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Biomedical subjects

J Melling

Publications and source records attributed to J Melling.

70 records · Page 4Linked to original sources
PubMed1979

Properties and production characteristics of vomiting, diarrheal, and necrotizing toxins of Bacillus cereus.

Evidence is provided that the enterotoxin of Bacillus cereus variously described in the literature as diarrheagenic toxin, diarrheal agent, fluid accumulation factor, vascular permeability factor, dermonecrotic toxin, and intestinonecrotic toxin is a single relatively unstable protein of molecular weight approximately 50,000 and isoelectric point of the order of 4.9. It is presumed to be the enterotoxin responsible for the diarrheal-type B. cereus food poisoning syndrome and it may also be the pyogenic and pyrogenic factor in nongastrointestinal B. cereus infections of man and animals. The enterotoxin is a vegetative growth metabolite produced to one degree or another by almost all B. cereus strains and is readily separated from phospholipase and heat-labile cereolysin but less readily differentiated from a heat-stable hemolysin. It is lethal to mice but may also be separable from another mouse lethal factor by electrofocusing. The emetic toxin responsible for the vomiting-type B. cereus food poisoning syndrome is clearly distinguishable from the diarrheal and other toxic factors and appears to be a highly stable compound of molecular size less than 5000.

Animals↗
PubMed1979

Assay of the heat-labile enterotoxin of Escherichia coli in infant rabbits.

Infant rabbits were shown to respond to Escherichia coli heat-labile enterotoxin by a consistent increase in intestinal fluid content, which was maximal 5 h after oral dosing. Infant rabbits could be used in a simple quantitative assay for heat-labile E. coli enterotoxin based on the ratios of gut weight to remaining body weight 5 h after oral dosing. Infant rabbits remained responsive to heat-labile enterotoxin up to 14 days of age, after which their gastric pH became low enough to destroy the enterotoxin. Rabbits that had been deprived of food before being dosed had a reduced gastric pH and a reduced response to the enterotoxin. Lincomycin andmitomycin C were found not to increase th e yield of heat-labile enterotoxin from E. coli strain P307.

Animals↗
PubMed1979

Export of extracellular levansucrase by Bacillus subtilis: inhibition by cerulenin and quinacrine.

Bacillus subtilis B secretes an inducible, extracellular enzyme, levansucrase. Inhibition studies were undertaken to investigate the possible mechanism of release of this enzyme. The antibiotic cerulenin, at a concentration of 10 micrograms/ml, totally inhibited de novo lipid synthesis in B. subtilis B for at least 1 h, while only slightly reducing protein and RNA synthesis. At this concentration cerulenin, added concomitantly with the inducer sucrose, prevented the release of levansucrase for at least 150 min. This was not due to the prevention of inducer uptake by the cells. The release of the enzyme was also independent of cell division. In B. subtilis 1007 the induction of beta-galactosidase by 5 mM lactose was not prevented by cerulenin. Preliminary evidence indicated the association of a lipid moiety with the enzyme as it passes through the cytoplasmic membrane. Quinacrine (0.2 mM), which inhibits the penicillinase-releasing protease of Bacillus licheniformis, inhibited levansucrase release from B. subtilis B, but had no effect on lipid synthesis.

Antifungal Agents↗
PubMed1976

Identification of a novel enterotoxigenic activity associated with Bacillus cereus.

A strain of Bacillus cereus isolated from a food poisoning outbreak characterized by vomiting has been shown to be capable of causing vomiting when cultures grown on rice, but not other media, were fed to Rhesus monkeys. In contrast, a strain isolated from a diarrhoeal outbreak produced diarrhoea, but not vomiting, when grown on various media in similar feeding trials. Furthermore, culture filtrates from the diarrhoeal strain caused fluid accumulation in ligated rabbit ileal loops whereas those from the vomiting strain did not. It is proposed that at least two enterotoxins are involved, one responsible for the vomiting and one for the diarrhoeal symptoms.

Animals↗
PubMed1972

Preparation of gram quantities of a purified R-factor-mediated penicillinase from Escherichia coli strain W3310.

Purified penicillinase, in gram quantities, has been prepared from Escherichia coli strain W3310 by using methods developed to handle large amounts of material. The final product had a specific enzyme activity of 3.08 units/mug of protein, which was over twice as high as that reported previously (Datta & Richmond, 1966). The purified enzyme was similar to that from E. coli strain TEM, but different in molecular weight and some other respects. The differences observed may be a result of the greater purity obtained.

Amino Acids↗
PubMedDate not supplied

Decontamination of Bacillus anthracis on Gruinard Island?

In experiments on Gruinard Island 40 years ago small bombs containing spores of Bacillus anthracis were suspended from a gantry and detonated, producing widespread contamination of the island's surface. Recently, analysis of soil samples has shown that the area where the spores can now be detected is small enough to be considered for decontamination. We investigated the effect of treating the soil with sporicidal chemicals, namely, potassium permanganate, formaldehyde, glutaraldehyde, Cidex ('activated' glutaraldehyde, Surgikos), dodecylamine and peracetic acid.

Bacillus anthracis↗
PubMedDate not supplied

Acceptors for botulinum neurotoxin reside on motor nerve terminals and mediate its internalization.

Botulinum neurotoxin (BoNY) type A, a causative agent of botulism, is a di-chain protein (molecular weight 140,000) from Clostridium botulinum, and the most neurotoxic substance known. Some cases of sudden infant cot deaths have been attributed to such a neuroparalytic condition. BoNT inhibits irreversibly the release of acetylcholine from peripheral nerves in a highly selective manner. Hence, it is potentially an invaluable probe for studying the mechanism of transmitter release. Here we demonstrate specific labelling of murine motor nerve terminals with neurotoxic, 125I-labelled BoNT (type A) by autoradiography. We observed saturable, temperature-sensitive binding of BoNT to sites which reside solely on the nerve terminal membrane; these were distributed on all unmyelinated areas, at an average density of 150-500 per micron2 of membrane. The binding was mediated by the larger subunit of the toxin and was inhibited partially by tetanus toxin, another microbial protein. No specific binding was detectable on any other cell types examined, including noradrenergic terminals. Following binding, internalization of radioactivity was observed; this process was energy-dependent as it could be prevented totally by azide or dinitrophenol (DNP). This direct demonstration of separable steps, including highly selective binding and acceptor-mediated internalization, is reconcilable with the unique potency and the multiphasic inhibitory action of BoNT on transmitter release, as shown electrophysiologically.

Animals↗