Preliminary evidence of endotoxic activity of Bilophila wadsworthia

D'Alagni, Marina; Prete, Raffaele Del; Michele, Gian Piero de; Summanen, Paula; Finegold, Sydney M.; Miragliotta, G.

doi:10.1016/s1075-9964(95)80379-3

Cited by 22 publications

(10 citation statements)

References 10 publications

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“…The organism lacks classical virulence factors like capsules, fimbriae, and extracellular enzymes (2). However, preliminary studies have indicated that B. wadsworthia exerts cytotoxic effects on two cell lines, and endotoxic activity of B. wadsworthia has been described (2,34).…”

mentioning

confidence: 99%

Dissimilatory Sulfite Reductase (Desulfoviridin) of the Taurine-Degrading, Non-Sulfate-Reducing Bacterium Bilophila wadsworthia RZATAU Contains a Fused DsrB-DsrD Subunit

et al. 2001

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A dissimilatory sulfite reductase (DSR) was purified from the anaerobic, taurine-degrading bacterium Bilophila wadsworthia RZATAU to apparent homogeneity. The enzyme is involved in energy conservation by reducing sulfite, which is formed during the degradation of taurine as an electron acceptor, to sulfide. According to its UV-visible absorption spectrum with maxima at 392, 410, 583, and 630 nm, the enzyme belongs to the desulfoviridin type of DSRs. The sulfite reductase was isolated as an ␣ 2 ␤ 2 ␥ n (n > 2) multimer with a native size of 285 kDa as determined by gel filtration. We have sequenced the genes encoding the ␣ and ␤ subunits (dsrA and dsrB, respectively), which probably constitute one operon. dsrA and dsrB encode polypeptides of 49 (␣) and 54 kDa (␤) which show significant similarities to the homologous subunits of other DSRs. The dsrB gene product of B. wadsworthia is apparently a fusion protein of dsrB and dsrD. This indicates a possible functional role of DsrD in DSR function because of its presence as a fusion protein as an integral part of the DSR holoenzyme in B. wadsworthia. A phylogenetic analysis using the available Dsr sequences revealed that B. wadsworthia grouped with its closest 16S rDNA relative Desulfovibrio desulfuricans Essex 6.Bilophila wadsworthia is a strictly anaerobic, gram-negative bacterium (2) which belongs to the family Desulfovibrionaceae in the delta subdivision of the Proteobacteria, but does not reduce sulfate (2, 25). B. wadsworthia has been found quite frequently in patients with appendicitis and its complications and is the third most common anaerobic isolate in such infections (11), but can also be isolated from a wide variety of other infections, e.g., biliary tract infection (41), liver abscess (41), and ear infections (39). B. wadsworthia has also been found in the normal fecal flora (2). The organism lacks classical virulence factors like capsules, fimbriae, and extracellular enzymes (2). However, preliminary studies have indicated that B. wadsworthia exerts cytotoxic effects on two cell lines, and endotoxic activity of B. wadsworthia has been described (2, 34).We recently isolated from a communal sewage plant a strain of B. wadsworthia which utilizes organic sulfonates (e.g., taurine [2-aminoethanesulfonate]) as a carbon source and electron sink. B. wadsworthia respires taurine anaerobically with electrons derived mainly from formate oxidation and oxidation of the taurine carbon (25). Taurine is transaminated to sulfoacetaldehyde (22), which is cleaved to sulfite and an unidentified organic product (K. Denger and A. M. Cook, unpublished). Finally, sulfite is reduced to sulfide by a dissimilatory sulfite reductase (DSR) (6, 25). In addition, sulfite or thiosulfate serves as an electron acceptor for anaerobic respiration with formate as the electron donor in B. wadsworthia (25).DSR, a key enzyme in dissimilatory sulfate reduction, occurs in all organisms capable of reducing sulfite during anaerobic respiration investigated so far (9, 33). Otherwise, DSRs are rare....

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confidence: 99%

Dissimilatory Sulfite Reductase (Desulfoviridin) of the Taurine-Degrading, Non-Sulfate-Reducing Bacterium Bilophila wadsworthia RZATAU Contains a Fused DsrB-DsrD Subunit

et al. 2001

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“…Although abscess formation is usually associated with presence of capsular polysaccharide, Bilophila does not appear to have a capsule; thus the specific virulence factor responsible for abscess formation is not yet known. As do most Gram-negative bacteria, Bilophila species induces clotting of Limulus amoebocyte lysate and promotes procoagulant activity by human mononuclear cells, both characteristics associated with the presence of endotoxin [9]. However, the magnitude of the endotoxin-like activity of the Bilophila species tested was less than that observed for typical Gramnegative organisms [9].…”

Section: Characteristics Of the Organismmentioning

confidence: 89%

“…As do most Gram-negative bacteria, Bilophila species induces clotting of Limulus amoebocyte lysate and promotes procoagulant activity by human mononuclear cells, both characteristics associated with the presence of endotoxin [9]. However, the magnitude of the endotoxin-like activity of the Bilophila species tested was less than that observed for typical Gramnegative organisms [9]. Tissue culture assays for cytotoxicity demonstrated some cytotoxic activity in two cell lines, but this factor has not been further studied.…”

Section: Characteristics Of the Organismmentioning

confidence: 95%

Bilophila wadsworthia: a Unique Gram-negative Anaerobic Rod

Baron

1997

Anaerobe

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“…Binding activity to laminin was reduced in eight further-tested strains by preincubation of the bacteliminary studies have indicated that B. wadsworthia exerts cytotoxic effects on two cell lines, and the endotoxic activity of B. wadrial cells with laminin. For six strains, preincubation with laminin was more inhibitory than preincubation with fibrinogen, indicating sworthia has been described [2,3]. The aim of the present study was to investigate the adhesion of this species to fibronectin and specificity of the laminin binding.…”

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confidence: 92%

Adherence of Bilophila wadsworthia to Laminin and Fibronectin.

Schumacher

1997

CLIN INFECT DIS

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Bilophila wadsworthia is a recently described anaerobic rod that and 116.1% and binding to fibronectin that ranged between 7.1% and 106.6%. Sixteen (17.9%) of the 89 strains (8 appendiceal is mainly associated with appendicitis but is also associated with other intraabdominal and extraabdominal infections [1]. This speisolates and 9 fecal isolates) showed marked laminin adherence, and nine of these strains also showed adherence to fibronectin, but cies lacks classic virulence factors such as capsules, fimbriae, or extracellular enzymes (lipase and lecithinase) [2]. However, preto a less pronounced degree. Binding activity to laminin was reduced in eight further-tested strains by preincubation of the bacteliminary studies have indicated that B. wadsworthia exerts cytotoxic effects on two cell lines, and the endotoxic activity of B. wadrial cells with laminin. For six strains, preincubation with laminin was more inhibitory than preincubation with fibrinogen, indicating sworthia has been described [2,3]. The aim of the present study was to investigate the adhesion of this species to fibronectin and specificity of the laminin binding. Adherence to fibronectin was reduced by preincubation with both fibronectin and fibrinogen. laminin.Eighty-nine strains of B. wadsworthia that were collected during Binding to laminin and fibronectin was strongly reduced in protease-and trypsin-treated bacterial cells, whereas periodate treata study of appendicitis in children (the strains included 51 isolates obtained from acutely or complicated inflamed appendices and 37 ment had no major effect. Binding activity was not influenced by the addition of various carbohydrates to the test system. fecal isolates) were tested for their ability to bind to laminin and fibronectin in protein-coated microtiter plates. A Bacteroides fraGlycoproteins such as laminin, fibronectin, and collagen are known to function as ligands for pathogenic microorganisms (e.g., gilis strain (ZB1, a blood culture isolate) with known laminin and fibronectin binding activity was used as a positive control, and Staphylococcus aureus, Streptococcus pyogenes, and Candida albicans). Binding to these proteins mediates adherence not only Micrococcus luteus was used as a negative control.Test strains were labeled with N-hydroxysuccinimidobiotin/ to host epithelial cells but also to extracellular matrix and basal membranes, and this is an important step in the development of dimethyl sulfoxide, as described by Ofek et al. [4]. Adherent bacteria were detected with the aid of peroxidase-linked avidin reagent infectious processes. The ability of B. fragilis to adhere to the basal membrane-associated glycoprotein laminin is significantly (ExtrAvidin-Horseradish Peroxidase; Sigma E2886, Sigma, Deisenhofen, Germany) and o-phenylenediamine dihydrochloride stronger than that of other Bacteroides species, and this finding may provide a possible explanation for the preponderance of (OPD; Sigma P9187) as the peroxidase substrate. Results were measured in a Milenia kinetic analyzer (Dia...

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Preliminary evidence of endotoxic activity of Bilophila wadsworthia

Cited by 22 publications

References 10 publications

Dissimilatory Sulfite Reductase (Desulfoviridin) of the Taurine-Degrading, Non-Sulfate-Reducing Bacterium Bilophila wadsworthia RZATAU Contains a Fused DsrB-DsrD Subunit

Dissimilatory Sulfite Reductase (Desulfoviridin) of the Taurine-Degrading, Non-Sulfate-Reducing Bacterium Bilophila wadsworthia RZATAU Contains a Fused DsrB-DsrD Subunit

Bilophila wadsworthia: a Unique Gram-negative Anaerobic Rod

Adherence of Bilophila wadsworthia to Laminin and Fibronectin.

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