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PubMed1994

Sequence variability of the 40-kDa outer membrane proteins of Fusobacterium nucleatum strains and a model for the topology of the proteins.

The complete nucleotide sequences of the fomA genes encoding the 40-kDa outer membrane proteins (OMPs) of strains ATCC 10953 and ATCC 25586 of Fusobacterium nucleatum were determined using the genomic DNA, or DNA fragments ligated into a vector plasmid, as template in a polymerase chain reaction. The deduced amino acid sequences of these two proteins were aligned with the amino acid sequence of the corresponding protein of F. nucleatum strain Fev1 and examined for conserved/variable polypeptide segments. A model for the topology of the 40-kDa OMPs is proposed on the basis of this alignment and application of the structural principles derived for OMPs of Escherichia coli. According to this model, sixteen polypeptide segments, which are highly conserved, traverse the outer membrane, thereby creating eight external loops, most of which are highly variable.

Amino Acid Sequence↗

PubMed1993

Human monocytes and gingival fibroblasts release tumor necrosis factor-alpha, interleukin-1 alpha and interleukin-6 in response to particulate and soluble fractions of Prevotella melaninogenica and Fusobacterium nucleatum.

In this study we provide evidence that structural and soluble components of periodontopathogenic bacteria, such as Prevotella melaninogenica and Fusobacterium nucleatum, induce the release of cytokines in vitro known to cause in vivo necrotic inflammatory phenomena and bone resorption (tumor necrosis factor-alpha, interleukin-1 alpha and interleukin-6). Human monocytes and gingival fibroblasts were cultivated in vitro in the presence of both particulate and soluble bacterial fractions. A dose-dependent production of tumor necrosis factor-alpha by monocytes and gingival fibroblasts was observed in the presence of fractions of P. melaninogenica and F. nucleatum. Interleukin-1 alpha was produced in approximately the same quantities in the presence of soluble fractions of either P. melaninogenica or F. nucleatum, but in greater quantities in response to particulate fractions of P. melaninogenica. Monocytes released larger amounts of interleukin-1 alpha (about 3000 pg/ml) than gingival fibroblasts (about 1500 pg/ml). Interleukin-6 was released in greater quantities by monocytes in the presence of the pellet fraction of P. melaninogenica (about 5.5 ng/ml), but gingival fibroblasts released larger amounts of interleukin-6, especially in the presence of particulate and soluble components of F. nucleatum (about 12 ng/ml). The ability to induce the release of these cytokines notably increases the pathogenic potential of the bacteria involved in the damage of periodontal tissue.

Chemical Fractionation↗

PubMed2003

[Bacterial meningitis as a complication of Fusobacterium necroforum infection in adults].

Fusobacterium necrophorum, an anaerobic, gram-negative rod, belongs to the physiological flora of the oropharynx. It causes Lemierre's syndrome characterized by oropharyngeal infection, septic thrombophlebitis of the neck, in particular of the internal jugular vein, and metastatic abscesses, predominantly in the lungs. Rarely, and mainly in children, it causes meningitis. Here we report the clinical course of a 25-year-old woman with F. necrophorum meningitis. She presented with incomplete, right third nerve palsy. Within a few days, she developed fever, meningism and progressive reduction of vigilance. Cerebrospinal fluid analysis showed typical signs of bacterial meningitis. After the identification of F. necrophorum, the antibiotic treatment was changed to meropenem, which led to continuous improvement of the clinical symptoms. Due to persistent signs of inflammation in the CSF, metronidazole was added to the antibiotic regime. This case report demonstrates that F. necrophorum should always be considered in the diagnostic workup of bacterial meningitis in adults.

Adult↗

PubMed1999

Infective endocarditis due to Fusobacterium nucleatum in an intravenous drug abuser.

Infective endocarditis due to anaerobic non-spore-forming gram-negative bacilli in intravenous drug abusers is exceedingly rare, with only two cases being previously reported in the literature. A case of endocarditis due to Fusobacterium nucleatum in an intravenous drug abuser is reported, accompanied by a review of the literature.

Adult↗

PubMed1981

Microbial surface interactions: reduction of the haemagglutination activity of the oral bacterium Fusobacterium nucleatum by absorption with Streptococcus and Bacteroides.

Oral strains of Fusobacterium nucleatum showed haemagglutination (HA) of sheep red blood cells and attachment of HA-active F. nucleatum fragments to other microorganisms allowed a means of studying microbial surface interactions. HA-active sonicated fragments (SF) prepared from F. nucleatum were mixed with whole cell suspensions of 48 bacterial strains and, after incubation, the whole cells were separated from the non-absorbed fragments by differential centrifugation. Attachment of F. nucleatum fragments to the cells was indicated by a reduction in the HA activity of the SF in the supernatant fluid remaining after absorption with whole cells. HA activity of the microbial cells used for absorption and the detection of F. nucleatum fragments on these cells by an indirect fluorescent antibody technique provided further evidence of attachment. Of the 48 strains tested, 10 absorbed F. nucleatum HA-active fragments. They included Bacteroides gingivalis, Bacteroides fragilis subsp. distasonis, Bacteroides corrodens, Streptococcus morbillorum, Streptococcus sanguis (Blackburn and JC 74) and Streptococcus mutans AHT, BHT, 10449 and 6715. Chelators revealed that F. nucleatum attached to the microorganisms via a Ca2+-dependent interaction. Sugar inhibition demonstrated that F. nucleatum attached to the microorganisms via a D-galactose-containing moiety on their surface. A reduction in the absorption of F. nucleatum HA-active fragments by Strep. mutans grown in a higher concentration of sucrose was observed.

Absorption↗

PubMed1982

Attachment of cell fragments of Fusobacterium nucleatum to oral epithelial cells, gingival fibroblasts and white blood cells.

The characteristic haemagglutination (HA) caused by Fusobacterium nucleatum strains was used for measuring their attachment to oral epithelial, gingival fibroblast and white blood cells. Whole cells and sonicated preparations of oral F. nucleatum strains VPI No. 4355, 10197 and ATCC No. 10953 haemagglutinated human and sheep red blood cells. Sonicated preparations of the organisms were tested for HA activity before and after absorption with human cells. Buccal epithelial, gingival fibroblast and white blood cells bound the HA-active fragments, as observed by: (1) decrease in the HA activity of the sonicated preparation after absorption, (2) increase in HA activity of the cells used for absorption, (3) presence of microbial fragments on the cells after absorption detected by fluorescent antibody. The HA-active fragments were released from the cells by EDTA; furthermore, galactose but not glucose inhibited the attachment of F. nucleatum to human cells. The role of cell binding in colonization by the organisms and in immune-stimulated damage to host cells is important.

Absorption↗

PubMed1983

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

Fusobacterium nucleatum and Bacteroides gingivalis are associated with oral disease. They both attach to haemagglutinate and human erythrocytes. Experiments were performed to determine whether haemolysis would occur following attachment of strains of F. nucleatum and Bacteroides species including B. gingivalis. The F. nucleatum strains consistently displayed both haemagglutination and haemolytic activity. The B. gingivalis strains and other Bacteroides species displayed haemagglutination but no measurable haemolytic activity. Varying the concentration of the F. nucleatum whole cells in the standard haemolysis assay suggested a F. nucleatum-erythrocyte binding site interaction. The haemolytic moiety was observed in various cell, cell wall and lipopolysaccharide extracts.

Bacteroides↗

PubMed1992

Different responses in B cells induced by Porphyromonas gingivalis and Fusobacterium nucleatum.

A phenotypic study had shown that gingival B cells respond differently to two periodontopathic bacteria, Porphyromonas gingivalis and Fusobacterium nucleatum. Further investigation now shows a reduction in the percentage of Ki-67 + T cells in cultures of gingival and peripheral blood mononuclear cells stimulated with P. gingivalis for 3 and 6 days, respectively, but no suppression of Ki-67 expression in B cells in response to either P. gingivalis or F. nucleatum. Depletion studies of cultures of peripheral blood mononuclear cells showed that in the absence of CD4 cells, the percentage of CD19+ and CD20+ B cells stimulated with P. gingivalis increased after 6 days whereas depletion of CD8 cells resulted in a rise in the percentage of F. nucleatum- and P. gingivalis-stimulated B cells, although this was not significant in the case of P. gingivalis. Specific antibody to P. gingivalis and F. nucleatum was found in culture supernatants of gingival but not of peripheral blood mononuclear cells, indicating a possible higher frequency of antigen-specific B cells in periodontal lesions. IgG was the predominant isotype in both gingival and control peripheral blood cultures, followed closely by IgA in gingival cultures. F. nucleatum stimulated higher levels of Ig in cultures of peripheral blood mononuclear cells than P. gingivalis or cells cultured in medium only, whereas in gingival cell cultures, stimulation by P. gingivalis appeared to result in higher levels of IgG. Also Ig was present at day 3 in gingival cultures, whereas in the blood cell cultures, Ig was only detected at day 6, further suggesting a degree of activation of of gingival B cells.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗

PubMedDate not supplied

In-vitro antimicrobial susceptibility of Bacteroides and Fusobacterium isolated from footrot in goats.

The agar dilution method was used to determine the antimicrobial activity of 17 antimicrobial agents against 132 strains belonging to the genus Bacteroides and 25 strains from the genus Fusobacterium, all isolated from 120 clinical cases of caprine footrot between October 1987 and November 1988. Josamycin, chloramphenicol and rifampin proved to be the most effective antibiotics in vitro. Significant resistance was found to the other antimicrobial agents studied.

Animals↗

PubMed1985

Specificity of monoclonal antibodies reactive with Fusobacterium nucleatum: effect of formalin fixation.

Monoclonal antibody specific for Fusobacterium nucleatum was reacted with untreated and formalin fixed F. nucleatum cells by an enzyme-linked immunosorbent assay (ELISA) and by indirect immunofluorescence. Treatment of bacterial cells with formalin destroyed the antigenic determinant responsible for reactivity with this monoclonal antibody in both assays. Formalin fixation had no effect on hemagglutination activity (HA) of F. nucleatum cells or reactivity with polyvalent rabbit antiserum in double diffusion in agar. Scanning electron microscopy demonstrated that formalin fixation did not affect binding of F. nucleatum cells to microtiter plates. When developing monoclonal antibodies to be used as diagnostic reagents, the antigenic form utilized for immunization should be identical to the antigenic form which will eventually be used in the diagnostic assay.

Animals↗

PubMed1981

Gas-containing brain abscess due to Fusobacterium nucleatum.

Gas-containing brain abscesses are rarely seen. Recently, in a 28-year-old man, such an abscess ruptured into the lateral ventricle but was treated successfully. Fusobacterium nucleatum, an anaerobic bacillus, was cultured from the pus obtained.

Adult↗

PubMed1987

Bacteria-phagocyte interactions: Fusobacterium-induced secretion of a neutrophil self-regulatory factor.

Direct interaction between Fusobacterium nucleatum and human neutrophils resulted in the secretion of a neutrophil self-regulatory factor(s). The secretion of this factor was bacteria specific, and depended on the integrity of the bacteria cell surface. Factor secretion occurred within 15 min of bacteria--neutrophil interaction. Pre-treatment of neutrophils with cytochalasin B but not sodium fluoride inhibited factor secretion. The factor was sensitive to trypsin and heat treatment. Ultrafiltration experiments showed that it has a molecular weight between 10,000 and 30,000 daltons. Its biologic role may be that of a molecular mediator for the recruitment of resting neutrophils so as to amplify the immunological and inflammatory response.

Antigens, Bacterial↗

PubMed1989

Recognition of Fusobacterium nucleatum subgroups Fn-1, Fn-2 and Fn-3 by ribosomal RNA gene restriction patterns.

DNA from representative strains of Fusobacterium nucleatum subgroups Fn-1, Fn-2 and Fn-3 was digested with restriction enzymes EcoRI and TaqI and the electrophoretically separated fragments hybridized with a 32P-16S rRNA gene probe from E. coli. The rRNA gene restriction patterns from DNA digested with either enzyme allowed the clustering of strains into the three subgroups. However, TaqI digested DNA yielded a wider distribution of taxonomically useful bands (ca 0.65 +/- 14.3 kbp) and the pattern produced was characteristic of each subgroup. The present method is a simple and reliable means of identifying the three subgroups of F. nucleatum and provides a useful method for further studies of the heterogeneity of F. nucleatum.

Blotting, Southern↗

PubMed1990

Diisopropylfluorophosphate-binding proteins in the outer membrane of Fusobacterium nucleatum: strain variations.

Six strains of Fusobacterium nucleatum were tested for their ability to react with [3H]diisopropylfluorophosphate (DFP), a serine protease inhibitor. Several cytoplasmic proteins were labelled but the strongest labelling was regularly observed in a few outer membrane proteins. The number and the molecular mass of the proteins detected varied according to the strain tested. A 61 kDa protein was labelled in all strains tested, including the two type strains ATCC 10953 and ATCC 25586. A 65 kDa protein was particularly strongly labelled in strains Fev1 and F6.

Bacterial Outer Membrane Proteins↗

PubMed1991

Isolation, purification and characterisation of 2-oxoglutarate reductase from Fusobacterium nucleatum.

2-Oxoglutarate reductase from Fusobacterium nucleatum was isolated by thiol-disulphide interchange covalent chromatography. The enzyme was purified approximately 4000-fold and had a molecular mass of 68 kDa. The Michaelis constants for 2-oxoglutarate and NADH were 6.4 x 10(-5) and 0.4 x 10(-5), respectively. The involvement of sulphahydryl groups in catalysis was shown from the inhibition of 2-oxoglutarate reduction in the presence of 2,2'-dipyridyl disulphide and reactivation with 2-mercaptoethanol. Allosteric effectors did not alter the rate of the reaction, or the enzyme stability. With the exception of 2-oxoglutarate, none of the other oxo-acids such as oxaloacetate, pyruvate, 2-oxobutyrate and glyoxylate were reduced. Although 2-oxoglutarate oxidised NADPH to a limited extent (3%), the enzyme was almost entirely specific towards NADH. 2-Oxoglutarate reductase was stable at 45 degrees C for 10 min, while incubation at 60 degrees C abolished all activity.

Alcohol Oxidoreductases↗

PubMed1993

Complete sequence of omp1, the structural gene encoding the 40-kDa outer membrane protein of Fusobacterium nucleatum strain Fev1.

The sequence of the omp1 gene coding for the 40-kDa outer membrane protein (OMP) of the Gram- oral bacterium, Fusobacterium nucleatum strain Fev1, has been determined. Degenerate oligodeoxyribonucleotide primers were used to prime the amplification of a 120-mer sequence of the gene. This sequence was successively used for constructing new primers applied in asymmetrical, symmetrical, and inverse polymerase chain reaction using as template genomic DNA, self-ligated DNA fragments, or fragments ligated into either pGEM-7Zf+ or pACYC184. The codon usage of the gene was unusual in that A or T was used as the third base in the codon triplets in all cases, except for those amino acids (aa) which have only one or two possible codon choices. Only 35 of the 61 sense codons were used. The aa sequence of the protein was deduced; it consisted of 348 aa (M(r) 39,954), which is in good agreement with the 40-kDa size estimated from electrophoretic analyses. The mature protein was preceded by a 20-aa signal peptide.

Amino Acid Sequence↗

PubMed1986

Studies on the purification of the leucocidin of Fusobacterium necrophorum and its neutralization by specific antisera.

Leucocidin from several strains of Fusobacterium necrophorum was partially purified by gel filtration on Fractogel HW55 (F), the majority of the activity being present in the 50 ml of filtrate collected after 1.1 void volumes had passed through the column (termed Fraction 1, or #1). The material also contained lipopolysaccharide in 12.5% SDS-PAGE gels run under reducing conditions, but the protein did not migrate into 7.5% PAGE gels run under non-reducing conditions. Rabbit and bovine antisera to the leucocidin possessed antibodies against antigens in concentrated, washed culture supernates from toxigenic F. necrophorum and neutralized the leucocidal activity of such supernates. Absorption of the antisera with homologous, washed F. necrophorum cells reduced ELISA antibody titres by greater than 50%, but decreased neutralization titres by 15%. Absorbed rabbit IgG anti-#1 precipitated a single rocket in crossed immunoelectrophoresis and identified two proteins, of molecular weights (M.W.) 14 000 and 13 000, and 1 protein of M.W. 13 500 in immunoblots from toxigenic and non-toxigenic strains, respectively. An additional protein of M.E. 103 000 was present after SDS-PAGE separation of supernates from toxigenic but not non-toxigenic F. necrophorum and was not present in whole cell components. It was considered that the leucocidin may be present in a dimeric form in culture supernates from toxigenic strains. Antisera to leucocidins from several strains of F. necrophorum exhibited variable neutralization titres against leucocidins from heterologous bacteria.

Agglutination Tests↗

PubMed1992

Aggregation of bovine platelets by Fusobacterium necrophorum.

Washed cell suspensions of biovar A strains of Fusobacterium necrophorum aggregated cattle platelets, but similar suspensions of biovar B strains did not. Platelets were also aggregated by heat-treated bacterial cells or the lipopolysaccharide of biovar A. No platelet aggregation occurred in the presence of the cell-free culture supernatant of biovar A and of all samples prepared from biovar B. Scanning electron microscopy revealed that aggregated platelets were not damaged. Platelet aggregation was inhibited by EDTA, aspirin and quinacrine, and lag time was retarded by these inhibitors, indicating the reaction was a Ca(2+)-dependent, cyclo-oxygenase sensitive event. Platelet aggregation may be a virulence marker, probably mediated by the lipopolysaccharide of F. necrophorum biovar A strains.

Animals↗