Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Bacillus thuringiensis”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

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

At least 397 records · Page 22Linked to original sources
PubMed1988

[Extracellular ribonuclease from Bacillus thuringiensis].

The ability of the strain Bacillus thuringiensis var. subtoxicus to produce extracellular ribonuclease (ribonuclease Bt) was studied. It was found that the culture medium possesses a RNA-depolymerizing activity whose maximum is observed 4-5 hours after the beginning of the linear growth phase. A three-step chromatography of the culture extract on phosphocellulose resulted in a homogeneous enzyme with a molecular mass of 12000 Da. The enzyme showed the maximum activity towards RNA at pH 8.5, catalyzed the hydrolysis of polyribonucleotides and guanosine-2',3'-cyclophosphate. Hence, the enzyme can be related to base-nonspecific cyclizing ribonucleases showing the guanylic specificity towards nucleoside-2',3'-cyclophosphates.

Bacillus thuringiensis↗
PubMed2003

Novel fermentation media for production of Bacillus thuringiensis subsp. israelensis.

The production of Bacillus thuringiensis subsp. israelensis (deBarjac) (Bti) as a biopesticide is not cost-effective using existing fermentation technology. In this study, we explored the use of several less expensive alternative culture media (potato, common sugar, and Bengal gram) for the growth and production of Bti. Growth was obtained in all tested media and was comparable to that obtained in conventional medium (Luria-Bertani). Toxicity assays showed that the toxin produced from the novel growth media were effective in killing larvae of Culex quinquefasciatus, Anopheles stephensi, and Aedes aegypti and toxicity was comparable to that produced from Luria-Bertani medium. These observations suggest that potato can be used as a cheap source of culture medium for the production of Bti toxin in mosquito control programs.

Aedes↗
PubMed1998

Similarity in moth-fly specific larvicidal activity between two serologically unrelated Bacillus thuringiensis strains.

Parasporal inclusions of a Bacillus thuringiensis isolate designated 92-KU-105-9 (H14/19) exhibited unusual larvicidal activity, specific for the moth-fly, Telmatoscopus albipunctatus (Diptera: Psychodidae), similar to that of a previously reported B. thuringiensis serovar leesis (H33) strain. The LC50 value of the purified inclusions was 4.92 micrograms ml-1 for the moth-fly larvae, while no mortality was shown in the mosquitoes Culex pipiens molestus and Anopheles stephensi, at protein concentrations up to 10 mg ml-1. Morphologically, the inclusion was a homogeneous globular body surrounded by an electron-dense, thick envelope. Multilamellar inner structure was evident between envelope membrane and inclusion matrix. SDS-PAGE revealed that the inclusions consist of five proteins with molecular masses of 72, 70, 68, 56 and 30 kDa. These proteins cross-reacted with the antibodies against inclusion proteins of the serovar leesis strain. High homologies existed in N-terminal amino acid sequences between the three major proteins (72, 70 and 68 kDa) and the two established protein classes, Cry4A and Cry10A.

Amino Acid Sequence↗
PubMed2003

Bacillus thuringiensis crystal proteins that target nematodes.

Bacillus thuringiensis (Bt) crystal proteins are pore-forming toxins used as insecticides around the world. Previously, the extent to which these proteins might also target the invertebrate phylum Nematoda has been mostly ignored. We have expressed seven different crystal toxin proteins from two largely unstudied Bt crystal protein subfamilies. By assaying their toxicity on diverse free-living nematode species, we demonstrate that four of these crystal proteins are active against multiple nematode species and that each nematode species tested is susceptible to at least one toxin. We also demonstrate that a rat intestinal nematode is susceptible to some of the nematicidal crystal proteins, indicating these may hold promise in controlling vertebrate-parasitic nematodes. Toxicity in nematodes correlates with damage to the intestine, consistent with the mechanism of crystal toxin action in insects. Structure-function analyses indicate that one novel nematicidal crystal protein can be engineered to a small 43-kDa active core. These data demonstrate that at least two Bt crystal protein subfamilies contain nematicidal toxins.

Animals↗
PubMed1985

Protease activation of the entomocidal protoxin of Bacillus thuringiensis subsp. kurstaki.

Two isolates of Bacillus thuringiensis subsp. kurstaki were examined which produced different levels of intracellular proteases. Although the crystals from both strains had comparable toxicity, one of the strains, LB1, had a strong polypeptide band at 68,000 molecular weight in the protein from the crystal; in the other, HD251, no such band was evident. When the intracellular proteases in both strains were measured, strain HD251 produced less than 10% of the proteolytic activity found in LB1. These proteases were primarily neutral metalloproteases, although low levels of other proteases were detected. In LB1, the synthesis of protease increased as the cells began to sporulate; however, in HD251, protease activity appeared much later in the sporulation cycle. The protease activity in strain LB1 was very high when the cells were making crystal toxin, whereas in HD251 reduced proteolytic activity was present during crystal toxin synthesis. The insecticidal toxin (molecular weight, 68,000) from both strains could be prepared by cleaving the protoxin (molecular weight, 135,000) with trypsin, followed by ion-exchange chromatography. The procedure described gave quantitative recovery of toxic activity, and approximately half of the total protein was recovered. Calculations show that these results correspond to stoichiometric conversion of protoxin to insecticidal toxin. The toxicities of whole crystals, soluble crystal protein, and purified toxin from both strains were comparable.

Bacillus thuringiensis↗
PubMed2006

Differences in susceptibility and physiological fitness of Mexican field Trichoplusia ni strains exposed to Bacillus thuringiensis.

The use of different commercial Bacillus thuringiensis (Bt) products in the Bajio guanajuatense area in Mexico began 12 yr ago, and resistance to Bt in this area has been reported for Plutella xylostella (L.) The current study provides a baseline response and resistance potential to Bt in field and laboratory strains of Bajio Trichoplusia ni (Hübner). Differences in susceptibility to Bt among T. ni populations were observed. T. ni neonates collected in Romita, Guanajuato, were more susceptible to Bt than those collected in Salvatierra or San Luis de la Paz, Guanajuato. After five generations of exposure to XenTari in the laboratory, decreased susceptibility was found only in the Salvatierra insects, with an LC50 that was 2.1-fold greater than that of a Mexican laboratory strain. The XenTari-selected San Luis de la Paz strain was from 16- to 87-fold more resistant to CrylA protoxins than U.S. (US) and Mexican laboratory strains. Although CrylAb is not a component of XenTari, this strain also was significantly less susceptible to CrylAb toxin compared with a US strain, with a resistance ratio of 40.4. The larval weights and lengths, pupal lengths, and percentage of pupation were significantly lower for the Salvatierra strain than for all other strains. The relationship of T. ni susceptibilities to Bt Cry toxins and protoxins after several generations of exposure to XenTari and its similarity to P. xylostella behavior.

Animals↗
PubMed1993

Structural characterization, membrane interaction, and specific assembly within phospholipid membranes of hydrophobic segments from Bacillus thuringiensis var. israelensis cytolytic toxin.

The Bacillus thuringiensis var. israelensis (Bti) cytolytic toxin is hypothesized to exert its toxic activity via pore formation in the cell membrane as a result of the aggregation of several monomers. To gain insight into the toxin's mode of action, 2 putative hydrophobic 22 amino acid peptides were synthesized and characterized spectroscopically and functionally. One peptide corresponded to the putative amphiphilic alpha-helical region (amino acids 110-131, termed helix-2), and the other to amino acids 50-71 (termed helix-1) [Ward, E. S., Ellar, D. J., & Chilcott, C. N. (1988) J. Mol. Biol. 202, 527-535] of the toxin. Circular dichroism spectroscopy revealed that both segments adopt high alpha-helical content in a hydrophobic environment, in agreement with previous models. To monitor peptide-lipid and peptide-peptide interactions, the peptides were labeled selectively with either 7-nitro-2,1,3-benzoxadiazol-4-yl (NBD) (to serve as donor) or tetramethylrhodamine (to serve as an acceptor), at their N-terminal amino acids. Both segments bind strongly to small unilamellar vesicles, composed of zwitterionic phospholipids, with surface partition coefficients on the order of 10(4) M-1. The shape of the binding isotherms indicates that helix-2 forms large aggregates within phospholipid membranes. Resonance energy transfer experiments demonstrated that the segments self-associate and interact with each other, but do not associate with unrelated membrane-bound peptides. Functional characterization demonstrated that helix-2 permeates phospholipid SUV with a potency similar to that of naturally occurring pore-forming peptides. Thus, the results support a role for helices-1 and -2 in the assembly and in the pore formation by Bti toxin.

Amino Acid Sequence↗
PubMed1984

[Intervariant transduction in Bacillus thuringiensis].

This report deals with intervariant transduction in strains of Bacillus thuringiensis subsp, dendrolimus and galleriae with bacteriophage Tg13. This bacteriophage has a broad host range and is of a large DNA molecular mass (40.3 mD). Transducing properties of this bacteriophage were studied in Bacillus thuringiensis var. galleriae using auxotrophic mutants requiring purine and pyrimidine bases or tryptophan as recipients. The frequency of transduction was 10(-5)-10(-6). In order to prove the possibility of intervariant transduction, two series of experiments have been conducted. In the first case, bacteriophage tg13 has been propagated on the prototrophic strain 49-18 (var. dendrolimus), 48gua (var. galleriae) being used as a recipient. In the second case, the prototrophic strain 69-6 (var. galleriae) served as a donor and 49-18-1 trp (var. dendrolimus) - as a recipient. The frequency of heterologous transduction was 10(-7). The positive result obtained in cross-transduction experiments may be explained by common metabolic pathways of purine and pyrimidine bases and amino acids in strains of different serotypes.

Bacillus thuringiensis↗
PubMed2000

Hyper-production of insecticidal crystal protein (delta-endotoxin) by Bacillus thuringiensis var. israelensis is not related to sporulation-specific biochemical functions.

Hypertoxic mutant strains of Bacillus thuringiensis var. israelensis were isolated by mutagenesis of the parent strain. The correlation, if any, between hyper-production of insecticidal crystal protein (delta-endotoxin) by hypertoxic mutant strains of Bacillus thuringiensis var. israelensis and sporulation-specific biochemical functions was studied. No increase in sporulation-specific biochemical markers was observed in the hypertoxic mutant strains. Asporogenous mutants of hypertoxic mutant strains blocked at different stages of sporulation were isolated, and larvicidal activity was studied. The hypertoxic parent strains and the sporulation-deficient, hypertoxic mutant strains showed almost identical larvicidal activity. Therefore, the increased production of toxin is not related to sporulation-specific biochemical changes.

Bacillus thuringiensis↗
PubMed1997

Characterization of Bacillus thuringiensis isolated from infections in burn wounds.

Four strains of Bacillus thuringiensis were isolated from infections in burn wounds and from water used in the treatment of burn wounds. The strains produced large parasporal inclusion bodies composed of 141, 83, and 81 kDa protoxins. The four strains were tested for insecticidal activity against larvae of Pieris brassicae and Aedes aegypti but showed no activity; Vero cell assays for the production of enterotoxins were also negative. Attempts to classify the strains according to flagellar H-serotype showed them all to be non-flagellated. Apart from two occupational health accidents that occurred during the handling of highly concentrated B. thuringiensis fluids, this is the first report of B. thuringiensis causing non-gastrointestinal clinical infection in immunosuppressed patients.

Aedes↗
PubMed2004

A Bacillus thuringiensis crystal protein with selective cytocidal action to human cells.

Bacillus thuringiensis crystal proteins, well known to be toxic to certain insects but not pathogenic to mammals, are used as insecticidal proteins in agriculture and forest management. We here identified a crystal protein that is non-insecticidal and non-hemolytic but has strong cytocidal activity against various human cells with a markedly divergent target specificity, e.g. highly cytotoxic to HepG2 and Jurkat and less cytotoxic to the normal hepatocyte (HC) and HeLa. In slices of liver and colon cancer tissues, the toxin protein preferentially killed the cancer cells, leaving other cells unaffected. The cytocidal effect of the protein is non-apoptotic with swelling and fragmentation of the susceptible cells, although the apoptotic process does occur when the cell damage proceeded slowly. The amino acid sequence deduced from the nucleotide sequence of the cloned gene of the protein has little sequence homology with the insecticidal crystal proteins of B. thuringiensis. These observations raise the presence of a new group of the B. thuringiensis toxin and the possibility of new applications for the protein in the medical field.

Bacillus thuringiensis↗
PubMed2000

Genetic and biochemical approach for characterization of resistance to Bacillus thuringiensis toxin Cry1Ac in a field population of the diamondback moth, Plutella xylostella.

Four subpopulations of a Plutella xylostella (L.) strain from Malaysia (F(4) to F(8)) were selected with Bacillus thuringiensis subsp. kurstaki HD-1, Bacillus thuringiensis subsp. aizawai, Cry1Ab, and Cry1Ac, respectively, while a fifth subpopulation was left as unselected (UNSEL-MEL). Bioassays at F(9) found that selection with Cry1Ac, Cry1Ab, B. thuringiensis subsp. kurstaki, and B. thuringiensis subsp. aizawai gave resistance ratios of >95, 10, 7, and 3, respectively, compared with UNSEL-MEL (>10,500, 500, >100, and 26, respectively, compared with a susceptible population, ROTH). Resistance to Cry1Ac, Cry1Ab, B. thuringiensis subsp. kurstaki, and B. thuringiensis subsp. aizawai in UNSEL-MEL declined significantly by F(9). The Cry1Ac-selected population showed very little cross-resistance to Cry1Ab, B. thuringiensis subsp. kurstaki, and B. thuringiensis subsp. aizawai (5-, 1-, and 4-fold compared with UNSEL-MEL), whereas the Cry1Ab-, B. thuringiensis subsp. kurstaki-, and B. thuringiensis subsp. aizawai-selected populations showed high cross-resistance to Cry1Ac (60-, 100-, and 70-fold). The Cry1Ac-selected population was reselected (F(9) to F(13)) to give a resistance ratio of >2,400 compared with UNSEL-MEL. Binding studies with (125)I-labeled Cry1Ab and Cry1Ac revealed complete lack of binding to brush border membrane vesicles prepared from Cry1Ac-selected larvae (F(15)). Binding was also reduced, although less drastically, in the revertant population, which indicates that a modification in the common binding site of these two toxins was involved in the resistance mechanism in the original population. Reciprocal genetic crosses between Cry1Ac-reselected and ROTH insects indicated that resistance was autosomal and showed incomplete dominance. At the highest dose of Cry1Ac tested, resistance was recessive while at the lowest dose it was almost completely dominant. The F(2) progeny from a backcross of F(1) progeny with ROTH was tested with a concentration of Cry1Ac which would kill 100% of ROTH moths. Eight of the 12 families tested had 60 to 90% mortality, which indicated that more than one allele on separate loci was responsible for resistance to Cry1Ac.

Animals↗
PubMed1986

Bacillus thuringiensis var. israelensis delta-endotoxin. Cloning and expression of the toxin in sporogenic and asporogenic strains of Bacillus subtilis.

A plasmid-borne gene from Bacillus thuringiensis var. israelensis encoding a 27,340 Mr insecticidal delta-endotoxin has been cloned on a bifunctional multicopy plasmid in a wild-type sporogenic strain and two asporogenic mutants of Bacillus subtilis. The delta-endotoxin gene is expressed at a low level during vegetative growth in all three strains, but the synthesis of the toxin increases markedly during the third hour of stationary phase for both the sporogenic strain and an asporogenic mutant containing the OJ lesion. However, in a stage OA mutant, this increase in delta-endotoxin synthesis is not observed. In both the wild-type sporogenic B. subtilis and the asporogenic OJ strain, phase-bright inclusions, resembling the israelensis crystal in appearance, are visible during late stationary phase. The insoluble inclusions from the B. subtilis transformants, consisting solely of the 27,340 Mr polypeptide, were purified by density gradient centrifugation and found to be extremely toxic to Aedes aegypti larvae. After solubilization in alkaline buffer, this polypeptide was also shown to be haemolytic for human erythrocytes and to lyse Aedes albopictus cells with the same LC50 value as native israelensis delta-endotoxin crystals. During stationary phase, novel mRNA species appear in both the wild-type strain and the OJ mutant, but not in the OA mutant, and these appear to be the major gene-specific transcripts. Transcriptional mapping of delta-endotoxin-specific mRNA has shown that the same region of initiation is used at a relatively low level in all three strains during vegetative growth.

Bacillus subtilis↗
PubMed1996

The chromosome map of Bacillus thuringiensis subsp. canadensis HD224 is highly similar to that of the Bacillus cereus type strain ATCC 14579.

A physical map of the Bacillus thuringiensis subsp. canadensis HD224 chromosome based on AscI, NotI, and SfiI restriction sites has been established. The chromosome map of 4.3 Mb was similar to a revised map of the chromosome of the B. cereus type strain ATCC 14579, except that the B. thuringiensis subsp. canadensis HD224 chromosome lacked a NotI site and had two additional AscI sites. The positions of 27 probes were identical in the common macromap. A probe for the insecticidal toxin gene, cryIA, hybridized only to the B. thuringiensis subsp. canadensis HD224 chromosome. The BssHII ribotype patterns were almost identical confirming the similarity between the two strains.

Bacillus cereus↗
PubMed2004

Isolation and characterization of a strain of Bacillus thuringiensis subsp. morrisoni PG-14 encoding delta-endotoxin Cry1Ac.

Bacillus thuringiensis 656-3, isolated from a soil sample collected at mushroom houses, showed high toxicity to mushroom flies, Lycoriella mali and Coboldia fuscipes. B. thuringiensis 656-3 produced bipyramidal inclusions and reacted with the H antiserum of B. thuringiensis subsp. morrisoni (H8a8b). The plasmid and protein profiles of B. thuringiensis 656-3 were similar to those of its reference strain, subsp. morrisoni PG-14. However, PCR analysis using cry gene primers showed that B. thuringiensis 656-3, unlike its reference strain, had cry4A, cry4B, cry10A, cry11A, and cry1Ac genes, suggesting that B. thuringiensis 656-3 was a unique strain with respect to gene type. In addition, B. thuringiensis 656-3 showed a high level of toxicity against mushroom flies, L. mali and C. fuscipes.

Agaricales↗
PubMed2001

Cloning and expression of the binary toxin gene from Bacillus sphaericus IAB872 in a crystal-minus Bacillus thuringiensis subsp. israelensis.

Bacillus sphaericus IAB872 has high toxicity against susceptible Culex spp. and medium larvicidal activity against binary toxin-resistant Culex spp. Sequence analysis revealed that the sequence of the binary toxin gene from IAB872 was totally identical to that of the reference strain 2362. The recombinant plasmids were introduced into an acrystalliferous B. thuringiensis strain 4Q7, and the resulting transformants produced parasporal inclusion composed of 51 kDa and 42 kDa proteins during sporulation. SDS-PAGE and Western blot further confirmed that B. thuringiensis transformants were able to express the binary toxin in a high level. Toxicity bioassays showed that they performed high toxicity to susceptible Culex spp. larvae, but no toxicity to resistant Culex larvae. It was, therefore, suggested that other unknown toxins perhaps existed in the wild strain IAB872 except the binary toxin. Their modes of action might be different from that of binary toxin, and they were possibly responsible for the activity of the wild strain IAB872 against resistant mosquito larvae.

Animals↗
PubMed1984

Oral toxicity of Bacillus thuringiensis subsp. israelensis to adult mosquitoes.

The solubilized entomotoxin of Bacillus thuringiensis subsp. israelensis killed adult male and female mosquitoes of several genera and of various physiological states when it was administered orally. Adult mosquito mortality was further influenced when the preparation was contained in sucrose solution. The potential implication for the control of adult mosquitoes is discussed.

Aedes↗