PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Bacillus thuringiensis”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources
PubMed1968

Fatty acids in the genus Bacillus. II. Similarity in the fatty acid compositions of Bacillus thuringiensis, Bacillus anthracis, and Bacillus cereus.

The nature and relative abundance of fatty acids produced by two strains each of Bacillus thuringiensis and of B. anthracis were studied by gas-liquid chromatography on a 12,000 theoretical plate polyester column capable of partially resolving iso- and anteiso-fatty acids with the same number of carbon atoms. Unsaturated fatty acids as the bromo derivatives were separated from the saturated acids and resolved in a short SE-30 column by use of programmed-temperature gas chromatography. All four strains produced 16 major fatty acids: 9 branched (i-C(12), i-C(13), i-C(14), i-C(15), i-C(16), i-C(17), a-C(13), a-C(15), and a-C(17)), 3 normal (n-C(14), n-C(15), and n-C(16)), and 4 monounsaturated (i-C(16) (1=), i-C(17) (1=), a-C(17) (1=), and n-C(16) (1=)), in addition to some minor fatty acids. In all cases, 12 branched acids, including saturated and monounsaturated, made up over 70% of the total fatty acids, and iso-C(15) acid was most abundant. These fatty acid distribution patterns were very similar to those of B. cereus and B. cereus var. mycoides. There were, however, minor but clear differences between the fatty acid distribution patterns of B. thuringiensis and B. anthracis. B. thuringiensis, like B. cereus, produced higher proportions of i-C(13), a-C(13), and i-C(14) fatty acids than did B. anthracis. This difference between these two species could be useful as a supplemental criterion in their differentiation. Indications are that the enzyme systems for monounsaturated fatty acid synthesis in B. thuringiensis and B. anthracis prefer normal fatty acids as substrates rather than branched-chain fatty acids.

Bacillus↗
PubMed1995

Expression and synergistic effect of three types of crystal protein genes in Bacillus thuringiensis.

Bacillus thuringiensis NT0423 newly isolated from sericultural farms in Korea produces quite atypical bipyramidal crystals of a common major band of ca. 130 kDa, and has dual specificity against Lepidoptera and Diptera. To enforce the Diptera toxicity of B. thuringiensis NT0423, cryIVD and cytA genes were transformed into B. thuringiensis NT0423. The transformant B. thuringiensis PT0529 was obtained from introduction of pCG5 into B. thuringiensis NT0423 by electroporation. The expression of crystal proteins in B. thuringiensis PT0529 was characterized by SDS-PAGE and electron microscopy. The results showed that crystalline inclusions of host, CryIVD and CytA were clearly observed in B. thuringiensis PT0529. Furthermore, the toxicity of B. thuringiensis PT0529 against Diptera was highly enforced by synergistic effect.

Animals↗
PubMed2000

Regulation of toxin and virulence gene transcription in Bacillus thuringiensis.

Bacillus thuringiensis is a spore-forming bacterium well known for its insecticidal properties and its ability to produce a crystal inclusion during sporulation. The specific activity of B. thuringiensis against insect larvae is due to the crystal proteins (Cry proteins). Two different transcriptional mechanisms (dependent and independent of sporulation) are responsible for cry gene transcription during the stationary phase. In addition to these specific insecticidal toxins, B. thuringiensis produces potential virulence factors including haemolysins, degradative enzymes and enterotoxins. A pleiotropic regulator (PlcR) that activates the transcription of various genes encoding such extracellular proteins has been identified. Its expression at the onset of the stationary phase is dependent on the growth medium and is controlled by the transition state regulator, SpoOA.

Bacillus thuringiensis↗
PubMed2002

Cloning and expression of cyt2Ba7 gene from a soil-isolated Bacillus thuringiensis.

Bacillus thuringiensis ( Bt) cyt genes coding hemolytic and cytolytic toxins constitute a gene family, which are divided into two groups: cyt1 and cyt2. A novel cyt2 gene was detected from a soil-isolated Bt strain T301, which was highly homologous to cyt2Ba1 and finally designated cyt2Ba7. Until now, Cyt2Ba has not been expressed alone in Bt or other hosts. In this study, the cyt2Ba7 gene was cloned into the vector pQE30 and expressed as a fusion protein with 6xHistidine residues in Escherichia coli. Unlike cyt1A, cyt2Ba7 was freely expressed and formed cytoplasmic inclusions without the need for a "helper" protein. The 6xHis-tagged Cyt2Ba7 was purified in one step by Ni-NTA affinity chromatography, examined cytolytic activity on Sf9 cells, and developed as an antigen to obtain the antiserum against Cyt2Ba by subcutaneous injection into rabbits. This gene was also cloned into the Bt-E. coli shuttle vector pHT3101 and expressed in Bt strain 4Q7. Immunoblotting analysis revealed that the antiserum was remarkably selective and specific to Cyt2Ba.

Bacillus thuringiensis↗
PubMed2001

Effects of the 20-kilodalton helper protein on Cry1Ac production and spore formation in Bacillus thuringiensis.

Bacillus thuringiensis produces large amounts of various pesticidal proteins during the stationary phase. In order to achieve a high yield and form crystals, some pesticidal proteins require the presence of other proteins. Helper protein P20 is required for efficient production of both the Cyt1A and Cry11A crystal proteins in B. thuringiensis subsp. israelensis. Although full-length Cry1 protoxins are usually independent in terms of expression and crystallization in B. thuringiensis, in this study P20 significantly enhanced production of Cry1Ac protoxin (133 kDa) in an acrystalliferous and plasmid-negative strain. In the presence of P20, the yield of Cry1Ac protoxin increased 2.5-fold, and on average the resulting crystals were 1.85 microm long and 0.85 microm wide, three times the size of the crystals formed in the control lacking P20. Correspondingly, the recombinant strain that coexpressed P20 and Cry1Ac exhibited higher toxicity against Heliothis armigera larvae than the control. Furthermore, serious degradation of Cry1Ac in vivo was observed, which has seldom been reported previously. Actually, most protein was completely degraded during synthesis, and after synthesis about one-third of the expressed protoxins were degraded further before crystallization. In this process, P20 protected only nascent Cry1Ac from degradation, indicating that it acted as a molecular chaperon. In addition, spores were smaller and rounder and had a thinner exosporium layer when they were produced in the presence of P20. In summary, Cry1Ac was severely degraded during synthesis; this degradation was effectively relieved by P20, which resulted in enhanced production. Our results indicated that P20 is an effective tool for optimizing protein production in vivo.

Animals↗
PubMed1990

Characterization of the cysteine residues and disulphide linkages in the protein crystal of Bacillus thuringiensis.

Bacillus thuringiensis produces a 130-140 kDa insecticidal protein in the form of a bipyramidal crystal. The protein in the crystals from the subspecies kurstaki HD-1 and entomocidus was found to contain 16-18 cysteine residues per molecule, present primarily in the disulphide form as cystine. Evidence that all the cysteine residues form symmetrical interchain disulphide linkages in the protein crystal was obtained from the following results: (i) the disulphide diagonal procedure [Brown & Hartley (1966) Biochem. J. 101, 214-228] gave only unpaired cysteic acid peptides in diagonal maps; (ii) the disulphide bridges were shown to be labile in dilute alkali and the crystal protein could be released quantitatively with 1 mM-2-mercaptoethanol; (iii) the thiol groups of the released crystal protein were shown by competitive labelling [Kaplan, Stevenson & Hartley (1971) Biochem. J. 124, 289-299] to have the same chemical properties as exposed groups on the surface of the protein; (iv) the thiol groups in the released crystal protein reacted quantitatively with iodoacetate or iodoacetamide. The finding that all the disulphide linkages in the protein crystal are interchain and symmetrical accounts for its alkali-lability and for the high degree of conservation in the primary structure of the cystine-containing regions of the protein from various subspecies.

Amino Acids↗
PubMed2002

Sporulation and delta-endotoxin synthesis by Bacillus thuringiensis.

Bacillus thuringiensis is distinguished from the very closely related Bacillus cereus and Bacillus anthracis by the presence of several plasmid-encoded delta-endotoxin genes. These delta-endotoxins, synthesized as protoxins, are produced in large quantities during sporulation and are packaged into intracellular inclusions. Ingestion of the inclusions by insect larvae leads to protoxin solubilization and conversion to toxins each specific for one of several orders of insects. The toxins form cation-selective channels in the membrane of cells lining the larval midgut with subsequent lethality. In most cases, delta-endotoxin synthesis and sporulation are closely coupled. The latter process in B. thuringiensis is probably virtually identical to that in Bacillus subtilis with the additional use of mother cell sporulation forms of RNA polymerase for the synthesis of the delta-endotoxins. There are other more subtle plasmid-encoded functions or plasmid interactions related to regulating protoxin synthesis. Consideration of both plasmid and chromosomal genes is thus critical for defining this organism.

Bacillus thuringiensis↗
PubMed2002

Requirement of flhA for swarming differentiation, flagellin export, and secretion of virulence-associated proteins in Bacillus thuringiensis.

Bacillus thuringiensis is being used worldwide as a biopesticide, although increasing evidence suggests that it is emerging as an opportunistic human pathogen. While phospholipases, hemolysins, and enterotoxins are claimed to be responsible for B. thuringiensis virulence, there is no direct evidence to indicate that the flagellum-driven motility plays a role in parasite-host interactions. This report describes the characterization of a mini-Tn10 mutant of B. thuringiensis that is defective in flagellum filament assembly and in swimming and swarming motility as well as in the production of hemolysin BL and phosphatidylcholine-preferring phospholipase C. The mutant strain was determined to carry the transposon insertion in flhA, a flagellar class II gene encoding a protein of the flagellar type III export apparatus. Interestingly, the flhA mutant of B. thuringiensis synthesized flagellin but was impaired in flagellin export. Moreover, a protein similar to the anti-sigma factor FlgM that acts in regulating flagellar class III gene transcription was not detectable in B. thuringiensis, thus suggesting that the flagellar gene expression hierarchy of B. thuringiensis differs from that described for Bacillus subtilis. The flhA mutant of B. thuringiensis was also defective in the secretion of hemolysin BL and phosphatidylcholine-preferring phospholipase C, although both of these virulence factors were synthesized by the mutant. Since complementation of the mutant with a plasmid harboring the flhA gene restored swimming and swarming motility as well as secretion of toxins, the overall results indicate that motility and virulence in B. thuringiensis may be coordinately regulated by flhA, which appears to play a crucial role in the export of flagellar as well as nonflagellar proteins.

Bacillus thuringiensis↗
PubMed1987

Evidence that N-methyl-N'-nitro-N-nitrosoguanidine induces adaptive response in Bacillus thuringiensis.

Bacillus thuringiensis is shown to have an inducible error-free repair system for alkylation damage as found in Escherichia coli and Bacillus subtilis. Growth of cells in the presence of low concentrations of N-methyl-N'-nitro-N-nitrosoguanidine (MNNG) induces an adaptive response which is characterized by an increase in resistance to killing and mutagenesis by challenge with higher concentrations of MNNG. In addition, we have noted with interest that adaptive low doses seem to produce lesions at a rate sufficient to induce an increase of mutation frequency, and inhibition of cell division. The possibility of an interaction between SOS and adaptive responses with these low doses of MNNG is discussed.

Adaptation, Physiological↗
PubMed1975

Metalloprotease from Bacillus thuringiensis.

Bacillus thuringiensis var. kurstaki was shown to produce an extracellular, metal chelator-sensitive protease during the early stages of sporulation. Protease production in nutrient broth was dependent upon supplementation with Mn2+ or Ca2. The addition of Ca24 was required for enzyme stabilization...

Bacillus thuringiensis↗
PubMed1989

Thuricin: the bacteriocin produced by Bacillus thuringiensis.

Bacillus thuringiensis serovar, thuringiensis (HD-2) demonstrated antibacterial activity against 48 of 56 strains of B. thuringiensis and against some other Gram-positive species but not against Gram-negative species. The antibacterial activity was not inducible by mitomycin C or by ultraviolet irradiation, and additional activity was not liberated from cells by sonication. Upon dilution of the antibacterial substance, zones of inhibition diminished without the appearance of plaques. Gel filtration chromatography indicated an Mr greater than 950,000 for the bacteriocin (thuricin) in its native form. The native thuricin was sedimented by ultracentrifugation, but electron microscopy of the pellet failed to reveal phage particles or phage components. Nondenaturing polyacrylamide gel electrophoresis (PAGE) of thuricin demonstrated the association of bacteriocin activity with a protein band which migrated only slightly into a 5% gel. Sodium dodecyl sulfate (SDS)-PAGE of partially purified thuricin revealed five major bands. Thuricin activity was substantially reduced by treatment with chymotrypsin, pronase, subtilisin, trypsin, and heat at 96 degrees C but not by treatment with lysozyme, phospholipase C, papain, peptidase, or organic solvents. It exhibited a bactericidal and bacteriolytic effect on a sensitive strain, B. thuringiensis serovar, canadensis (MF4). Partially purified preparations of thuricin had phospholipase A activity which was adsorbed by sensitive cells but not by cells which were insensitive to thuricin. Antibacterial activity was blocked by preincubation of thuricin with phospholipid. Loss of a 150-mDa plasmid was correlated with loss of thuricin production.

Animals↗
PubMed1989

[Intraspecies plasmid transformation of Bacillus thuringiensis].

Bacillus thuringiensis strains 1009, 3004, 3029 of the natural isolates of var. dendrolimus harbouring two large plasmids were transformed by a mix of small plasmids DNA. One of transforming plasmids carried a gene for tetracyclinresistance. The natural isolates of var. dendrolimus strain 2002 and var. berliner strain 1035 were used as donors for plasmid DNA transformation. Three variants of plasmid spectra registered in tetracycliresistant transformants are discussed.

Bacillus thuringiensis↗
PubMedDate not supplied

[Synthetic medium for cultivating Bacillus thuringiensis].

Bacillus thuringiensis subsp. galleriae 69/6 was cultivated in a synthetic medium containing 5 amino acids and nicotinic acid. The dynamics of the culture growth and amino acid assimilation were studied in this medium and in a medium containing yeast extract. The phase of spore germination increased, the yield decreased and the maximal growth rate became higher when the culture grew in the synthetic medium. The percentage of thermoresistant spores was slightly lower in the synthetic medium comparing to the medium with yeast extract.

Amino Acids↗
PubMedDate not supplied

[Effect of proteins on exoprotease synthesis by Bacillus thuringiensis].

Bacillus thuringiensis was shown to grow better in media with albumin, gelatin and casein than in a chemically defined medium; proteins did not induce the synthesis of exoprotease. Two maxima were found in the enzyme synthesis: the first one at the exponential phase of the cultural growth, and the second one during spore formation by the culture. The synthesis at the exponential growth phase was susceptible to nitrogen metabolite repression while the synthesis of exoprotease at the stationary phase of growth was not repressed in the presence of high concentrations of ammonium ions in the medium.

Albumins↗
PubMed2006

Transcriptional response of Choristoneura fumiferana to sublethal exposure of Cry1Ab protoxin from Bacillus thuringiensis.

Bacillus thuringiensis is a microbial control agent active against Choristoneura fumiferana, a lepidopteran defoliator of North American forests. Although the B. thuringiensis insecticidal crystal protoxins have a relatively narrow host range, there is concern about their impact on non-target species where intoxication effects may not be overt. Larval toxicity effects can be assessed at the molecular level by determining altered transcriptional profiles in response to sublethal protoxin exposure in sensitive insects. Subtraction hybridization libraries were created using two larval populations, control and protoxin-fed and were characterized by sequencing 1091 clones. Differential mRNA expression of selected clones, as measured by quantitative polymerase chain reaction, identified a number of metabolic and stress-related genes that were either transcriptionally enhanced or repressed after protoxin exposure.

Animals↗
PubMed2002

Biochemistry and genetics of insect resistance to Bacillus thuringiensis.

Bacillus thuringiensis (Bt) is a valuable source of insecticidal proteins for use in conventional sprayable formulations and in transgenic crops, and it is the most promising alternative to synthetic insecticides. However, evolution of resistance in insect populations is a serious threat to this technology. So far, only one insect species has evolved significant levels of resistance in the field, but laboratory selection experiments have shown the high potential of other species to evolve resistance against Bt. We have reviewed the current knowledge on the biochemical mechanisms and genetics of resistance to Bt products and insecticidal crystal proteins. The understanding of the biochemical and genetic basis of resistance to Bt can help design appropriate management tactics to delay or reduce the evolution of resistance in insect populations.

Animals↗
PubMedDate not supplied

[Effect of different carbon and purine nucleotide sources on exoprotease synthesis by Bacillus thuringiensis].

Bacillus thuringiensis cells, depending on their physiological state, produce different quantities of exoprotease. Easily metabolizable carbon sources in the medium can affect the process in the opposite way: they inhibit synthesis of the enzyme by the cells in the exponential growth phase, and stimulate it by the sporulating cells. Apparently, cAMP is not an effector of catabolite repression regulating exoprotease synthesis by the cells in the exponential growth phase, inspite of stimulating the enzyme synthesis at the background of easily metabolizable carbon sources. The same effect is produced by cAMP in the absence of additional carbon sources. AMP, adenine, GMP and guanine exhibit a similar action on the enzyme synthesis; the effect is most pronounced in the medium without easily metabolizable carbon sources. The action of cGMP is specific: cGMP inhibits the synthesis of exoprotease in the presence of additional carbon sources, and stimulates it in the absence of easily metabolizable compounds.

Bacillus thuringiensis↗