Clostridium difficile toxin B: Characterization and sequence of three peptides

Bisseret, Françoise; Keith, Gérard; Rihn, Bertrand; Amiri, Iradj; Werneburg, B; Girardot, Raymonde; Baldacini, Olivier; Green, Gaynor; Nguyen, Vu Khue; Monteil, H.

doi:10.1016/s0378-4347(00)82764-4

Cited by 17 publications

(6 citation statements)

References 17 publications

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“…5). These results support the studies of Bisseret et al [15] which indicate that the amino acid sequence of cytotoxin B is similar to enolases from rat and S. cerivisiae. …”

Section: Time (Minutes)supporting

confidence: 91%

Degradation of 2‐phosphoglycerate by cytotoxin B of Clostridium difficile

1990

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Cytotoxin B of C. difficile was highly purified by selective ammonium sulfate precipitation, Biogel A5m chromatography, phenyl boronate hydrophobic interaction chromatography and ultracentrifugation. The final cytotoxic product had a specific activity of 7.8 × 108 protein and showed a single protein band with an estimated molecular weight of 163000 when subjected to SDS‐PAGE. Immunoelectrophoresis of the final product showed a single precipitin arc. The addition of cytotoxin B to imidazole‐HCl buffer (pH 7.4) containing MgSO4, KCl and the substrate 2‐phosphoglycerate resulted in the formation of phosphoenolpyruvate as demonstrated by spectrophotometric analysis. Phosphoglycerate conversion was absent when the cytotoxin was heat‐inactivated of reacted with specific antitoxin prior to assay.

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“…5). These results support the studies of Bisseret et al [15] which indicate that the amino acid sequence of cytotoxin B is similar to enolases from rat and S. cerivisiae. …”

Section: Time (Minutes)supporting

confidence: 91%

Degradation of 2‐phosphoglycerate by cytotoxin B of Clostridium difficile

1990

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“…It has been reported that other glycolytic enzymes may be involved in a variety of cellular events in addition to their primary catalytic role [33,34], such as GAPDH, which has been found in the nucleus of certain cell types [35] and has been shown to bind DNA [36]. Several other functions have been reported for K-enolase : it is a heat shock protein in yeast [37], it has been identi¢ed as the eye lens crystallin d in reptiles and birds [38], it has been described as a component of the centrosome in HeLa cells [39], it functions as a plasminogen receptor in human peripheral blood cells [16], it is one of the hypoxia-inducible proteins in human cells [40], an immunodominant antigen in Candida albicans [41], and it has even been identi¢ed as toxin B in Clostridium di¤cile [42]. This report indicates an additional functional role for K-enolase carried out by an alternatively translated product whose structural and functional characteristics strongly support its identity with MBP-1.…”

Section: Discussionmentioning

confidence: 99%

ENO1 gene product binds to the c‐myc promoter and acts as a transcriptional repressor: relationship with Myc promoter‐binding protein 1 (MBP‐1)

et al. 2000

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“…These functions include its identi ed role as Hsp48, a heat shock protein in Saccharomyces cerevisiae, its structural role in crystallin formation in the turtle eye lens and its possible identity as cytotoxin B of Clostridium dif cile, in which it acts to disrupt the micro lament cytoskeleton by inhibiting adenosine diphosphate (ADP)-ribosylation of the guanosine 5 0 -triphosphate (GTP)-binding protein Rho [1][2][3][4][5][6]. It exhibits additional, nonglycolytic functions in some organisms.…”

Section: Introductionmentioning

confidence: 99%

Plasminogen-binding activity of enolase in the opportunistic pathogenPneumocystis carinii

Fox

Smulian²

2001

Med Mycol

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The glycolytic enzyme enolase is one of the most abundant proteins expressed in fungi and has been shown to be an immunodominant cell-wall-associated antigen of the pathogenic fungus, Candida albicans. Enolase has also been found on the surface of some mammalian cells where it functions as a plasminogen-binding motif and facilitator of plasminogen activation to plasmin. To investigate the immunogenicity of enolase in the opportunistic pathogen, Pneumocystis carinii, the genomic and complementary DNA (cDNA) enolase were cloned and characterized. The predicted protein comprises 433 amino-acid residues and shows extensive homology to other fungal enolases, including those of C. albicans (76%), Aspergillus oryzae (79%) and Saccharomyces cerevisiae (77%). The purified recombinant P. carinii enolase was immunogenic, and may be an important antigen and indicator of P. carinii infection. The active site and conformation metal ion-binding site residues necessary for dimerization and enzyme function are conserved in the predicted P. carinii enolase protein. Enolase of P. carinii is unique among the fungal enolases in that it possesses a catalytic carboxyl-terminal lysyl residue that was necessary and sufficient for the plasminogen-binding activity of the enolase of P. carinii. The activity of the plasminogen binding suggests its involvement in the local regulation of fibrinolysis within the alveolar space.

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Clostridium difficile toxin B: Characterization and sequence of three peptides

Cited by 17 publications

References 17 publications

Degradation of 2‐phosphoglycerate by cytotoxin B of Clostridium difficile

Degradation of 2‐phosphoglycerate by cytotoxin B of Clostridium difficile

ENO1 gene product binds to the c‐myc promoter and acts as a transcriptional repressor: relationship with Myc promoter‐binding protein 1 (MBP‐1)

Plasminogen-binding activity of enolase in the opportunistic pathogenPneumocystis carinii

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