Distribution, Frequency, and Diversity of
            <i>Bacillus thuringiensis</i>
            in an Animal Feed Mill

Meadows, M P; Ellis, D. J.; Butt, J.; Jarrett, P.; Burges, H. D.

doi:10.1128/aem.58.4.1344-1350.1992

Cited by 156 publications

(68 citation statements)

References 29 publications

(18 reference statements)

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“…It has been also reported, however, that noninsecticidal B. thuringiensis is ubiquitous in natural environments (Ohba and Aizawa 1986;Hastowo et al 1992;Meadows et al 1992;Ohba 1996;Mizuki et al 1999b;Ichimatsu et al 2000). The observations suggest that B. thuringiensis as a species is not characterized by insecticidal activity of parasporal inclusions.…”

Section: Introductionmentioning

confidence: 88%

In vitro cytotoxicity of non-Cyt inclusion proteins of a Bacillus thuringiensis isolate against human cells, including cancer cells

et al. 2000

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A soil isolate designated 90‐F‐45‐14, belonging to Bacillus thuringiensis serovar dakota (H15), was examined for characterization of in vitro cytotoxicity, associated with parasporal inclusion proteins, against human cells. When activated with proteolytic processing, inclusion proteins of the isolate 90‐F‐45‐14 exhibited a moderate cytotoxicity against the human uterus cervix cancer cells (HeLa) with an EC50 value of 60·8 µg ml−1, while showing extremely high activities on the human leukaemic T cells (MOLT‐4) and the normal T cells with EC50 values of 0·27 and 0·20 µg ml−1, respectively. Anti‐leukaemic cell activity of the 90‐F‐45‐14 proteins was eight to nine times greater than that of the B. thuringiensis serovar israelensis proteins containing the Cyt1 protein, a broad‐spectrum cytolysin. The cytopathy by the 90‐F‐45‐14 proteins was characterized by marked cell‐ballooning, while the israelensis proteins induced early breakdown of the cells due to cytolysis. Inclusions of the isolate consisted of five major polypeptides of 170, 103, 73, 40 and 32 kDa. A 100% homology was observed in the sequence of 15 N‐terminal amino acids between the proteins of 170 and 103 kDa. There was no N‐terminal sequence homology between 90‐F‐45‐14 proteins and the existing Cry/Cyt proteins of B. thuringiensis. Proteolytic processing by proteinase K yielded several proteins with molecular masses ranging from 40 to 28 kDa.

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Section: Introductionmentioning

confidence: 88%

In vitro cytotoxicity of non-Cyt inclusion proteins of a Bacillus thuringiensis isolate against human cells, including cancer cells

et al. 2000

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“…Soil adjacent to an intensive livestock unit in Warwickshire, UK was subjected to the enrichment method of Johnson and Bishop [12]. For comparison strains were also selected after heat shock (60³C for 30 min) on the basis of their ability to produce insecticidal crystal proteins (ICPs) visible under light microscopy, adapted from Meadows et al [13].…”

Section: Isolation Of B Thuringiensismentioning

confidence: 99%

Prevalence of β-exotoxin, diarrhoeal toxin and specific δ-endotoxin in natural isolates of Bacillus thuringiensis

Perani¹

1998

FEMS Microbiology Letters

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Of newly isolated colonies with the appearance of Bacillus thuringiensis, 47.5% were found to produce the parasporal crystals characteristic of this species. These positive isolates were screened using the polymerase chain reaction for their possession of a gene encoding a specific protoxin type, CryIB. Strains with and without this gene were screened for their ability to produce Lexotoxin and Bacillus cereus-type enterotoxin. It was found that 35% of the isolates possessed the cryIB gene; of these 83% also produced enterotoxin and 58% produced L-exotoxin. No statistical significance was found for linkage between any of these characteristics. The probability, therefore, of isolating a strain of B. thuringiensis which specifically possessed the cryIB gene but did not produce either of the other, undesired, toxins, from the soil sample used, was 1.2%. z 1998 Federation of European Microbiological Societies. Published by Elsevier Science B.V.

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“…For several decades, a number of insecticidal B. thuringiensis isolates have been recovered from various regions of the world. On the other hand, many studies have reported that noninsecticidal B. thuringiensis strains are more widely distributed than insecticidal ones (Hastowo et al 1992;Meadows et al 1992;Ohba 1996;Mizuki et al 1999b). Therefore, a screening method by optical biosensor was attempted to detect insecticidal strains against certain insects and pests (Okumura et al 2001).…”

Section: Introductionmentioning

confidence: 99%

Bacillus thuringiensis serovar shandongiensis strain 89-T-34-22 produces multiple cytotoxic proteins with similar molecular masses against human cancer cells

Okumura

Akao

Higuchi

et al. 2004

Lett Appl Microbiol

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Aims: To prove that Bacillus thuringiensis serovar shandongiensis strain 89-T-34-22 produces several novel cytotoxic proteins against human leukaemic T cells. Methods and Results: Parasporal inclusion protein was solubilized and processed by proteinase K and was separated by anion-exchange chromatography. Cytopathic effects of each fraction against MOLT-4 and Jurkat cells were monitored. Conclusions: Existence of at least two novel cytotoxic proteins was suggested and N-terminal sequences of the newly identified proteins were determined to be QSTTDVIREY and X (Y or I) (P or I) NLANELA (X indicates uncertain amino acids). Molecular masses of the two proteins were approx. 27-28 kDa. Significance and Impact of the Study: In this study, we demonstrated that the strain 89-T-34-22 produces at least two novel cytotoxic proteins with similar molecular masses against human cancer cells. This is the first strain of B. thuringiensis which produces multiple cytotoxic proteins against human cancer cells.

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Distribution, Frequency, and Diversity of Bacillus thuringiensis in an Animal Feed Mill

Cited by 156 publications

References 29 publications

In vitro cytotoxicity of non-Cyt inclusion proteins of a Bacillus thuringiensis isolate against human cells, including cancer cells

In vitro cytotoxicity of non-Cyt inclusion proteins of a Bacillus thuringiensis isolate against human cells, including cancer cells

Prevalence of β-exotoxin, diarrhoeal toxin and specific δ-endotoxin in natural isolates of Bacillus thuringiensis

Bacillus thuringiensis serovar shandongiensis strain 89-T-34-22 produces multiple cytotoxic proteins with similar molecular masses against human cancer cells

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