Disease relevance of pCPF4969_31

• The amino acid sequence of the enterotoxin from Clostridium perfringens type A [1].
• Clostridium perfringens type A isolates carrying an enterotoxin (cpe) gene are an important cause of human gastrointestinal diseases, including food poisoning, antibiotic-associated diarrhoea (AAD) and sporadic diarrhoea (SD) [2].
• Cloning, nucleotide sequencing, and expression of the Clostridium perfringens enterotoxin gene in Escherichia coli [3].
• The enterotoxin gene (cpe) is usually chromosomal in food poisoning isolates but plasmid-borne in AAD/SPOR isolates [4].
• The contribution of enterotoxigenic C. perfringens to this association, was assessed by use of the reverse passive latex agglutination test for enterotoxin (RPLA; Oxoid Unipath) and vero cell toxicity neutralized by antitoxin on stored faecal samples and sporulated faecal isolates of C. perfringens [5].

High impact information on pCPF4969_31

• Clostridium perfringens enterotoxin is a superantigen reactive with human T cell receptors V beta 6.9 and V beta 22 [6].
• Toxin A, an enterotoxin from Clostridium difficile, mediates pseudomembranous colitis in humans [7].
• Toxin A, a 308,000-Mr enterotoxin from Clostridium difficile, mediates antibiotic-associated diarrhea and colitis in humans [8].
• Enterotoxin A is one of the major virulence factors of Clostridium difficile, and the causative agent of antibiotic-associated pseudomembranous colitis [9].
• The purpose of this study was to characterize the surface receptor for toxin A, the enterotoxin from Clostridium difficile, on rabbit intestinal brush borders (BB) and on rat basophilic leukemia (RBL) cells [10].

Chemical compound and disease context of pCPF4969_31

• Comparative Effects of Osmotic, Sodium Nitrite-Induced, and pH-Induced Stress on Growth and Survival of Clostridium perfringens Type A Isolates Carrying Chromosomal or Plasmid-Borne Enterotoxin Genes [11].
• The amino acid sequence of the enterotoxin from Clostridium perfringens type A was determined by analysis of peptides derived from the protein by digestion with trypsin chymotrypsin, thermolysin, pepsin, a lysine-specific protease [1].
• Stimulation of Clostridium perfringens enterotoxin formation by caffeine and theobromine [12].
• Enterotoxin-like protein was extracted from spores of three enterotoxin-positive and three enterotoxin-negative strains of Clostridium perfringens type A by urea/mercaptoethanol, alkaline mercaptoethanol and alkaline dithiothreitol [13].
• Effect of purine derivatives, papaverine hydrochloride, and imidazole on enterotoxin formation by Clostridium perfringens type A [14].

Biological context of pCPF4969_31

• Enterotoxin was shown to cause a rapid loss of intracellular 86Rb+ (Mr approx. 100) with time- and dose-dependent kinetics [15].
• Clostridium perfringens type A isolates causing food poisoning have a chromosomal enterotoxin gene (cpe), while C. perfringens type A isolates responsible for non-food-borne human gastrointestinal diseases carry a plasmid cpe gene [16].
• The trypsin activation of the enterotoxin involves hydrolysis of Lys15-Glu16 and Lys25-Thr26 bonds [17].
• The enterotoxin gene was on a 6.3 kb transposon which, in addition to the two flanking copies of IS1470, included IS1469 and two 1 kb stretches, one on each side of cpe, with no open reading frames [18].
• Direct plasmid sequencing has identified a translational reading frame within this clone which correlates with the known protein sequence for the type A enterotoxin [19].

Anatomical context of pCPF4969_31

• Enterotoxin released 86Rb and 51Cr from the Vero cells preloaded with the isotope [20].
• Zn2+ and Co2+ also inhibited 51Cr release caused by the enterotoxin previously bound to the cell membrane [20].
• Characterization of a parasporal inclusion body from sporulating, enterotoxin-positive Clostridium perfringens type A [21].
• Enterotoxin production of all isolates was confirmed in vitro in HT-29 cells [22].
• CLINICAL IMPLICATIONS: The presence of C perfringens enterotoxin in feces of dogs, as detected by the latex agglutination assay used in this study, correlates poorly with the number of fecal endospores, regardless of the dog's clinical status [23].

Associations of pCPF4969_31 with chemical compounds

• The osmotic stabilizers, sucrose and poly(ethylene glycol), differentially inhibited enterotoxin-induced larger label loss versus 86Rb+ loss [15].
• The purified enterotoxin often separated, apparently due to slight charge differences, into two protein bands on 7% polyacrylamide gels [24].
• In the case of NCTC 8238, caffeine and theobromine caused a three- to fourfold increase in the percentages of cells possessing refractile spores and a similar increase in enterotoxin concentration [12].
• Spore coat proteins were extracted from 14-strains by alkaline dithiothreitol, and the extracts were assayed for enterotoxin-like spore protein [25].
• Additional dextrin increased the amount of enterotoxin in extracts of sporulating cells of strain NCTC 10239 [26].

Analytical, diagnostic and therapeutic context of pCPF4969_31

• The location of the cpe gene, encoding the enterotoxin responsible for food poisoning in humans, has been studied in a series of enterotoxigenic Clostridium perfringens strains by means of pulsed field gel electrophoresis of genomic DNA [27].
• Molecular cloning of the 3' half of the Clostridium perfringens enterotoxin gene and demonstration that this region encodes receptor-binding activity [28].
• The detailed structural elements revealed by the sequence analysis are presented and used to develop a new perspective on the molecular basis of enterotoxin production in this important food-poisoning bacterium [29].
• Polymerase chain reaction (PCR1) based on the DNA sequence for the whole enterotoxin gene [2] yielded a fragment from an equine isolate of the anticipated size which, cloned into plasmid M13 phage, had a sequence essentially identical to the published sequence [5].
• The major enterotoxin from type C showed a reaction of complete identity with enterotoxin from type A in immunodiffusion using anti-enterotoxin serum prepared against the latter; it induced erythema when injected intradermally into depilated guinea pigs and caused fluid accumulation in the rabbit ileal loop [25].

References