Nucleotide sequence of the gene coding for Clostridium barati type F neurotoxin: Comparison with other clostridial neurotoxins

Thompson, Dewi H.

doi:10.1016/0378-1097(93)90581-l

Cited by 9 publications

(11 citation statements)

References 22 publications

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“…These facts may explain the apparent neutralization of C. baratii toxin F by both C. botulinum antitoxins E and F while confirming the partial sequence uniqueness of the C. baratii toxin F. This structural difference is further supported by studies showing that it requires more type F botulinal antitoxin to neutralize a given amount of C. baratii toxin F than it does to neutralize botulinal toxin F and that C. baratii toxin F is more susceptible to cross-neutralization by type E antitoxin (7). The partial sequence uniqueness of C. baratii toxin F is in contrast to the sequence identities found between the light and heavy chains of C. butyricum toxin E and those of C. botulinum toxin E, 96 and 98.1% homology, respectively (13).…”

Section: Vol 40 2002 Notes 2261mentioning

confidence: 82%

“…Recently, there have been several studies on the genetic and structural relationships among clostridial neurotoxins (5,8,9,13). Sequence analysis has shown that there is high genetic homology between the toxins E produced by C. butyricum and C. botulinum but low relatedness between the genes coding for the toxins F of C. baratii and saccharolytic C. botulinum.…”

Section: Vol 40 2002 Notes 2261mentioning

confidence: 99%

“…Sequence analysis has shown that there is high genetic homology between the toxins E produced by C. butyricum and C. botulinum but low relatedness between the genes coding for the toxins F of C. baratii and saccharolytic C. botulinum. This suggests that some strains of C. baratii possess the capacity to synthesize a unique type of toxin F, whereas C. butyricum acquires its ability to produce toxin E through lateral gene transfer from C. botulinum (8,13).…”

Section: Vol 40 2002 Notes 2261mentioning

confidence: 99%

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Botulism Due to Clostridium baratii Type F Toxin

2002

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Botulism results from consumption of preformed toxin or in vivo toxin elaboration in wounds or intestine. Of U.S. food-borne botulism cases since 1950, the majority were due to toxin A, but a significant number of suspect cases were never confirmed by culture or toxin detection. We report here a possible case of food-borne botulism attributed to toxin F production by a Clostridium baratii organism isolated from food consumed by the patient. The isolation of a toxin-producing Clostridium species other than Clostridium botulinum from food and stool requires deviation from the usual laboratory protocols, which may account for the lack of complete laboratory confirmation of clinically diagnosed cases.

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Section: Vol 40 2002 Notes 2261mentioning

confidence: 82%

Section: Vol 40 2002 Notes 2261mentioning

confidence: 99%

Section: Vol 40 2002 Notes 2261mentioning

confidence: 99%

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Botulism Due to Clostridium baratii Type F Toxin

2002

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“…Botulinum neurotoxins are produced by host bacterial cells in the form of single polypeptide chains, which are about 1500 amino acid residues in length (Mr~150 kDa) (Binz et al, 1990; East et al, 1992; Hauser et al, 1990; Poulet et al, 1992; Thompson et al, 1993). A single molecule of each toxin possesses three functional domains: receptor-recognizing, transport and catalytic.…”

Section: Introductionmentioning

confidence: 99%

Epitope mapping of botulinum neurotoxins light chains

Zdanovsky

Zdanovskaia

2012

Toxicon

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Botulinum neurotoxins (BoNTs) are listed among the most potent biothreat agents. Simultaneously, two out of seven known serotypes of these toxins are used in medicine and cosmetics. This situation calls for development of detailed epitope maps of these toxins. Such maps will help to develop new ways for decreasing damage caused by these toxins if they were to be used as weapons while retaining the therapeutic effect of these toxins used as medicine. Here, we used a library of random fragments of DNA encoding the catalytic domain of botulinum neurotoxin serotype A to identify short epitope-forming sequences. We demonstrated that knowledge of such sequences in a BoNT of one serotype can be used for identification of epitope-forming sequences in other serotypes of BoNTs. We also demonstrated a serodiagnostic value of identified sequences and their ability to retain epitope-specific structures and trigger production of corresponding antibodies, even when they are transferred into a background of a completely alien carrier protein.

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“…Therefore, it has been difficult to construct Clostridium strains that produce derivatives of neurotoxins and other proteins. Genes for all eight clostridial neurotoxins have been cloned, and their sequences have been identified (2,6,9,18,30,31). Many attempts to express fragments of clostridial neurotoxins in Escherichia coli have failed because of the unusually high AT content of clostridial DNA.…”

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confidence: 99%

Simple and Efficient Method for Heterologous Expression of Clostridial Proteins

Zdanovsky

Zdanovskaia

2000

Appl Environ Microbiol

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Many clostridial proteins are poorly produced in Escherichia coli. It has been suggested that this phenomena is due to the fact that several types of codons common in clostridial coding sequences are rarely used in E. coli and the quantities of the corresponding tRNAs in E. coli are not sufficient to ensure efficient translation of the corresponding clostridial sequences. To address this issue, we amplified three E. coli genes, ileX, argU, and leuW, in E. coli; these genes encode tRNAs that are rarely used in E. coli (the tRNAs for the ATA, AGA, and CTA codons, respectively). Our data demonstrate that amplification of ileX dramatically increased the level of production of most of the clostridial proteins tested, while amplification of argU had a moderate effect and amplification of leuW had no effect. Thus, amplification of certain tRNA genes for rare codons in E. coli improves the expression of clostridial genes in E. coli, while amplification of other tRNAs for rare codons might not be needed for improved expression. We also show that amplification of a particular tRNA gene might have different effects on the level of protein production depending on the prevalence and relative positions of the corresponding codons in the coding sequence. Finally, we describe a novel approach for improving expression of recombinant clostridial proteins that are usually expressed at a very low level in E. coli.Clostridial proteins, such as tetanus toxin and seven serologically distinct botulinum neurotoxins (botulinum neurotoxin serotype A [BoNT/A], BoNT/B, BoNT/C, BoNT/D, BoNT/E, BoNT/F, and BoNT/G) that are produced by Clostridium tetani, Clostridium botulinum, Clostridium argentiensis, and Clostridium baratti, are powerful tools for studying the mechanisms of synaptic vesicle exocytosis (3,(20)(21)(22)(23). These toxins have been also used for therapeutic purposes, such as the treatment of strabismus, blepharospasms (24,25), and many other neurological conditions, as well as in clinical dermatology (4).Currently, BoNT/A and other clostridial neurotoxins and their fragments are purified from native Clostridium strains by using traditional purification protocols. Because these microorganisms are anaerobes, they pose technical problems. In addition, gene manipulation methods have not been developed for these microorganisms. Therefore, it has been difficult to construct Clostridium strains that produce derivatives of neurotoxins and other proteins. Genes for all eight clostridial neurotoxins have been cloned, and their sequences have been identified (2,6,9,18,30,31). Many attempts to express fragments of clostridial neurotoxins in Escherichia coli have failed because of the unusually high AT content of clostridial DNA. Makoff et al. successfully expressed a tetanus toxin fragment in E. coli (12) by optimizing sequences for codon usage in E. coli by complete synthesis of these sequences de novo. This approach, however, is very laborious and expensive.Recently, several groups of workers have demonstrated that rarely used codons can...

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Nucleotide sequence of the gene coding for Clostridium barati type F neurotoxin: Comparison with other clostridial neurotoxins

Cited by 9 publications

References 22 publications

Botulism Due to Clostridium baratii Type F Toxin

Botulism Due to Clostridium baratii Type F Toxin

Epitope mapping of botulinum neurotoxins light chains

Simple and Efficient Method for Heterologous Expression of Clostridial Proteins

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