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Wolinella recta, Wolinella curva, Bacteroides ureolyticus, and Bacteroides gracilis are microaerophiles, not anaerobes.

Although the nonfermentative, asaccharolytic, putative anaerobes Wolinella curva, Wolinella recta, Bacteroides ureolyticus, and Bacteroides gracilis are phylogenetically related to the true campylobacters, the type strains of these species exhibited O2-dependent microaerophilic growth in brucella broth and on brucella agar. The optimum O2 levels for growth of these strains ranged from 4 to 14% in brucella broth and from 2 to 8% on brucella agar, when H2 was provided as the electron donor. No growth occurred under 21% O2, and scant or no growth occurred under anaerobic conditions unless fumarate or nitrate was provided as a terminal electron acceptor. Aspartate, asparagine, and malate also served as apparent electron acceptors. The organisms were catalase negative and, except for B. gracilis, oxidase positive. Catalase added to brucella broth enhanced growth. O2 uptake by all species was inhibited by cyanide and 2-heptyl-4-hydroxyquinoline N-oxide. We concluded that these organisms are not anaerobes but instead are microaerophiles, like their campylobacter relatives.

Anaerobiosis↗

Comparison of strains of gram-negative, anaerobic, agar-corroding rods isolated from soft tissue infections in cats and dogs with type strains of Bacteroides gracilis, Wolinella recta, Wolinella succinogenes, and Campylobacter concisus.

A total of 64 strains of gram-negative, asaccharolytic, anaerobic, agar-corroding, rod-shaped bacteria from soft-tissue infections of cats and dogs were compared with other agar-corroding, anaerobic organisms isolated from human periodontal pockets (Wolinella recta ATCC 33238T), bovine rumens (Wolinella succinogenes ATCC 29543T), and gingival crevices of humans (Bacteroides gracilis ATCC 33236T and Bacteroides ureolyticus NCTC 10941T). Campylobacter concisus ATCC 33237T (from human gingival crevices) which did not corrode agar but which biochemically resembled organisms in this group was also included in this study. Although the type strains of W. recta, W. succinogenes, and B. gracilis resembled the animal strains phenotypically and in DNA base ratios, none had bacterial protein patterns (as indicated by isoelectric focusing) identical with the animal strains studied. The animal strains could be divided into motile and nonmotile groups. The motile animal strains were similar biochemically but could be divided into three groups by isoelectric focusing of bacterial proteins. Some had cell wall ultrastructural features identical with W. recta; others had the smooth walls of conventional gram-negative organisms. One group of nonmotile animal strains closely resembled B. gracilis phenotypically, and they had the cell wall ultrastructure of conventional gram-negative bacteria as described previously (4). The other nonmotile group had cell wall ultrastructure like that of W. recta.

Agar↗

Cytochrome composition and oxygen-dependent respiration-driven proton translocation in Wolinella curva, Wolinella recta, Bacteroides ureolyticus, and Bacteroides gracilis.

The membrane fractions of the microaerobically grown type strains of Wolinella curva, Wolinella recta, Bacteroides ureolyticus, and Bacteroides gracilis contained membrane-bound cytochrome b, cytochrome c, and CO-binding cytochrome c. Soluble cytochrome c and CO-binding cytochrome c were also present. Although B. gracilis is oxidase negative, it possessed cytochrome c. With H2 or formate as the electron donor, proton efflux from anaerobic cells occurred upon addition of a pulse of oxygen. With formate as the electron donor, the H+/O ratios of W. curva, W. recta, B. ureolyticus, and B. gracilis were 0.75, 1.66, 2.06, and 2.04, respectively. With H2 as the electron donor, the H+/O ratios of W. curva, B. ureolyticus, and B. gracilis were 1.25, 1.97, and 2.36, respectively. Proton translocation was inhibited by the protonophore carbonylcyanide m-chlorophenylhydrazone. The results confirm that the organisms are not anaerobes but are microaerophiles capable of respiring with oxygen.

Bacteroides↗

Revision of Campylobacter, Helicobacter, and Wolinella taxonomy: emendation of generic descriptions and proposal of Arcobacter gen. nov.

Hybridization experiments were carried out between DNAs from more than 70 strains of Campylobacter spp. and related taxa and either 3H-labeled 23S rRNAs from reference strains belonging to Campylobacter fetus, Campylobacter concisus, Campylobacter sputorum, Campylobacter coli, and Campylobacter nitrofigilis, an unnamed Campylobacter sp. strain, and a Wolinella succinogenes strain or 3H- or 14C-labeled 23S rRNAs from 13 gram-negative reference strains. An immunotyping analysis of 130 antigens versus 34 antisera of campylobacters and related taxa was also performed. We found that all of the named campylobacters and related taxa belong to the same phylogenetic group, which we name rRNA superfamily VI and which is far removed from the gram-negative bacteria allocated to the five rRNA superfamilies sensu De Ley. There is a high degree of heterogeneity within this rRNA superfamily. Organisms belonging to rRNA superfamily VI should be reclassified in several genera. We propose that the emended genus Campylobacter should be limited to Campylobacter fetus, Campylobacter hyointestinalis, Campylobacter concisus, Campylobacter mucosalis, Campylobacter sputorum, Campylobacter jejuni, Campylobacter coli, Campylobacter lari, and "Campylobacter upsaliensis." Wolinella curva and Wolinella recta are transferred to the genus Campylobacter as Campylobacter curvus comb. nov. and Campylobacter rectus comb. nov., respectively. Bacteroides gracilis and Bacteroides ureolyticus are generically misnamed and are closely related to the genus Campylobacter. Campylobacter nitrofigilis, Campylobacter cryaerophila, and an unnamed Campylobacter sp. strain constitute a new genus, for which the name Arcobacter is proposed; this genus contains two species, Arcobacter nitrofigilis comb. nov. (type species) and Arcobacter cryaerophilus comb. nov. Wolinella succinogenes so far is the only species of the genus Wolinella. The genus Helicobacter is also emended; Campylobacter cinaedi and Campylobacter fennelliae are included in this genus as Helicobacter cinaedi comb. nov. and Helicobacter fennelliae comb. nov., respectively. The genus "Flexispira," with "Flexispira rappini" as the only species, is closely related to the genus Helicobacter. The free-living, sulfur-reducing campylobacters do not belong to any of these genera; they probably constitute a distinct genus within rRNA superfamily VI.

Bacterial Typing Techniques↗

Multivariate analyses of cellular fatty acids in Bacteroides, Prevotella, Porphyromonas, Wolinella, and Campylobacter spp.

The genera Bacteroides, Wolinella, and Campylobacter contain several similar species that require taxonomic revision. Fatty acid profiles of whole bacterial cells have proven useful for taxonomy. In this study, cellular fatty acids from Bacteroides, Prevotella, Porphyromonas, Wolinella, and Campylobacter spp. were identified and quantitated by gas chromatography and gas chromatography-mass spectrometry, and the data were subjected to principal component analyses. Bacteroides fragilis, the type species of the genus Bacteroides, was distinct from the other organisms. While Bacteroides gracilis, Wolinella succinogenes, Wolinella curva, Wolinella recta, and Campylobacter fetus subsp. venerealis were close to each other, Prevotella (Bacteroides) buccae, Prevotella oralis, Prevotella oris, Prevotella disiens, Prevotella veroralis, Prevotella heparinolyticus, Porphyromonas (Bacteroides) endodontalis, and Bacteroides ureolyticus could be distinguished. B. fragilis was characterized by the presence of C3OH-i-1-, Ca-15, and Ci-15 and the absence of C12:0 and unsaturated fatty acids. For comparison, B. gracilis, B. ureolyticus, W. succinogenes, W. curva, W. recta, and Campylobacter fetus subsp. venerealis contained C12:0, C16:1, C18:1, and C3-OH-14 acids but lacked branched hydroxy and branched nonhydroxy acids. B. gracilis and B. ureolyticus are not "true" bacteroides.

Bacteria↗

Comparative study of lipopolysaccharides from Wolinella recta, W. curva, W. succinogenes and Campylobacter sputorum ssp. sputorum.

Lipopolysaccharides (LPS) were extracted from cells of Wolinella recta ATCC 33238, W. curva ATCC 33224, W. succinogenes ATCC 29543 and Campylobacter sputorum ssp. sputorum A 3563 by a hot phenol-water method and purified by nuclease treatment and by repeated ultracentrifugation. Chemical compositions of the purified LPS including fatty acid and sugar composition were examined and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was performed. All LPS preparations contained a monosaccharide identified as L-glycero-D-mannoheptose, and another heptose isomer identified as D-glycero-D-mannoheptose was a typical constituent of the LPS from all three Wolinella species.

Campylobacter↗

The function of methyl-menaquinone-6 and polysulfide reductase membrane anchor (PsrC) in polysulfide respiration of Wolinella succinogenes.

Wolinella succinogenes grows by oxidative phosphorylation with polysulfide as terminal electron acceptor and either H2 or formate as electron donor (polysulfide respiration). The function of the respiratory chains catalyzing these reactions was investigated. Proteoliposomes containing polysulfide reductase (Psr) and either hydrogenase or formate dehydrogenase isolated from the membrane fraction of Wolinella succinogenes catalyzed polysulfide respiration, provided that methyl-menaquinone-6 isolated from W. succinogenes was also present. The specific activities of electron transport were commensurate with those of the bacterial membrane fraction. Using site-directed mutagenesis, certain residues were substituted in PsrC, the membrane anchor of polysulfide reductase. Replacement of Y23, D76, Y159, D218, E225 or R305 caused nearly full inhibition of polysulfide respiration without affecting the activity of Psr, which was still bound to the membrane. These residues are predicted to be located in hydrophobic helices of PsrC, or next to them. Substitution of 13 other residues of PsrC either caused partial inhibition ofblankpolysulfide respiration or had no effect. The function of methyl-menaquinone-6, which is thought to be bound to PsrC, is discussed.

Amino Acid Sequence↗

Detection of a putative novel Wolinella species in patients with squamous cell carcinoma of the esophagus.

BACKGROUND: Certain regions of South Africa exhibit an extraordinarily high incidence of esophageal carcinoma that develops via an esophagitis-dysplasia-carcinoma sequence. Bacteria belonging to the family Helicobacteraceae are candidates for involvement in the initiation of the esophagitis. We investigated patients with esophageal carcinoma for the occurrence of Helicobacter-related species. METHODS: Biopsies from tumor and nonlesional tissue of the esophagus from nine patients with squamous cell carcinoma were investigated for Helicobacteraceae using a PCR-based method targeting the 16S rRNA gene. RESULTS: Four out of nine patients tested negative, while samples from the other five patients revealed an infection by different Helicobacter species. Sequence analysis of the PCR fragments led to the identification of a hitherto unknown bacterium in three of these patients. Phylogenetically, this bacterium was assigned to the genus Wolinella within the family of Helicobacteraceae. Helicobacter pylori was identified in three patients, and one revealed a coinfection with the novel Wolinella species. CONCLUSIONS: Helicobacteraceae were detected in approximately 50% of South African patients with esophageal carcinoma. Furthermore, a novel bacterium was identified that might be linked to the enhanced incidence of esophagitis and subsequent malignant disease in South Africa.

Biopsy↗

Nucleotide sequence of the Wolinella succinogenes flagellin, which contains in the antigenic domain two conserved regions also present in Campylobacter spp. and Helicobacter pylori.

Wolinella succinogenes possesses one polar flagellum, which shows a characteristic surface pattern of parallel lines along the axis of the filament in electron microscopic images. We determined the gene sequence of the Wolinella flagellin, which is, as in most other bacteria, the only structural component of the filament. Sequence comparison with other members of the Proteobacteria revealed two highly conserved regions in the central part of the flagellin molecule among Campylobacter spp. and Helicobacter pylori, an area that had previously been described as highly variable. Similar surface patterns are found in related polarly flagellated bacteria, but not in Escherichia coli and Bacillus subtilis, which also lack these conserved regions.

Amino Acid Sequence↗

PA-1, a Versatile Anaerobe Obtained in Pure Culture, Catabolizes Benzenoids and Other Compounds in Syntrophy with Hydrogenotrophs, and P-2 plus Wolinella sp. Degrades Benzenoids.

Methanogenic enrichments catabolizing 13 mM phenylacetate or 4 mM phenol were established at 37 degrees C, using a 10% inoculum from a municipal anaerobic digester. By using agar roll tubes of the basal medium plus 0.1% yeast extract-25 mM fumarate, a hydrogenotrophic lawn of Wolinella succinogenes and phenol or phenylacetate, strains P-2 and PA-1, respectively, were isolated in coculture with W. succinogenes. With the lawn deleted, PA-1 was isolated in pure culture. Strain P-2 is apparently a new species of anaerobic, motile, gram-negative, spindle-shaped, small rod that as yet has been grown only in coculture with W. succinogenes. It used phenol, hydrocinnamate, benzoate, and phenylacetate as energy sources. Product recovery by the coculture, per mole of phenol and 4.4 mol of fumarate used, included 2.03, 0.12, 0.08, and 3.23 mol, respectively, of acetate, propionate, butyrate, and succinate. Carbon recovery was 75% and H recovery was 80%, although CO(2) and a few other possible products were not determined. That P-2 is an obligate proton-reducing acetogen and possible pathways for its degradation of phenol are discussed. Strain PA-1 is apparently a new species of anaerobic, motile, relatively small, gram-negative rod. It utilized compounds such as phenylacetate, hydrocinnamate, benzoate, phenol, resorcinol, gallate, 4-aminophenol, 2-aminobenzoate, pyruvate, Casamino Acids, and aspartate as energy sources in coculture with W. succinogenes. Per mole of phenylacetate and 1.44 mol of fumarate used, 1.04, 0.53, and 0.78 mol of acetate, propionate, and succinate, respectively, were recovered from the coculture. Only about 50% of the carbon and H were recovered. In coculture with Methanospirillum hungatei, 0.96 mol of acetate and 0.25 mol of methane were recovered per mol of pyruvate used; 0.90 mol of acetate and 0.33 mol of methane, per mol of fumarate used; 0.93 mol of acetate and 0.54 mol of methane, per mol of aspartate used; and 1.71 mol of acetate and 0.57 mol of methane, per mol of glucose used. Carbon and H recoveries, assuming CO(2) and ammonia were produced in stoichiometric amounts, were 97 and 98% for pyruvate, 72.5 and 82% for fumarate, 96.5 and 98% for aspartate, and 61.8 and 76% for glucose. No explanation such as contamination could be found for the fact that the coculture PA-1 plus Wolinella sp. did not use glucose; after growth with M. hungatei on pyruvate, however, the latter coculture used glucose. The PA-1 pure culture produced 0.86 mol of propionate per mol of succinate used during growth. PA-1 produced a small amount of H(2). Strain PA-1 is the most versatile anaerobic bacterium yet known that catabolizes monobenzenoids in the absence of electron acceptors such as sulfate or nitrate.

Journal Article↗

Campylobacter-Wolinella group organisms are the only oral bacteria that form arylsulfatase-active colonies on a synthetic indicator medium.

Most oral bacteria tested formed colonies on a chemically defined medium with a chromogenic arylsulfatase substrate. Arylsulfatase activity was, however, restricted to Campylobacter-Wolinella group organisms, including Wolinella recta, a possible periodontopathogen. W. recta was the only arylsulfatase-active species against which consistently high levels of antibody were detected in human sera.

Arylsulfatases↗

Extraction, purification, and characterization of major outer membrane proteins from Wolinella recta ATCC 33238.

The outer membrane of Wolinella recta ATCC 33238 was isolated by French pressure cell disruption and differential centrifugation. Outer membrane proteins (OMPs) were solubilized by Zwittergent 3.14 extraction and separated by DEAE-Sephacel ion-exchange chromatography. The major OMPs that were found in W. recta ATCC 33238 and in several other Wolinella spp. consisted of proteins with apparent molecular masses of 51, 45, and 43 kDa. These three conserved proteins were purified to essential homogeneity by one- and two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and characterized chemically. Heating at between 75 and 100 degrees C revealed both the 43- and 51-kDa proteins to be heat modified from apparent molecular masses of 32 and 38 kDa, respectively. The 45-kDa protein was unmodified at all temperatures tested. Two-dimensional isoelectric focusing-SDS-PAGE revealed the 51-kDa protein to be composed of multiple pIs between a pH of 5.0 and greater than 8.0 while the 43- and 45-kDa proteins had a pI of approximately 6.0. N'-terminal amino acid sequence analysis of the first 30 to 40 amino acids and search of the Protein Identification Resource data base for similar proteins only revealed the 43-kDa protein to be similar to the P.69 OMP of Bordetella pertussis; however, the homology was weak (33%). Amino acid analysis revealed the 43-kDa protein to be noncharged and the 45- and 51-kDa proteins to be hydrophilic, containing between 38 to 42% polar residues but no cysteine. This study reports the purification and partial characterization of three conserved proteins in W. recta ATCC 33238.

Amino Acid Sequence↗

Cell surface protein antigen from Wolinella recta ATCC 33238T.

A high-molecular-weight (approximately 150,000) protein was selectively isolated by acid extraction from the cell surface of Wolinella recta and purified by negative adsorption on DEAE-cellulose and gel filtration. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis showed that this protein was found in W. recta but not in other Wolinella species, such as W. curva and W. succinogenes. Sera from patients with periodontitis reacted strongly with this protein antigen, whereas sera from healthy donors showed little or no reactivity, as determined by immunoblotting analysis. In serum, titers of immunoglobulin G antibodies to the protein antigen were significantly higher in patients with periodontitis than in periodontally healthy donors, as detected by an enzyme-linked immunosorbent assay.

Antigens, Bacterial↗

Wolinella recta and spirochetes in relation to alteration of probing depth in a population without regular dental care.

The purpose of this study was to determine the occurence of spirochetes and Wolinella sp. in untreated, nonselected subjects and to relate the presence of these organisms to changes in probing depth over a period of 180 days. Clinical parameters were recorded and subgingival microbial samples were taken mesiobuccally on the upper first molars of 120 subjects (mean age 37 +/- 14 years) with a history of no regular dental care. The number of motile rods and spirochetes were determined in the darkfield microscope. The samples were cultured anaerobically on a selective medium which favoured the growth of Wolinella sp. The grown microorganisms were submitted to a number of tests for the identification of W. recta. Of the 172 sites investigated longitudinally, 73 harboured motile rods, 45 harboured W. recta and 88 harboured spirochetes. 13 sites showed an increase in probing depth of greater than or equal to 2 mm. A multiple regresssion analysis revealed no statistically significant correlation between the numbers of W. recta at baseline and the likelihood of breakdown during the observation period. The number of spirochetes at baseline, however, was significantly related to the changes of probing depth (p greater than 0.001). It was concluded that spirochetes were more closely related to changes of probing depth in this population than the number of W. recta organisms present.

Adult↗

A diffusion-controlled step in the catalytic cycle of nitrous oxide reductase from Wolinella succinogenes.

The viscosity test was applied to the highly active nitrous oxide reductase purified from Wolinella succinogenes to determine whether the catalytic cycle may contain a diffusion-controlled step. For this test, the benzyl viologen cation (BV+)-N2O oxidoreductase reaction, which exhibits a kcatBV/KmBV approximately 2 x 10(8) M-1 s-1 at 23 degrees C and pH 7.1, was run in solutions of nominally nondenaturing viscogens that were used to increase microviscosity. The parameters kcatN2O and kcatBV were unaffected by viscosity in the range of viscogen concentrations that were not inhibitory and where the data were well behaved. KmBV, but not KmN2O, was observed to increase linearly with relative viscosity with a slope of 0.14 for all viscogens surveyed. The results, when considered in the context of a plausible kinetic model for the BV(+)-N2O oxidoreductase reaction, suggest that one of the two one-electron reactions between BV+ and enzyme is diffusion-controlled but only partially rate determining. The ratio of the second-order-rate constants for these two one-electron steps is estimated to be about 6.1, and the larger rate constant to be about 1.1 x 10(9) M-1 s-1. There would appear to be no diffusion-controlled step associated with the half-reaction which results in reduction of N2O to N2.

Diffusion↗

Cloning and nucleotide sequence of the structural genes encoding the formate dehydrogenase of Wolinella succinogenes.

The formate dehydrogenase of Wolinella succinogenes is a membraneous molybdo-enzyme which is involved in phosphorylative electron transport. The gene (fdhA) encoding the largest subunit was isolated from a gene bank by immunological screening. The fdhA gene was located in an apparent transcriptional unit (fdhA,B,C,D) together with three more structural genes. The N-terminal sequences of three polypeptides present in the isolated enzyme were found to map within the fdhA, B and C structural genes. A polypeptide corresponding to fdhD was not detected in the enzyme preparation. This suggested that the functional formate dehydrogenase was made up of three or four different subunits. The genes fdhA and C encode larger preproteins which differ from the corresponding mature proteins by N-terminal signal peptides. The N-terminal half of the mature FdhA is homologous to the larger subunits of the formate dehydrogenases of E. coli (formate-hydrogenlyase linked) and Methanobacterium formicicum as well as to three bacterial reductases containing molybdenum. It harbours a conserved cysteine cluster and two more domains which may be involved in binding the molybdenum cofactor. FdhB may represent an iron-sulphur protein, twelve cysteine residues of which are arranged in two clusters which are typical of ligands of the iron-sulfur centers in ferredoxins. FdhC is a hydrophobic protein with four predicted transmembrane segments, which appears to be identical with the cytochrome b present in the isolated formate dehydrogenase. It may form the membrane anchor of the enzyme and react with the bacterial menaquinone.

Amino Acid Sequence↗

DMSO respiration by the anaerobic rumen bacterium Wolinella succinogenes.

The anaerobic rumen bacterium Wolinella succinogenes was able to grow by respiration with dimethylsulphoxide (DMSO) as electron acceptor and formate or H2 as electron donors. The growth yield amounted to 6.7 g and 6.4 g dry cells/mol DMSO with formate or H2 as the donors, respectively. This suggested an ATP yield of about 0.7 mol ATP/mol DMSO. Cell homogenates and the membrane fraction contained DMSO reductase activity with a high Km (43 mM) for DMSO. The electron transport from H2 to DMSO in the membranes was inhibited by 2-(heptyl)-4-hydroxyquinoline N-oxide, indicating the participation of menaquinone. Formation of DMSO reductase activity occurred only during growth on DMSO, presence of other electron acceptors (fumarate, nitrate, nitrite, N2O, and sulphur) repressed the DMSO reductase activity. DMSO can therefore be used by W. succinogenes as an acceptor for phosphorylative electron transport, but other electron acceptors are used preferentially.

Anaerobiosis↗

Cysteine-mediated electron transfer in syntrophic acetate oxidation by cocultures of Geobacter sulfurreducens and Wolinella succinogenes.

Syntrophic cocultures of Geobacter sulfurreducens and Wolinella succinogenes oxidize acetate with nitrate as terminal electron acceptor. It has been postulated earlier that electrons are transferred in these cocultures not via hydrogen, but via a different carrier, e.g., a small c-type cytochrome that is detected in the supernatant of growing cultures. In the present study, L -cysteine, which was provided as a reducing agent, was found to mediate the electron transfer between the two partners. Low concentrations of L -cysteine or L -cystine (10-100 microM) supported syntrophic growth, and no acetate oxidation was observed in the absence of cysteine or cystine. Cell suspensions of G. sulfurreducens or coculture cell suspensions reduced cystine to cysteine, and suspensions of W. succinogenes or coculture suspensions oxidized cysteine with nitrate, as measured by the formation or depletion of free thiol groups. Added cysteine was rapidly oxidized by the coculture during growth, but the formed cystine was not entirely rereduced even under acceptor-limited conditions. The redox potential prevailing in acetate-oxidizing cocultures was -160 to -230 mV. Sulfide at low concentrations supported syntrophic growth as well and could replace cysteine. Neither growth nor acetate degradation was found with D-cysteine, homocysteine, cysteamine, 3-mercaptopropionate, dithiothreithol, thioglycolate, glutathione, coenzyme M, dimethylsulfoxide, trimethylamine- N-oxide, anthraquinone-2,6-disulfonate, or ascorbate.

Acetates↗