but do not play a prominent role in the innate immune response to P. gingivalis
Graves, D. T., Naguib, G. H., Lü, H., Desta, T., & Amar, S. (2005) · Journal of Endotoxin Research · doi:10.1177/09680519050110010501 · Cited by 21
Designing a peptide-based vaccine against Porphyromonas gingivalis
Lauritano, D. (2012) · Frontiers in Bioscience-Scholar · doi:10.2741/s395 · Cited by 19
Porphyromonas gingivalis fimbria-stimulated bone resorption in vitro is inhibited by a tyrosine kinase inhibitor
Hanazawa, S., Kawata, Y., Murakami, Y., Naganuma, K., Amano, S., Miyata, Y., & Kitano, S. (1995) · Infection and Immunity · doi:10.1128/iai.63.6.2374-2377.1995 · Cited by 19
Adhesion of Porphyromonas gingivalis Strains to Cultured Epithelial Cells From Patients With a History of Chronic Adult Periodontitis or From Patients Less Susceptible to Periodontitis
Quirynen, M., Papaioannou, W., van Steenbergen, T. J. M., Dierickx, K., Cassiman, J. J., & van Steenberghe, D. (2001) · Journal of Periodontology · doi:10.1902/jop.2001.72.5.626 · Cited by 18
Development of a novel plasmid vector pTIO-1 adapted for electrotransformation of Porphyromonas gingivalis
Tagawa, J., Inoue, T., Naito, M., Sato, K., Kuwahara, T., Nakayama, M., Nakayama, K., Yamashiro, T., & Ohara, N. (2014) · Journal of Microbiological Methods · doi:10.1016/j.mimet.2014.07.032 · Cited by 17
The role of the RgpA–Kgp proteinase–adhesin complexes in the adherence of Porphyromonas gingivalis to fibroblasts
Pathirana, R. D., O’brien-simpson, N. M., Visvanathan, K., Hamilton, J. A., & Reynolds, E. C. (2008) · Microbiology · doi:10.1099/mic.0.2008/019943-0 · Cited by 17
“…by IP: 54.70.40.11 On: Sat, 15 Dec 2018 01:34:35 Previous studies have reported that P. gingivalis fimbriae play a significant role in mediating the adherence of strains ATCC 33277 and 381 to gingival fibroblast cells (Hamada et al., 1994; Kontani et al., 1996; Ogawa et al., 1997).”
BackgroundInfluential
Antagonistic effect of synthetic peptides corresponding to the binding regions within fimbrial subunit protein from Porphyromonas gingivalis to human gingival fibroblasts
Ogawa, T., Ogo, H., & Kinoshita, A. (1997) · Vaccine · doi:10.1016/s0264-410x(96)00127-2 · Cited by 17
Secretion ofPorphyromonas gingivalisFimbrillin Polypeptides by RecombinantStreptococcus gordonii
Sharma, A., Sojar, H. T., Hruby, D. E., Kuramitsu, H. K., & Genco, R. J. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7306 · Cited by 17
Gingipain enzymes from Porphyromonas gingivalis preferentially bind immobilized extracellular proteins: a mechanism favouring colonization?
McAlister, A. D., Sroka, A., FITZPATRICK, R. E., Quinsey, N. S., Travis, J., Potempa, J., & Pike, R. N. (2008) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.2008.01128.x · Cited by 16
“The Gram negative, anaerobic bacteria Porphyromonas gingivalis is associated with adult periodontal disease in humans and uses a number of adhesin molecules to aid colonisation of the oral cavity, including fimbriae, hemagglutinins and protease/adhesin complexes [1,2,3,4].”
BackgroundMethod
DNA-based adaptive immunity protect host from infection-associated periodontal bone resorption via recognition of Porphyromonas gingivalis virulence component
Han, X., LaRosa, K. B., Kawai, T., & Taubman, M. A. (2013) · Vaccine · doi:10.1016/j.vaccine.2013.09.004 · Cited by 16
“Mutation of the fimA gene, encoding fimbrillin, the major subunit of the fimbriae, prevents Pg to adhere to host cells [7].”
Porphyromonas gingivalis genes isolated by screening for epithelial cell attachment
Duncan, M. J., Emory, S. A., & Almira, E. C. (1996) · Infection and Immunity · doi:10.1128/iai.64.9.3624-3631.1996 · Cited by 16
“The gene encoding fimbrillin (fimA), the protein subunit of fimbriae, was cloned and sequenced (8), and two independently isolated fimA insertion mutants show a loss of ability to adhere not only to saliva-coated hydroxyapatite (25) but also to human epithelial cells (12).”
Background
Induction of immune responses and prevention of alveolar bone loss by intranasal administration of mice with Porphyromonas gingivalis fimbriae and recombinant cholera toxin B subunit
Takahashi, Y., Kumada, H., Hamada, N., Haishima, Y., Ozono, S., Isaka, M., Yasuda, Y., Tochikubo, K., & Umemoto, T. (2007) · Oral Microbiology and Immunology · doi:10.1111/j.1399-302x.2007.00373.x · Cited by 15
Production of monoclonal antibody against FimA protein from Porphyromonas gingivalis in rice cell suspension culture
Kim, B.-G., Kim, S., Kim, N.-S., Huy, N.-X., Choi, Y., Lee, J. Y., Jang, Y., Yang, M., & Kim, T.-G. (2014) · Plant Cell Tissue and Organ Culture (PCTOC) · doi:10.1007/s11240-014-0481-9 · Cited by 13
“Porphyromonas gingivalis, a black-pigmented gramnegative anaerobe, is one of the most important pathogens implicated in the pathogenesis of periodontal disease in adults (Lamont and Jenkinson 1998; Hamada et al. 1994).”
Background
Construction of a sIgA-enhancing anti-Porphyromonas gingivalis FimA vaccine and nasal immunization in mice
Guo, H., Wang, X., Jiang, G., & Yang, P. (2006) · Immunology Letters · doi:10.1016/j.imlet.2006.07.008 · Cited by 13
Purification and characterization of a putative fimbrial protein/receptor of Porphyromonas gingivalis
Dashper, 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.tb00155.x · Cited by 13
Hyporesponsiveness of inflamed human gingival fibroblasts from patients with chronic periodontal diseases against cell surface components of Porphyromonas gingivalis
Ogawa, T., Ozaki, A., Shimauchi, H., & Uchida, H. (1997) · FEMS Immunology & Medical Microbiology · doi:10.1111/j.1574-695x.1997.tb01023.x · Cited by 12
Peptide Mapping of a Functionally Versatile Fimbrial Adhesin from Porphyromonas gingivalis
Hajishengallis, G. (2007) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-007-9084-1 · Cited by 11
“These binding interactions require the presence of fimbriae since FimA-deficient mutants of P. gingivalis interact poorly with gingival epithelial cells (Hamada et al., 1994; Weinberg et al., 1997).”
Background
Inhibitory effects of azithromycin on the adherence ability of Porphyromonas gingivalis
Kan, P., Sasaki, H., Inaba, K., Watanabe, K., Hamada, N., & Minabe, M. (2019) · Journal of Periodontology · doi:10.1002/jper.18-0559 · Cited by 11
Cloning and characterization of heavy and light chain genes encoding the FimA-specific monoclonal antibodies that inhibit Porphyromonas gingivalis adhesion
Koh, E.-M., Kim, J., Kim, T.-G., Moon, J.-H., Oh, J.-H., Lee, J., & Jang, Y. (2011) · Microbiology and Immunology · doi:10.1111/j.1348-0421.2011.00305.x · Cited by 11
“gingivalis with mutation in the FimA gene fails to attach to human gingival fibroblasts and epithelial cells (7).”
Background
Potential Value of a Rice Protein Extract, Containing Proteinaceous Inhibitors against Cysteine Proteinases fromPorphyromonas gingivalis, for Managing Periodontal Diseases
Taiyoji, M., Yamanaka, T., Tsuno, T., & Ohtsubo, S. (2013) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.120585 · Cited by 11
Production of Monoclonal Antibodies Specific to FimA of Porphyromonas gingivalis and Their Inhibitory Activity on Bacterial Binding
Koh, E.-M., Kim, J., Lee, J.-Y., & Kim, T.-G. (2009) · Immune Network · doi:10.4110/in.2009.9.5.203 · Cited by 11
Identification of a new genetic variant (G231N, E232T, N235D) of peptidylarginine deiminase from P. gingivalis in advanced periodontitis
Bereta, G. P., Strzelec, K., Łazarz‐Bartyzel, K., Dziedzic, A., Nowakowska, Z., Krutyhołowa, A., Bielecka, E., Kantyka, T., Grabiec, A. M., Kaczmarzyk, T., et al. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1355357 · Cited by 10
Salivary immunoglobulin A production against a synthetic oligopeptide antigen of Actinobacillus actinomycetemcomitans fimbriae
Honma, K., Kato, T., & Okuda, K. (1999) · Oral Microbiology and Immunology · doi:10.1034/j.1399-302x.1999.140504.x · Cited by 10
The gingipains from Porphyromonas gingivalis do not directly induce osteoclast differentiation in primary mouse bone marrow cultures
FITZPATRICK, R. E., Campbell, P. D., Sivagurunathan, S., Pagel, C. N., Potempa, J., Mackie, E. J., & Pike, R. N. (2008) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.2008.01151.x · Cited by 8
Reduced fimbria-associated activities of Porphyromonas gingivalis induced by recombinant fimbrial expression
Takahashi, Y., Yoshimoto, H., Kato, D., Hamada, N., Arai, M., & Umemoto, T. (2001) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2001.tb10524.x · Cited by 7
Mesaconate from Bacillus subtilis R0179 Supernatant Attenuates Periodontitis by Inhibiting Porphyromonas gingivalis in Mice
Zhao, W., Ji, L., Li, J., Liu, D., Yan, C., Zhang, C., Wang, X., Liu, Y., & Zheng, S. (2024) · Journal of Periodontal Research · doi:10.1111/jre.13363 · Cited by 6

Authors: Hamada, N., Watanabe, K., Sasakawa, C., Yoshikawa, M., Yoshimura, F., & Umemoto, T.
Affiliations: Kanagawa Dental University (JP)
ORCID: Watanabe, K
Yoshimura, F
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: green
europepmc.org
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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Construction and characterization of a fimA mutant of Porphyromonas gingivalis

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