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Journal articles on the topic 'Bacteroides gingivalis'

Author: Grafiati

Published: 4 June 2021

Last updated: 29 July 2025

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1

Okuda, K., and I. Takazoe. "The Role of Bacteroides Gingivalis in Periodontal Disease." Advances in Dental Research 2, no. 2 (1988): 260–68. http://dx.doi.org/10.1177/08959374880020021001.

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The microbial flora in adult advanced periodontitis lesions is comprised of Gram-negative rods, with Bacteroides gingivalis as one of the major representatives. This review deals with biological properties of surface antigens, hemagglutinin (attachment factor), and capsular structure of B. gingivalis. Sera containing high IgG antibody levels to B. gingivalis enhanced the complement-mediated bactericidal activity in vitro, although the susceptibility to complement-mediated lysis differed among B. gingivalis strains. The protective effect of immunization against B. gingival is infection was exam

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2

Naito, Y., and R. J. Gibbons. "Attachment of Bacteroides gingivalis to Collagenous Substrata." Journal of Dental Research 67, no. 8 (1988): 1075–80. http://dx.doi.org/10.1177/00220345880670080301.

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The ability of Bacteroides gingivalis 381 to attach to hydroxyapatite (HA) beads, treated with either human type I or type IV collagen, or to particles of bovine bone collagen was studied. All preparations were blocked with human albumin prior to being incubated with 3H-thymidine-labeled B. gingivalis 381 cells. The presence of collagen on HA surfaces (C-HA) significantly promoted attachment of the organism. HA treated with Type IV collagen bound B. gingivalis cells more effectively than did HA treated with type I collagen. Attachment of two additional strains of B. gingivalis to HA was also p

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3

Abiko, Y., M. Hayakawa, H. Aoki, and H. Takiguchi. "Gene Cloning and Expression of a Bacteroides Gingivalis-Specific Protein Antigen in Escherichia Coli." Advances in Dental Research 2, no. 2 (1988): 310–14. http://dx.doi.org/10.1177/08959374880020021801.

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Gene banks of chromosomal DNA from Bacteroides gingival is 381 were constructed utilizing the bacteriophage replacement vector λCharon4A. A clone encoding a protein antigen from B. gingivalis was identified by Western-blot screening, with use of antiserum induced to extracts of B. gingivalis cells. DNA fragments from the phage clone were subcloned into the plasmid vector pACYC184 to yield an immunoreactive clone. Cell extracts from the subclone reacted with antiserum against B. gingivalis, but did not react with antisera to B. asaccharolyticus, B. intermedius, or B. melaninogenicus. The antise

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4

Larjava, H., V. J. Uitto, E. Eerola, and M. Haapasalo. "Inhibition of gingival fibroblast growth by Bacteroides gingivalis." Infection and Immunity 55, no. 1 (1987): 201–5. http://dx.doi.org/10.1128/iai.55.1.201-205.1987.

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5

Li, J., and R. P. Ellen. "Relative Adherence of Bacteroides Species and Strains to Actinomyces viscosus on Saliva-coated Hydroxyapatite." Journal of Dental Research 68, no. 9 (1989): 1308–12. http://dx.doi.org/10.1177/00220345890680090301.

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The study was designed to compare the adherence of several Bacteroides species to A. viscosus. Using 3H, we labeled 24 laboratory strains, including 13 Bacteroides species and I I fresh clinical isolates of three Bacteroides species. Their adherence to A. viscosus bound to a saliva-coated mineral surface was quantified by liquid scintillation. Adherence relative to a standard strain, B. gingivalis 2561, was compared. Among the lab bacteroides, those of B. gingivalis (eight strains) were the greatest binders (mean, 80.5 ± 12.4%). Strains of other lab bacteroides bound less well (mean, 33.4 ± 6.

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6

Maeda, K., T. Hirofuji, N. Chinju, et al. "The Modulation of Polymorphonuclear Leukocyte Function by Bacteroides Gingivalis." Advances in Dental Research 2, no. 2 (1988): 315–18. http://dx.doi.org/10.1177/08959374880020021901.

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B acteroides gingivalis has been recognized as a pathogen causing adult periodontal disease. In this study, we examined the culture supernatants of B. gingival is for their ability to alter the function of polymorphonuclear leukocytes (PMNs). After a 60-minute incubation with the culture supernatants of B. gingivalis, it was found that there was a significant reduction of f-methionyl-leucyl-phenylalanine (FMLP) receptor in human and guinea pig PMNs. Superoxide anion (O- 2) production of PMNs stimulated by FMLP was also suppressed when cells were pre-incubated with the culture supernatants of B

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7

Yamasaki, T., A. Nagata, T. Kiyoshige, M. Sato, and R. Nakamura. "Black-pigmented, asaccharolytic Bacteroides species resembling Porphyromonas gingivalis (Bacteroides gingivalis) from beagle dogs." Oral Microbiology and Immunology 5, no. 6 (1990): 332–35. http://dx.doi.org/10.1111/j.1399-302x.1990.tb00436.x.

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8

Abiko, Y., M. Hayakawa, S. Murai, and H. Takiguchi. "Glycylprolyl Dipeptidylaminopeptidase from Bacteroides gingivalis." Journal of Dental Research 64, no. 2 (1985): 106–11. http://dx.doi.org/10.1177/00220345850640020201.

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9

Nelson, Karen E., Robert D. Fleischmann, Robert T. DeBoy, et al. "Complete Genome Sequence of the Oral Pathogenic Bacterium Porphyromonas gingivalis Strain W83." Journal of Bacteriology 185, no. 18 (2003): 5591–601. http://dx.doi.org/10.1128/jb.185.18.5591-5601.2003.

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ABSTRACT The complete 2,343,479-bp genome sequence of the gram-negative, pathogenic oral bacterium Porphyromonas gingivalis strain W83, a major contributor to periodontal disease, was determined. Whole-genome comparative analysis with other available complete genome sequences confirms the close relationship between the Cytophaga-Flavobacteria-Bacteroides (CFB) phylum and the green-sulfur bacteria. Within the CFB phyla, the genomes most similar to that of P. gingivalis are those of Bacteroides thetaiotaomicron and B. fragilis. Outside of the CFB phyla the most similar genome to P. gingivalis is

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10

NAGATA, Atsushi, Makoto SATO, and Ryo NAKAMURA. "Serotype specific antigens of Bacteroides gingivalis." JOURNAL OF DENTAL HEALTH 40, no. 2 (1990): 251–53. http://dx.doi.org/10.5834/jdh.40.251.

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11

ENDO, Hideaki, and Hiroshi HORIUCHI. "Superoxide dismutase activity in Bacteroides gingivalis." Nihon Shishubyo Gakkai Kaishi (Journal of the Japanese Society of Periodontology) 27, no. 4 (1985): 816–23. http://dx.doi.org/10.2329/perio.27.816.

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12

Lantz, M. S., R. W. Rowland, L. M. Switalski, and M. Höök. "Interactions of Bacteroides gingivalis with fibrinogen." Infection and Immunity 54, no. 3 (1986): 654–58. http://dx.doi.org/10.1128/iai.54.3.654-658.1986.

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13

Suido, H., J. J. Zambon, P. A. Mashimo, R. Dunford, and R. J. Genco. "Correlations between Gingival Crevicular Fluid Enzymes and the Subgingival Microflora." Journal of Dental Research 67, no. 8 (1988): 1070–74. http://dx.doi.org/10.1177/00220345880670080201.

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Bacteroides gingivalis is a Gram-negative micro-organism implicated in the pathogenesis of adult periodontitis and producing relatively large amounts of specific enzymes. In the present study, subgingival samples taken from adults with moderate periodontitis were examined for the presence and relative amounts of enzymatic activity toward certain substrates. Enzyme levels were then correlated with clinical periodontal indices and microbiological analysis of subgingival plaque, including darkfield microscopy for bacterial morphotypes and immunofluorescence microscopy for B. gingivalis and Bacter

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14

Johne, Berit, Ingar Olson, and Klaus Bryn. "Fatty acids and sugars in lipopolysaccharides from Bacteroides intermedius, Bacteroides gingivalis and Bacteroides loescheii." Oral Microbiology and Immunology 3, no. 1 (1988): 22–27. http://dx.doi.org/10.1111/j.1399-302x.1988.tb00600.x.

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15

Lantz, M. S., R. D. Allen, P. Bounelis, L. M. Switalski, and M. Hook. "Bacteroides gingivalis and Bacteroides intermedius recognize different sites on human fibrinogen." Journal of Bacteriology 172, no. 2 (1990): 716–26. http://dx.doi.org/10.1128/jb.172.2.716-726.1990.

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16

Wennström, Jan L., Gunnar Dahlén, Jörgen Svensson, and Sture Nyman. "Actinobacillus actinomycetemcomitans, Bacteroides gingivalis and Bacteroides intermedius: predictors of attachment loss?" Oral Microbiology and Immunology 2, no. 4 (1987): 158–63. http://dx.doi.org/10.1111/j.1399-302x.1987.tb00300.x.

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17

Slots, Jergen, and Max A. Listgarten. "Bacteroides gingivalis, Bacteroides intermedius and Actinobacillus actinomycetemcomitans in human periodontal diseases." Journal of Clinical Periodontology 15, no. 2 (1988): 85–93. http://dx.doi.org/10.1111/j.1600-051x.1988.tb00999.x.

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18

Ellen, Richard P., Susanne Schwarz-Faulkner, and David A. Grove. "Coaggregation among periodontal pathogens, emphasizing Bacteroides gingivalis –Actinomyces viscosus cohesion on a saliva-coated mineral surface." Canadian Journal of Microbiology 34, no. 3 (1988): 299–306. http://dx.doi.org/10.1139/m88-055.

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Teeth offer nonshedding surfaces on which a wide range of bacterial species accumulate as thick, cohesive plaques. Intergeneric coaggregation mediated by specific recognition between surface "cohesins" is thought to contribute to both the cohesiveness of plaque and the sequence in which bacteria colonize the tooth surface. There is some evidence that Gram-positive species, like the efficient tooth colonizer Actinomyces viscosus, enhance subsequent tooth colonization by the more virulent periodontal pathogen Bacteroides gingivalis. To study their mechanism of cohesion, we have developed an in v

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19

Suido, H., T. Eguchi, T. Tanaka, and M. Nakamura. "Identification of Periodontopathic Bacteria Based Upon their Peptidase Activities." Advances in Dental Research 2, no. 2 (1988): 304–9. http://dx.doi.org/10.1177/08959374880020021701.

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Black-pigmented Bacteroides (BPB) and spirochetes are associated with some forms of periodontal diseases. The enzymes produced by these bacteria may participate in the destruction of gingival and periodontal tissues. Certain proteases and peptidases are unique to Bacteroides gingivalis and Treponema denticola. Our purpose was to study the peptidases of periodontopathogens and to evaluate the use of unique peptidases for detection and identification of these bacteria. Bacteria used were BPB, Treponema, Fusobacterium, Capnocytophaga, Actinobacillus (Haemophilus), and Eikenella species. Twenty-fi

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20

KIKUCHI, Yasuo, Tatsuo KIYOSHIGE, Shuji SASAKI, et al. "Protective efficacy of antiserum against Bacteroides gingivalis." Nihon Shishubyo Gakkai Kaishi (Journal of the Japanese Society of Periodontology) 27, no. 1 (1985): 106–13. http://dx.doi.org/10.2329/perio.27.106.

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21

Barua, P. K., D. W. Dyer, and M. E. Neiders. "Effect of iron limitation on Bacteroides gingivalis." Oral Microbiology and Immunology 5, no. 5 (2007): 263–68. http://dx.doi.org/10.1111/j.1399-302x.1990.tb00423.x.

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22

Lawson, D. A., and T. F. Meyer. "Biochemical characterization of Porphyromonas (Bacteroides) gingivalis collagenase." Infection and Immunity 60, no. 4 (1992): 1524–29. http://dx.doi.org/10.1128/iai.60.4.1524-1529.1992.

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23

Rotimi, V. O., B. E. Laughon, J. G. Bartlett, and H. A. Mosadomi. "Activities of Nigerian chewing stick extracts against Bacteroides gingivalis and Bacteroides melaninogenicus." Antimicrobial Agents and Chemotherapy 32, no. 4 (1988): 598–600. http://dx.doi.org/10.1128/aac.32.4.598.

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24

Goldstein, Ellie J. C., Diane M. Citron, C. Vreni Merriam, Yumi Warren, and Kerin Tyrrell. "Activities of Telithromycin (HMR 3647, RU 66647) Compared to Those of Erythromycin, Azithromycin, Clarithromycin, Roxithromycin, and Other Antimicrobial Agents against Unusual Anaerobes." Antimicrobial Agents and Chemotherapy 43, no. 11 (1999): 2801–5. http://dx.doi.org/10.1128/aac.43.11.2801.

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ABSTRACT The comparative activity of telithromycin (HMR 3647) against 419 human anaerobic isolates was determined by the agar dilution method. At concentrations of ≤0.5 μg/ml, telithromycin was active againstActinomyces israelii, Actinomyces odontolyticus, Bacteroides tectum, Bacteroides ureolyticus, Bacteroides gracilis (nowCampylobacter gracilis), Porphyromonas spp. (including Porphyromonas gingivalis and Porphyromonas macacae), Prevotella intermedia, Prevotella heparinolytica, and almost all Peptostreptococcusspecies. Clostridia showed species and strain variability, often with a biphasic p

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25

SHAH, H. N., and M. D. COLLINS. "Proposal for Reclassification of Bacteroides asaccharolyticus, Bacteroides gingivalis, and Bacteroides endodontalis in a New Genus, Porphyromonas." International Journal of Systematic Bacteriology 38, no. 1 (1988): 128–31. http://dx.doi.org/10.1099/00207713-38-1-128.

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26

Loos, B. G., D. Mayrand, R. J. Genco, and D. P. Dickinson. "Genetic Heterogeneity of Porphyromonas (Bacteroides) gingivalis by Genomic DNA Fingerprinting." Journal of Dental Research 69, no. 8 (1990): 1488–93. http://dx.doi.org/10.1177/00220345900690080801.

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This study describes the use of total genomic DNA fingerprinting with the use of restriction endonucleases to characterize clinical isolates of Porphyromonas gingivalis (Bacteroides gingivalis) obtained from patients with periodontitis or with root-canal infections. The majority of independent isolates had a unique DNA fingerprint, indicating extensive genetic heterogeneity within this species. Twenty-nine distinct DNA fingerprints were found among the 33 isolates investigated. This is in contrast to biotyping and serotyping, where only one type and three types, respectively, have been reporte

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27

TANAKA, Midori. "A study of lipopolysaccharide derived from Bacteroides gingivalis." Nihon Shishubyo Gakkai Kaishi (Journal of the Japanese Society of Periodontology) 32, no. 1 (1990): 111–20. http://dx.doi.org/10.2329/perio.32.111.

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28

Vasel, D., T. J. Sims, B. Bainbridge, L. Houston, R. Darveau, and R. C. Page. "Shared antigens of Porphymmonas gingivalis and Bacteroides forsythus." Oral Microbiology and Immunology 11, no. 4 (1996): 226–35. http://dx.doi.org/10.1111/j.1399-302x.1996.tb00174.x.

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29

Eke, P. I., B. E. Laughon, and V. O. Rotimi. "Cytotoxic activity of crude extracts of Bacteroides gingivalis." Journal of Medical Microbiology 28, no. 1 (1989): 5–8. http://dx.doi.org/10.1099/00222615-28-1-5.

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30

Naito, Y., K. Okuda, T. Kato, and I. Takazoe. "Monoclonal antibodies against surface antigens of Bacteroides gingivalis." Infection and Immunity 50, no. 1 (1985): 231–35. http://dx.doi.org/10.1128/iai.50.1.231-235.1985.

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31

Hunt, D. E., J. V. Jones, and V. R. Dowell. "Selective medium for the isolation of Bacteroides gingivalis." Journal of Clinical Microbiology 23, no. 3 (1986): 441–45. http://dx.doi.org/10.1128/jcm.23.3.441-445.1986.

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32

Millar, S. J., P. B. Chen, and E. Hausmann. "Monoclonal antibody for identification of Bacteroides gingivalis lipopolysaccharide." Journal of Clinical Microbiology 25, no. 12 (1987): 2437–39. http://dx.doi.org/10.1128/jcm.25.12.2437-2439.1987.

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33

Deslauriers, M., F. Chandad, and C. Mouton. "Caracterisation immunochimique d'une adhesine hemagglutinante de Bacteroides gingivalis." Médecine et Maladies Infectieuses 20 (December 1990): 165–71. http://dx.doi.org/10.1016/s0399-077x(05)80084-8.

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34

Grenier, D., and B. C. McBride. "Surface location of a Bacteroides gingivalis glycylprolyl protease." Infection and Immunity 57, no. 11 (1989): 3265–69. http://dx.doi.org/10.1128/iai.57.11.3265-3269.1989.

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35

Chen, P. B., L. B. Davern, R. Schifferle, and J. J. Zambon. "Protective immunization against experimental Bacteroides (Porphyromonas) gingivalis infection." Infection and Immunity 58, no. 10 (1990): 3394–400. http://dx.doi.org/10.1128/iai.58.10.3394-3400.1990.

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36

Neiders, M. E., P. B. Chen, H. Suido, et al. "Heterogeneity of virulence among strains of Bacteroides gingivalis." Journal of Periodontal Research 24, no. 3 (1989): 192–98. http://dx.doi.org/10.1111/j.1600-0765.1989.tb02005.x.

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37

van Steenbergen, T. J. M., F. G. A. Delemarre, F. Namavar, and J. de Graaff. "Differences in virulence within the species Bacteroides gingivalis." Antonie van Leeuwenhoek 53, no. 4 (1987): 233–44. http://dx.doi.org/10.1007/bf00393930.

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38

Schifferle, R. E., M. S. Reddy, J. J. Zambon, R. J. Genco, and M. J. Levine. "Characterization of a polysaccharide antigen from Bacteroides gingivalis." Journal of Immunology 143, no. 9 (1989): 3035–42. http://dx.doi.org/10.4049/jimmunol.143.9.3035.

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Abstract A polysaccharide Ag (PS) was isolated from the phenol-water extract of Bacteroides gingivalis strain A7A1-28 and separated from LPS by Sephacryl S-400 HR chromatography. The PS was composed of glucose, glucosamine, galactosamine, and galactosaminuronic acid, while the LPS contained rhamnose, mannose, galactose, glucose, glucosamine, galactosamine, phosphate, and lipid, but not galactosaminuronic acid. The PS and LPS were immunochemically distinct by immunoelectrophoresis in agarose with homologous rabbit antiserum. The phenol-water extract from strain A7A1-28 was immunoreactive by imm

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39

Chen, Tsute, Hong Dong, Yixin P. Tang, Mary M. Dallas, Michael H. Malamy, and Margaret J. Duncan. "Identification and Cloning of Genes fromPorphyromonas gingivalis after Mutagenesis with a Modified Tn4400 Transposon from Bacteroides fragilis." Infection and Immunity 68, no. 1 (2000): 420–23. http://dx.doi.org/10.1128/iai.68.1.420-423.2000.

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ABSTRACT Porphyromonas gingivalis is a gram-negative, black-pigmented, oral anaerobe strongly associated with adult periodontitis. Previous transposon mutagenesis studies with this organism were based on the Bacteroides transposon Tn4351. Characterization of Tn4351-disrupted genes by cloning has not been an efficient way to analyze large numbers of mutants and is further complicated by the high rate of cointegration of the suicide delivery vector containing Tn4351. In this study, we mutagenized P. gingivalis with a modified version of the Bacteroides fragilis transposon Tn4400. Plasmid pYT646B

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40

Hanazawa, S., K. Hirose, Y. Ohmori, S. Amano, and S. Kitano. "Bacteroides gingivalis fimbriae stimulate production of thymocyte-activating factor by human gingival fibroblasts." Infection and Immunity 56, no. 1 (1988): 272–74. http://dx.doi.org/10.1128/iai.56.1.272-274.1988.

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41

Li, J., and R. P. Ellen. "Coaggregation of Porphyromonas (Bacteroides) gingivalis, other species of Bacteroides, and Actinomyces viscosus: methodological evaluation." Journal of Microbiological Methods 12, no. 2 (1990): 91–96. http://dx.doi.org/10.1016/0167-7012(90)90018-2.

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42

Chandad, Fatiha, and Christian Mouton. "Molecular size variation of the hemagglutinating adhesin HA-Ag2, a common antigen of Bacteroides gingivalis." Canadian Journal of Microbiology 36, no. 10 (1990): 690–96. http://dx.doi.org/10.1139/m90-117.

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The array of Bacteroides gingivalis W83 antigens revealed by crossed Immunoelectrophoresis includes one antigen that is associated with an erythrocyte-binding capacity, termed the hemagglutinating adhesin HA-Ag2. This antigen was excised from crossed-immunoelectrophoresis plates to produce two polyclonal antisera, VL 011 and WL 303, whose restricted specificity for HA-Ag2 was assessed using crossed Immunoelectrophoresis, crossed Immunoelectrophoresis with an intermediate gel, and crossed imunoaffinoelectrophoresis. Both antisera, when used to probe blots of an EDTA cell surface extract of B. g

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43

Bourgeau, G., and D. Mayrand. "Aggregation of Actinomyces strains by extracellular vesicles produced by Bacteroides gingivalis." Canadian Journal of Microbiology 36, no. 5 (1990): 362–65. http://dx.doi.org/10.1139/m90-063.

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The aggregation of Actinomyces viscosus and Actinomyces naeslundii with extracellular vesicles of Bacteroides gingivalis was studied. Factors influencing the aggregation phenomenon were examined. L-Arginine was found to effectively inhibit aggregation as was an antibody preparation directed against a B. gingivalis surface hemagglutinin. Aggregation occurred over a wide pH range and did not seem to be affected by high salt concentrations or the presence of carbohydrates. Treatment of the vesicle preparation with proteases, sodium dodecyl sulphate, and high temperatures diminished or eliminated

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44

Barkocy-Gallagher, Genevieve A., Joseph W. Foley, and Marilyn S. Lantz. "Activities of the Porphyromonas gingivalis PrtP Proteinase Determined by Construction ofprtP-Deficient Mutants and Expression of the Gene inBacteroides Species." Journal of Bacteriology 181, no. 1 (1999): 246–55. http://dx.doi.org/10.1128/jb.181.1.246-255.1999.

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ABSTRACT PrtP is a major cysteine proteinase of Porphyromonas gingivalis. The gene encoding this proteinase, prtP, was cloned into the Escherichia coli-Bacteroides shuttle vectors pFD288 and pFD340 and was expressed in Bacteroidescells, apparently under the control of its own promoter, when in pFD288, or a Bacteroides promoter present on pFD340. Proteolytically active PrtP was detected by fibrinogen zymography in cells or spent growth medium of several Bacteroides species harboring the recombinant plasmids. The proteinase was recovered fromBacteroides fragilis ATCC 25285(pFD340-prtP) cells by

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45

MOUTON, Christian. "Immunobiology of Bacteroides (Porphyromonas) gingivalis from laboratory to clinic." Nihon Shishubyo Gakkai Kaishi (Journal of the Japanese Society of Periodontology) 33, Supplement1 (1991): 27. http://dx.doi.org/10.2329/perio.33.supplement1_27.

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46

Miyauchi, T., M. Hayakawa, and Y. Abiko. "Purification and characterization of glycylprolyl aminopeptidase from Bacteroides gingivalis." Oral Microbiology and Immunology 4, no. 4 (2007): 222–26. http://dx.doi.org/10.1111/j.1399-302x.1989.tb00256.x.

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47

Simonson, L. G., B. R. Merrell, R. F. Rouse, and I. L. Shklair. "Production and Characterization of Monoclonal Antibodies to Bacteroides gingivalis." Journal of Dental Research 65, no. 2 (1986): 95–97. http://dx.doi.org/10.1177/00220345860650021801.

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48

ISOGAI, Hiroshi, Emiko ISOGAI, Hitomi WAKIZAKA, et al. "Effects of lipopolysaccharide from bacteroides gingivalis in SUS rats." Japanese Journal of Veterinary Science 51, no. 5 (1989): 1095–97. http://dx.doi.org/10.1292/jvms1939.51.1095.

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49

Nishikata, Makoto, and Fuminobu Yoshimura. "Characterization of Porphyromonas (bacteroides) gingivalis hemagglutinin as a protease." Biochemical and Biophysical Research Communications 178, no. 1 (1991): 336–42. http://dx.doi.org/10.1016/0006-291x(91)91819-x.

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50

McBride, B. C., A. Joe, and U. Singh. "Cloning of Bacteroides gingivalis surface antigens involved in adherence." Archives of Oral Biology 35 (1990): S59—S68. http://dx.doi.org/10.1016/0003-9969(90)90132-t.

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