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At least 19 recordsLinked to original sources
PubMed1991

Identification of Clostridium botulinum, Clostridium argentinense, and related organisms by cellular fatty acid analysis.

On the basis of 686 analyses of 285 strains of Clostridium botulinum, Clostridium argentinense (formerly C. botulinum type G), and phenotypically related organisms, 14 cellular fatty acid (CFA) groups of toxic organisms and 6 CFA groups of nontoxic organisms were delineated. The CFA groups of toxic strains included two of type A, three of proteolytic strains of type B, two of proteolytic strains of type F, one each of nonproteolytic strains of types B, E, and F, and one each of types C alpha, C beta, and D and C. argentinense. The groups of phenotypically similar nontoxic strains included Clostridium sporogenes, Clostridium putrificum, nontoxic strains with phenotypic characteristics similar to those of nonproteolytic strains of C. botulinum types B, E, and F (BEF-like), two groups of nontoxigenic organisms with phenotypic characteristics similar to those of C. botulinum types C and D and Clostridium novyi (CDN-like), and Clostridium subterminale, which has phenotypic characteristics similar to those of C. argentinense. Within the toxin types, 89 to 100% of the strains were correctly identified by CFA analysis, and 74 to 100% of the analyses were correct. Of 36 strains of C. sporogenes, 30 (83%) were correctly identified; 17% of the strains of C. sporogenes were incorrectly identified as C. botulinum type A or B. All analyses of C. putrificum and C. subterminale were correctly identified. There was no significant level of similarity between strains of C. botulinum and phenotypically similar organisms and 85 other species of clostridia or 407 other taxa of gram-positive and gram-negative bacteria. Additionally, the one strain each of Clostridium baratii and Clostridium butyricum previously reported to produce C. botulinum toxin could be differentiated from C.botulinum types as well as from strains of C. baratii and C. butyricum that did not produce neurotoxin.

Bacterial Toxins↗
PubMed1993

Nucleotide sequence of the gene coding for Clostridium botulinum (Clostridium argentinense) type G neurotoxin: genealogical comparison with other clostridial neurotoxins.

The neurotoxin gene from Clostridium botulinum type G was cloned as a series of overlapping DNA fragments generated using polymerase chain reaction (PCR) technology and primers designed to conserved regions of published botulinal toxin (BoNT) sequences. The 5'-end of the gene was obtained using a primer based on a conserved region of the nontoxic-nonhaemagglutinin gene lying upstream of the toxin gene. Translation of the nucleotide sequence derived from the cloned PCR fragments demonstrated that the gene encodes a protein of 1297 amino acid residues (rmm 149, 147). Comparative alignment of the determined BoNT/G sequence with those of other clostridial neurotoxins revealed highest sequence relatedness (approx. 58% amino acid identity) with BoNT/B of proteolytic and non-proteolytic C. botulinum. Tetanus toxin (TeTx) and other BoNT types revealed lower levels of relatedness with BoNT/G (approximate range 35-42% amino acid identity).

Amino Acid Sequence↗
PubMed1997

Molecular characterization of the clusters of genes encoding the botulinum neurotoxin complex in clostridium botulinum (Clostridium argentinense) type G and nonproteolytic Clostridium botulinum type B.

The cluster of genes encoding components of the progenitor botulinum neurotoxin complex has been mapped and cloned in Clostridium botulinum type G strain ATCC 27322. Determination of the nucleotide sequence of the region has revealed open reading frames encoding nontoxic components of the complex, upstream of the gene encoding BoNT/G (botG). The arrangement of these genes differs from that in strains of other antigenic toxin types. Immediately upstream of botG lies a gene encoding a protein of 1198 amino acids, which shows homology with the nontoxic-nonhemagglutinin (NTNH) component of the progenitor complex. Further upstream there are genes encoding proteins with homology to hemagglutinin components (HA-17, HA-70) and a putative positive regulator of gene expression (P-21). Sequence comparison has shown that BoNT/G has highest homology with BoNT/B. The sequence of the BoNT-cluster of genes in non-proteolytic C. botulinum type B strain Eklund 17B has been extended to include the complete NTNH and HA-17, and partial HA-70 gene sequences. Comparison of NTNH/G with other NTNHs reveals that it shows highest homology with NTNH/B consistent with the genealogical affinity shown between BoNT/G and BoNT/B genes.

Amino Acid Sequence↗
PubMed1988

Partial characterization of the enzymatic activity associated with the binary toxin (type C2) produced by Clostridium botulinum.

Clostridium botulinum produces a binary toxin that possesses a heavy chain (approximately 100,000 daltons) and a light chain (approximately 50,000 daltons). The heavy chain is a binding component that directs the toxin to vulnerable cells, and the light chain is an enzyme that has mono(ADP-ribosyl)ating activity. A number of experiments have been done to help characterize the enzymatic activity of the toxin. The data reveal that the enzyme has a pH optimum within the range of 7.0 to 8.0. It is not inhibited or stimulated by physiological concentrations of sodium, potassium, calcium, or magnesium. The enzyme is inhibited by high concentrations of salt, however, as well as high concentrations of nicotinamide, thymidine, theophylline, and histamine; and it is stimulated by histone and lysolecithin. Boiling irreversibly denatures the light chain of the toxin, but denaturation caused by guanidine and urea is substantially reversible. Enzymatic activity is not altered by short exposure to lysosomal proteases, including cathepsin B, cathepsin H, dipeptidyl aminopeptidase, and catheptic carboxypeptidase B.

ADP Ribose Transferases↗
PubMed1999

Molecular properties of a hemagglutinin purified from type A Clostridium botulinum.

Clostridium botulinum causes the food poisoning disease botulism by producing botulinum neurotoxin, the most potent toxin known. The neurotoxin is produced along with a group of neurotoxin-associated proteins, or NAPs, which protect it from the low pH and proteases of the gastrointestinal tract. Recently, we isolated one of the major components of NAPs, a 33-kDa hemagglutinin (Hn-33) [Fu et al. (1998), J. Protein Chem. 17, 53-60]. In this study, we present molecular properties of Hn-33 derived from several biochemical and biophysical techniques. Hn-33 in pure form requires a 66-fold lower concentration of sugar inhibition of its hemagglutination activity than in its complexed form with the neurotoxin and other NAPs. However, its protease resistance is not affected by sugar binding. Based on FT-IR and circular dichroism (CD) analysis, Hn-33 is a predominantly beta-sheet protein (74-77%). Hn-33 analysis by laser desorption mass spectrometry and size exclusion column chromatography reveals that it exists predominantly in a dimeric form in the aqueous solution. Even a very low concentration of SDS (0.05%) irreversibly destroyed the biological activity of Hn-33 by changing its secondary structure as revealed by far-UV CD analysis.

Bacterial Proteins↗
PubMed2007

Genomic analysis of the phosphotransferase system in Clostridium botulinum.

Clostridium botulinum is capable of fermenting carbohydrates, but there have been no detailed studies of the uptake of sugars and related substrates. In bacteria, a common and often predominant system of carbohydrate uptake is the phosphoenolpyruvate (PEP)-dependent phosphotransferase system (PTS). This multi-protein complex catalyses a group translocation involving both uptake and phosphorylation of carbohydrates, and is also known to play an important role in environmental sensing and metabolic regulation. The genome of C. botulinum encodes 15 PTSs which have a similar domain structure to the PTS in other bacteria. Based on phylogenetic relationships and analysis of gene clusters, the C. botulinum PTS appears to be involved in the uptake of hexoses, hexose derivatives and disaccharides. C. botulinum also contains the components of PTS-associated regulatory mechanisms which have been characterised in other bacteria. It therefore seems likely that the PTS plays a significant, and previously unrecognised, role in the physiology of this bacterium.

Biological Transport↗
PubMed1967

Arginine and ornithine catabolism by Clostridium botulinum.

Clostridium botulinum 62-A was shown to catabolize l-arginine via citrulline to ornithine, NH(3), and CO(2). The individual enzymes of the dihydrolase system were all demonstrated in extracts of cells, spores, and germinated spores. There was no liberation of urea from l-arginine, so no functional arginase enzyme is present, but there was some transamidinase activity in cell extracts. l-Ornithine was degraded at a significant rate by cells grown in an l-ornithine-supplemented medium; it was partially decarboxylated to putrescine and partially fermented to NH(3), CO(2), volatile acids, and delta-aminovaleric acid. Results from the fermentation of l-ornithine-C(14), -1-C(14), and -2-C(14) demonstrated that essentially all of the CO(2) was derived from carbon 1, and volatile acids from carbons 2 to 5. Assays for the products of l-ornithine-C(14) fermentation revealed that the volatile acids consisted of acetate, propionate, valerate, and butyrate (in order of decreasing concentrations), and that delta-amino-valerate was the primary reduced product. A small amount of citrulline was formed during the fermentation. The carbon and redox balances indicated that l-ornithine is fermented as a single substrate. Preliminary experiments demonstrated that the fermentation of l-ornithine is carried out by cell extracts with the production of volatile acids.

Arginase↗
PubMed1992

[Distribution of Clostridium botulinum and Clostridium tetani in Okinawa Prefecture].

Soil samples from the sugar cane fields and muscovado samples from the manufacturing processes at sugar manufacturies in many parts of Okinawa Prefecture were collected, mainly in 1988 and 1989, and examined for Clostridium botulinum and Clostridium tetani. Of 290 soil samples 21 (7.2%) were positive for C. botulinum. Four (1.4%) and 17 (5.9%) contained types E and C respectively. C. botulinum type E was demonstrated in the North and South areas of Okinawa main island. Type A and B were not demonstrated from soil samples in Okinawa Prefecture. Of 53 samples of the manufacturing processes of muscovado 5 (9.4%) were positive for C. botulinum type C. Type A, B and E were not found from muscovado samples in Okinawa Prefecture. Of 290 soil samples 54 (18.6%) were positive for C. tetani. Among the 53 muscovado samples from the manufacturing processes of the sugar cane, 10 (18.9%) were positive for C. tetani.

Botulinum Toxins↗
PubMed2004

Organization and regulation of the neurotoxin genes in Clostridium botulinum and Clostridium tetani.

Botulinum and tetanus neurotoxins are structurally and functionally related 150 kDa proteins that are potent inhibitors of neuroexocytosis. Botulinum neurotoxin associates with non-toxic proteins to form complexes of various sizes. The botulinum neurotoxin and non-toxic protein genes are clustered in a DNA segment called the botulinum locus. This locus is probably located on a mobile or degenerate mobile element, which accounts for the various genomic localizations (chromosome, plasmid, phage) in different Clostridium botulinum types. The botulinum neurotoxin and non-toxic protein genes are organized in two polycistronic operons (ntnh-bont and ha operons) transcribed in opposite orientations. The gene that separates the two operons of the botulinum locus in C. botulinum A encodes a 21 kDa protein BotR/A, which is a positive regulator of the expression of the botulinum locus genes. Similarly, in Clostridium tetani, the gene located immediately upstream of the tetanus toxin gene, encodes a positive regulatory protein, TetR. BotR and TetR are possibly alternative sigma factors related to TxeR and UviA, which regulate C. difficile toxin and C. perfringens bacteriocin production, respectively. TxeR and UviA define a new sub-group of the sigma(70) family of RNA polymerase initiation factors. In addition, the C. botulinum genome contains predicted two-component system genes, some of which are possibly involved in regulation of toxinogenesis.

Journal Article↗
PubMed1975

Common mesophilic anaerobes, including Clostridium botulinum and Clostridium tetani, in 21 soil specimens.

A relatively rich medium was markedly superior to a dilute medium for the isolation of anaerobic bacteria from soil. The obligate anaerobes isolated from 21 soil samples were all clostridia and the counts ranged from 2.7 X 10-2 to 3.3 X 10-6 per g. The organisms most frequently isolated were Clostridium subterminate, C. sordelii, C. sporogenes, C. indolis, C. bifermentans, C. mangenoti, and C. perfringens. Seventeen other species were also recognized but almost one-third of the isolates could not be identified with any known species of Clostridium. C. botulinum type A was demonstrated in six soil samples, and type B in one. These soils were neutral to alkaline in reaction (average pH 7.9) and low in organic matter content (1.4%). The association of C. botulinum types A and B with neutral to alkaline soils was statistically significant (P = 0.001) as was their association with soils low in organic matter (P = 0.005). C. botulinum types E and F were found in one soil sample, pH 4.5, with organic matter 13.7%. C. tetani was isolated from two soil samples, both of intermediate pH value and higher than average organic matter content.

Anaerobiosis↗