Haemolysis of human erythrocytes by the Fusobacterium nucleatum associated with periodontal disease

Falkler, William A.; Clayman, Elaine B.; Shaefer, D F

doi:10.1016/0003-9969(83)90109-7

Cited by 25 publications

(28 citation statements)

References 26 publications

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“…DNA segment vaccines directed to a single component of a cariogenic bacterium (13,15,23) or a periodontal pathogen (31, 55) have been described. Since whole-genomic bacterial DNA contains many CpG motifs, we hypothesized that whole-genomic DNA from periodontal disease-associated bacteria (e.g., Porphyromonas gingivalis [39] and Fusobacterium nucleatum [12]) might enhance the immune response to a vaccine bystander antigen. In this study we used glucosyltransferase (GTF), an enzyme associated with dental caries pathogenesis (44) from dental caries-associated Streptococcus sobrinus, as antigen.…”

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confidence: 99%

Periodontal Bacterial DNA Suppresses the Immune Response to Mutans Streptococcal Glucosyltransferase

Taubman¹,

Han²,

LaRosa³

et al. 2007

Infect Immun

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Certain CpG motifs found in bacterial DNA enhance immune responses through Toll-like receptor 9 (TLR-9) and may also demonstrate adjuvant properties. Our objective was to determine if DNA from bacteria associated with periodontal disease could affect the immune response to other bacterial antigens in the oral cavity. Streptococcus sobrinus glucosyltransferase (GTF), an enzyme involved in dental caries pathogenesis, was used as a test antigen. Rowett rats were injected with aluminum hydroxide (alum) with buffer, alum-GTF, or alum-GTF together with either Escherichia coli DNA, Fusobacterium nucleatum DNA, or Porphyromonas gingivalis DNA. Contrary to expectation, animals receiving alum-GTF plus bacterial DNA (P. gingivalis in particular) demonstrated significantly reduced serum immunoglobulin G (IgG) antibody, salivary IgA antibody, and T-cell proliferation to GTF compared to animals immunized with alum-GTF alone. A diminished antibody response was also observed after administration of alum-GTF with the P. gingivalis DNA either together or separately, indicating that physical complexing of antigen and DNA was not responsible for the reduction in antibody. Since TLR triggering by DNA induces synthesis of prospective suppressive factors (e.g., suppressor of cytokine signaling [SOCS]), the effects of P. gingivalis DNA and GTF exposure on rat splenocyte production of SOCS family molecules and inflammatory cytokines were investigated in vitro. P. gingivalis DNA significantly up-regulated SOCS1 and SOCS5 expression and down-regulated interleukin-10 expression by cultured splenocytes. These results suggested that DNA from periodontal disease-associated bacteria did not enhance, but in fact suppressed, the immune response to a protein antigen from cariogenic streptococci, potentially through suppressive SOCS components triggered by innate mechanisms.

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confidence: 99%

Periodontal Bacterial DNA Suppresses the Immune Response to Mutans Streptococcal Glucosyltransferase

Taubman¹,

Han²,

LaRosa³

et al. 2007

Infect Immun

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“…Glutamic acid, lysine, and several other amino acids may be fermented by F. nucleatum to yield a mixture of acetic acid and butyric acid (1,14,16). Penetration of periodontal tissue by these organic acids may be a causative factor in the etiology of periodontitis and gingivitis (8,12,18,19,26).…”

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Amino acid-dependent transport of sugars by Fusobacterium nucleatum ATCC 10953

Robrish¹,

Oliver²,

Thompson³

1987

J Bacteriol

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Resting cells of Fusobacterium nucleatum 10953 (grown previously in a medium containing glucose) failed to accumulate glucose under aerobic or anaerobic conditions. However, the addition of glutamic acid, lysine, or histidine to anaerobic suspensions of cells caused the immediate and rapid accumulation of glucose. Except for the amino acid-dependent transport of galactose and fructose (the latter being transported at approximately one-third the rate of glucose), no other sugars tested were accumulated by the resting cells. Amino acid-dependent uptake of sugar(s) by F. nucleatum was abolished by exposure of cells to air, and under aerobic conditions the rates of fermentation of glutamic acid and lysine were <15% of the rates determined anaerobically. The energy necessary for active transport of the sugars (acetyl phosphate and ATP) is derived from the anaerobic fermentation of glutamic acid, lysine, or histidine. Competition studies revealed that glucose and galactose were mutual and exclusive inhibitors of transport, and it is suggested that the two sugars (Km = 14 ,uM) are translocated via a common carrier. The products of amino acid-dependent sugar transport were recovered from resting cells as ethanol-precipitable, high-molecular-weight polymers. Polymer formation by F. nucleatum, during growth in medium containing glucose or galactose, was confirmed by electron microscopy.

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“…However, Porphyromonas gingivalis, a putative pathogen of adult human periodontitis [l-4] is devoid of siderophore systems and this species utilizes heme as an iron source [5]. Although heme and heme analogs could be present in the periodontal sites [6,7], hemopexin binds and transports them to the liver [8]. It thus seems to be reasonable to consider that heme is derived by this species for itself from hemoglobin, consider-…”

Section: Introductionmentioning

confidence: 99%

Some binding properties of the envelope of Porphyromonas gingivalis to hemoglobin

Fujimura

1995

FEMS Immunology and Medical Microbiology

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Abstmct: Porphyromonas gingiualis was found to bind to hemoproteins (hemoglobin, myoglobin, catalase, cytochrome c) and the binding properties of the envelope of P. gingiualti to hemoglobin were investigated. Maximum amount of hemoglobin bound to 1 mg of the envelope was 58 pg. No significant binding was observed at 4°C and the binding was inhibited strongly by tosyl-L-lysine chloromethyl ketone, Leupeptin, EDTA and partially by meta-periodate. Heating of the envelope at 70°C for 15 min resulted in complete loss of the binding activity. The binding activity of the envelope was not influenced by the treatment with the endogenous proteases. The envelope saturated with hemoglobin could no longer bind to other hemoproteins tested, indicating that binding site for these hemoproteins are common.

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Haemolysis of human erythrocytes by the Fusobacterium nucleatum associated with periodontal disease

Cited by 25 publications

References 26 publications

Periodontal Bacterial DNA Suppresses the Immune Response to Mutans Streptococcal Glucosyltransferase

Periodontal Bacterial DNA Suppresses the Immune Response to Mutans Streptococcal Glucosyltransferase

Amino acid-dependent transport of sugars by Fusobacterium nucleatum ATCC 10953

Some binding properties of the envelope of Porphyromonas gingivalis to hemoglobin

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