A comparative biochemical, pharmacological and immunological study of Clostridium novyi alpha-toxin, C. difficile toxin B and C. sordellii lethal toxin.

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RESEARCH PRODUCT

A comparative biochemical, pharmacological and immunological study of Clostridium novyi alpha-toxin, C. difficile toxin B and C. sordellii lethal toxin.

A. Oksche P Bette F Mauler Michel-robert Popoff Ernst Habermann Christoph Von Eichel-streiber

subject

Bacterial Toxins Clostridium sordellii Clostridium difficile toxin B Chick Embryo Biology Pulmonary Artery Toxicology medicine.disease_cause Median lethal dose Microbiology Lethal Dose 50 chemistry.chemical_compound Mice Bacterial Proteins medicine Animals Microscopy Phase-Contrast Uridine Cells Cultured Clostridium Adenosine Diphosphate Ribose Toxin Clostridioides difficile Cytotoxins Rats Inbred Strains biology.organism_classification Clostridium novyi Uridine Rats Endothelial stem cell chemistry ADP-ribosylation Potassium Female Endothelium Vascular

description

The three clostridial cytotoxins, i.e. alpha-toxin of C. novyi (Tox alpha-nov), toxin B of C. difficile (ToxB-dif) and lethal toxin of C. sordellii (LT-sor) consist of single peptide chains of about 200,000 (Tox alpha-nov), 250,000 (LT-sor) and 275,000 (ToxB-dif) mol. wts. ToxB-dif and LT-sor but not Tox alpha-nov cross-reacted with rabbit polyclonal antibodies. Toxicity upon i.v. injection in mice was similar (LD50, 100 hr, 50-200 ng/kg) and was characterized by a slowly developing fluid loss into the interstitial space. When injected into the rat paw the toxins caused a delayed local edema lasting for days. In vitro the three toxins provoked a persistent retraction of endothelial cells cultured from pig pulmonary artery. ToxB-dif and Tox alpha-nov triggered the accumulation of F-actin in the perinuclear region at the expense of the tight peripheral bands whereas LT-sor led to a random loss of microfilament structure. The toxins inhibited uridine incorporation into endothelial or chicken embryonic cells whereas T 84 cells responded by an about 10-fold increase of uridine incorporation. Neither toxin ADP-ribosylated actin. The similarities between the three cytotoxins warrant their arrangement into a common group which perturbs the microfilament system.

year	journal	country	edition	language
1991-01-01	Toxicon : official journal of the International Society on Toxinology

10.1016/0041-0101(91)90224-f https://pubmed.ncbi.nlm.nih.gov/1926186