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PubMed2000

Susceptibility of Spanish populations of the corn borers Sesamia nonagrioides (Lepidoptera: Noctuidae) and Ostrinia nubilalis (Lepidoptera: Crambidae) to a Bacillus thuringiensis endotoxin.

Baseline susceptibility to the Cry1Ab delta-endotoxin from Bacillus thuringiensis (Berliner) was determined for four populations of Sesamia nonagrioides (Lefebvre) and two populations of Ostrinia nubilalis (Hübner) from Spain. This study shows that S. nonagrioides is at least as susceptible as O. nubilalis to B. thuringiensis Cry1Ab protein. We found small differences in susceptibility among the Spanish populations of S. nonagrioides that can be attributed to natural variation, because there are no records of B. thuringiensis products being used on corn crops in Spain. There were no differences in susceptibility to Cry1Ab toxin between the two populations of O. nubilalis.

Animals↗
PubMed1986

Three classes of homologous Bacillus thuringiensis crystal-protein genes.

Four homologous genes encoding insecticidal crystal proteins from Bacillus thuringiensis have been cloned in Escherichia coli. Differences in lengths of HindIII restriction fragments containing the 5' ends of the genes allowed the identification of three classes termed the '4.5- and 5.3- and 6.6-kb-class genes'. A survey of 24 strains from subspecies kurstaki and thuringiensis revealed strains containing one, two, or three of these classes of crystal protein genes. The 4.5- and 6.6-kb-class genes encode polypeptides of Mr 133,500 and 133,330, respectively, while the two 5.3-kb-class genes encode a ca. 130-kDa polypeptide. The polypeptide composition of crystals from the B. thuringiensis strains agreed with the composition predicted from the content of the three classes of genes. The representative genes from each class were isolated from B. thuringiensis plasmids of different sizes. An analysis of plasmid DNA flanking three of these genes revealed a complex pattern of two different inverted repeat (IR) sequences, IR2150 and IR1750. Four variant forms of IR1750 were found. The IR elements were located near deletions and rearrangements adjacent to crystal protein genes and may account for the diversity of plasmids carrying crystal protein genes in other subspecies of B. thuringiensis.

Bacillus thuringiensis↗
PubMed1992

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

Bacillus thuringiensis was isolated from 36 of 50 residue samples obtained from an animal feed mill (a stored-product environment). Of 710 selected colonies having Bacillus cereus-B. thuringiensis morphology isolated from the samples, 477 were classified as B. thuringiensis because of production of parasporal delta-endotoxin crystals. There was a diverse population of B. thuringiensis, as revealed by differentiation of the isolates into 36 subgroups by using (i) their spectra of toxicity to the lepidopterans Heliothis virescens, Pieris brassicae, and Spodoptera littoralis and the dipteran Aedes aegypti and (ii) their parasporal crystal morphology. A total of 55% of the isolates were not toxic to any of these insects at the concentrations used in the bioassays; 40% of all isolates were toxic to one or more of the Lepidoptera; and 20, 1, and 1% of the isolates were toxic to only P. brassicae, H. virescens, and S. littoralis, respectively. The most frequent toxicity was toxicity to P. brassicae (36% of all isolates); 18% of the isolates were toxic to A. aegypti (5% exclusively), 10% were toxic to H. virescens, and 4% were toxic to S. littoralis. Toxicity to P. brassicae was more often linked with toxicity to H. virescens than with toxicity to S. littoralis. The frequency of toxicity was significantly greater in isolates that produced bipyramidal crystals than in isolates that produced irregular pointed, irregular spherical, rectangular, or spherical crystals.

Journal Article↗
PubMed1999

Development and field performance of a broad-spectrum nonviable asporogenic recombinant strain of Bacillus thuringiensis with greater potency and UV resistance.

The main problems with Bacillus thuringiensis products for pest control are their often narrow activity spectrum, high sensitivity to UV degradation, and low cost effectiveness (high potency required). We constructed a sporulation-deficient SigK(-) B. thuringiensis strain that expressed a chimeric cry1C/Ab gene, the product of which had high activity against various lepidopteran pests, including Spodoptera littoralis (Egyptian cotton leaf worm) and Spodoptera exigua (lesser [beet] armyworm), which are not readily controlled by other Cry delta-endotoxins. The SigK(-) host strain carried the cry1Ac gene, the product of which is highly active against the larvae of the major pests Ostrinia nubilalis (European corn borer) and Heliothis virescens (tobacco budworm). This new strain had greater potency and a broader activity spectrum than the parent strain. The crystals produced by the asporogenic strain remained encapsulated within the cells, which protected them from UV degradation. The cry1C/Ab gene was introduced into the B. thuringiensis host via a site-specific recombination vector so that unwanted DNA was eliminated. Therefore, the final construct contained no sequences of non-B. thuringiensis origin. As the recombinant strain is a mutant blocked at late sporulation, it does not produce viable spores and therefore cannot compete with wild-type B. thuringiensis strains in the environment. It is thus a very safe biopesticide. In field trials, this new recombinant strain protected cabbage and broccoli against a pest complex under natural infestation conditions.

Animals↗
PubMed1984

Larvicidal activity of Bacillus thuringiensis subsp. israelensis in the dipteran Haematobia irritans.

A strain of Bacillus thuringiensis subsp. israelensis was found to be larvicidal to horn flies, Haematobia irritans (L. [Diptera:Muscidae]). The toxic activity was particulate, appeared during sporulation, and could be prevented by the addition of streptomycin before sporulation. Density gradient centrifugation in Renografin was used to separate endospores, crystals, and low-density particulate matter (fraction 3) from sporulated preparations. Larvicidal activity was restricted to purified crystals and fraction 3, indicating that delta-endotoxin of B. thuringiensis subsp. israelensis was active against horn fly larvae. Purified crystals produced mortality during larval feeding stages, but not pupal stages. Fraction 3 produced significant mortality during both larval and pupal stages. The mortality data indicated the presence of at least two dipteran-active toxins.

Bacillus thuringiensis↗
PubMed2005

Toxicity of Bacillus thuringiensis to parasitic and free-living life-stages of nematode parasites of livestock.

A collection of Bacillus thuringiensis (Bt) strains (Bts) were screened for activity against the free-living larval stages of nematode parasites of livestock. Two strains were identified with significant activity in inhibiting larval development of Haemonchus contortus, Trichostrongylus colubriformis and Ostertagia circumcincta. These strains were also toxic to the adult parasitic stages of these nematode species in vitro. Adult H. contortus and O. circumcincta showed complete cessation of movement within 2 and 4 days, respectively. Trichostrongylus colubriformis adults were less affected, however, movement was still significantly reduced compared with controls. The in vitro activity against the larval stages was of a magnitude similar to or greater than that seen with the anthelmintic drugs thiabendazole and levamisole. N-terminal amino acid sequencing indicated that the two Bts contained either Cry5A and Cry5B proteins, or a Cry13 protein, and the presence of the corresponding cry5A, cry5B and cry13 genes was confirmed by PCR and sequencing. Bacillus thuringiensis spore-crystal suspensions exposed to acidic pH conditions (pH<or=3) showed greatly reduced toxicity in subsequent bioassays with nematode larvae, highlighting the need to protect the toxin from the acidic conditions of the sheep abomasum if it were to be administered per os as an anthelmintic. This study indicates that both the parasitic adult stages and the free-living larval stages of economically significant nematode parasites are susceptible to the effects of Bt, thus identifying this group of toxins as potential biocontrol agents.

Animals↗
PubMed1995

Mapping and characterization of the entomocidal domain of the Bacillus thuringiensis CryIA(b) protoxin.

The amino acid sequences necessary for entomocidal activity of the CryIA(b) protoxin of Bacillus thuringiensis were determined. Introduction of stop codons behind codons Arg601, Phe604 or Ala607 showed that amino acid residues C-terminal to Ala607 are not required for insecticidal activity and that activation by midgut proteases takes place distal to Ala607. The two shortest polypeptides, deleted for part of the highly conserved beta-strand, were prone to proteolytic degradation, explaining their lack of toxicity. Apparently, this beta-strand is essential for folding of the molecule into a stable conformation. Proteolytic activation at the N-terminus was investigated by removing the first 28 codons, resulting in a translation product extending from amino acid 29 to 607. This protein appeared to be toxic not only to susceptible insect larvae such as Manduca sexta and Heliothis virescens, but also to Escherichia coli cells. An additional mutant, encoding only amino acid residues 29-429, encompassing the complete putative pore forming domain, but lacking a large part of the receptor-binding domain, was similarly toxic to E. coli cells. This suggests a role for the N-terminal 28 amino acids in rendering the toxin inactive in Bacillus thuringiensis, and indicates that the cytolytic potential of the pore forming domain is only realized after proteolytic removal of these residues by proteases in the insect gut. In line with this hypothesis are results obtained with a mutant protein in which Arg28 at the cleavage site was replaced by Asp. This substitution prevented the protein from being cleaved by trypsin in vitro, and reduced its toxicity to M. sexta larvae.

Animals↗
PubMedDate not supplied

[Change in the permeability of liposome phospholipid membranes under the effect of Bacillus thuringiensis delta-endotoxins].

We studied release of the fluorescent calcein marker from egg-lecithin liposomes under action of intact delta-endotoxin from Bacillus thuringiensis var. israilensis, and hydrolysed preparation of delta-endotoxin from Bacillus thuringiensis var. kurstaki together with the motional parameters of 5- and 12-doxyl stearic radical probes in the liposomal membrane. The yield of the non-penetrating fluorescent marker was shown to be a sensitive indicator of the disturbance of the membrane barrier function.

Bacillus thuringiensis↗
PubMed1989

Transformation of Bacillus thuringiensis vegetative cells by electroporation.

A highly efficient procedure for the transformation of Bacillus thuringiensis and Bacillus subtilis using covalently closed circular plasmid DNA was developed by using the small Staphylococcus aureus plasmid pC194 and electroporation. We have achieved transformation efficiencies in B. thuringiensis subsp. kurstaki (HD-73) greater than 5 x 10(6) transformants/micrograms plasmid DNA. The electro-transformation (or electroporation) procedure also worked with B. subtilis 168 although at a 200-fold less level of efficiency. The results indicated that the plasmid exists in double and single-stranded forms both in B. subtilis and B. thuringiensis. A second single-stranded species was also observed in both species. This technique may prove to be applicable to other members of the genus Bacillus.

Bacillus thuringiensis↗
PubMed2006

Cyt2Ba of Bacillus thuringiensis israelensis: activation by putative endogenous protease.

The gene cyt2Ba of Bacillus thuringiensis subsp. israelensis was cloned for expression, together with p20, in an acrystalliferous strain. The large hexagonal crystals formed were composed of Cyt2Ba, which facilitated its purification. Crystal solubilization in the presence of endogenous proteases (with spores and cell debris) enabled quick and simple procedure to obtain rather pure and active toxin species by cleavage between amino acid residues 34 and 35, most likely by a camelysin-like protease that was discovered in association with activated Cyt2Ba. The product of this cleavage displayed haemolytic activity comparable to that of exogenously activated Cyt2Ba. The sequence of this putative protease shares high homology with the cell envelope-bound metalloprotease (camelysin) of the closely related species Bacillus cereus.

Amino Acid Sequence↗
PubMed1994

Expression of the crystal protein gene under the control of the alpha-amylase promoter in Bacillus thuringiensis strains.

The expression of an insecticidal crystal protein gene of Bacillus thuringiensis under the control of the alpha-amylase gene promoter was investigated. The cryIC gene, which encodes a protein known to have a unique activity against Spodoptera (armyworm) species, was used in this investigation. The cryIC gene was placed, along with the alpha-amylase promoter from B. subtilis, in a B. thuringiensis-derived cloning vector, generating a pair of recombinant plasmids, pSB744 and pSB745. The cloning vector that contains the minimal replicon of B. thuringiensis subsp. kurstaki HD73 is stably maintained in a variety of B. thuringiensis strains, as previously reported by Gamel and Piot (Gene 120:17-26, 1992). The present study confirmed that the recombinant plasmids are also stably maintained in B. thuringiensis subsp. kurstaki Cry-B and HD73 growing in media without selection pressure for at least 48 h. The cryIC gene on the recombinant plasmids were notably expressed at high levels in both recombinant strains. Expression of the introduced cryIC gene on the recombinant plasmid in B. thuringiensis subsp. kurstaki HD73 did not impair expression of the resident cryIA(c) gene. The CryIA(c) protein is known to have a high level of activity against loopers such as Trichoplusia ni (the cabbage looper). As a result of coexpression of the introduced cryIC gene and the resident cryIA(c) gene, recombinant strain HD73 acquired an additional insecticidal activity against Spodoptera exigua (the beet armyworm) whereas the original activity level against T. ni was maintained.

Animals↗
PubMed2000

[Characterization of the insecticidal crystal protein genes of Bacillus thuringiensis YBT-1520].

The insecticidal crystal protein genes of highly toxic Bacillus thuringiensis YBT-1520 were analyzed. Southern hybridization and PCR analysis indicated that this strain bears cry1Aa, cry1Ab, cry1Ac and cry2 genes. The copy number of three cry1A genes is different and cry1Ac gene (here named cry218) is the highest. The restriction location of three genes is different from that in typical strains, such as HD-1 and HD-73 strains. 4190 bp nucleotide sequence of cry218 gene was determined and this gene was named cry1Ac10 in the recently published gene nomenclature.

Bacillus thuringiensis↗
PubMed2003

Transgenic loblolly pine (Pinus taeda L.) plants expressing a modified delta-endotoxin gene of Bacillus thuringiensis with enhanced resistance to Dendrolimus punctatus Walker and Crypyothelea formosicola Staud.

A synthetic version of the CRY1Ac gene of Bacillus thuringiensis has been used for the transformation of loblolly pine (Pinus taeda L.) using particle bombardment. Mature zygotic embryos were used to be bombarded and to generate organogenic callus and transgenic regenerated plants. Expression vector pB48.215 DNA contained a synthetic Bacillus thuringiensis (B.t.) CRY1Ac coding sequence flanked by the double cauliflower mosaic virus (CaMV) 35S promoter and nopaline synthase (NOS) terminator sequences, and the neomycin phosphotransferase II (NPTII) gene controlled by the promoter of the nopaline synthase gene was introduced into loblolly pine tissues by particle bombardment. The transformed tissues were proliferated and selected on media with kanamycin. Shoot regeneration was induced from the kanamycin-resistant calli, and transgenic plantlets were then produced. More than 60 transformed plants from independent transformation events were obtained for each loblolly pine genotype tested. The integration and expression of the introduced genes in the transgenic loblolly pine plants was confirmed by polymerase chain reactions (PCR) analysis, by Southern hybridization, by Northern blot analysis, and by Western blot analysis. Effective resistance of transgenic plants against Dendrolimus punctatus Walker and Crypyothelea formosicola Staud was verified in feeding bioassays with the insects. The transgenic plants recovered could represent a good opportunity to analyse the impact of genetic engineering of pine for sustainable resistance to pests using a B. thuringiensis insecticidal protein. This protocol enabled the routine transformation of loblolly pine plants that were previously difficult to transform.

Amino Acid Oxidoreductases↗
PubMedDate not supplied

Potentiation of antitumor activity of bleomycin towards solid tumors in mice by Bacillus thuringiensis subsp. israelensis toxin.

We previously reported that a 25-kDa Bacillus thuringiensis subsp. israelensis (BTI) toxin is cytotoxic to cultured tumor cells and can also potentiate the cytotoxic effect of some antitumor agents in vitro. In this study, we examined the in vivo effect of BTI toxin on the potentiation of antitumor activity of bleomycin (BLM) against solid tumor-bearing mice. Three tumor cell lines, Ehrlich carcinoma, B16 melanoma and Meth A fibrosarcoma, were employed. It was shown that dose of BTI toxin, ineffective alone, potentiated the antitumor activity of BLM when used in combination.

Animals↗
PubMed1988

Interaction between the delta-endotoxin produced by Bacillus thuringiensis ssp. entomocidus and liposomes.

The delta-endotoxin produced by Bacillus thuringiensis ssp. entomocidus induced the release of encapsulated [14C]sucrose from reverse-phase vesicles composed of phosphatidylcholine and cholesterol. No such release was detected when the phospholipid component of the vesicles was either phosphatidylethanolamine, phosphatidylglycerol, or sphingomyelin. The toxin-induced release was competitively inhibited by negatively charged organic ions while positively charged organic ions, apart from choline chloride, had no such effect. The existence of a polar head group in the phospholipid as well as intermolecular hydrogen bonding at the membrane surface, was found to be of major importance in the toxin-liposome interaction.

Anions↗
PubMed1992

[Morphology and delta-endotoxin proteins of Bacillus thuringiensis from soils and their toxicities to insects].

94 strains of Bacillus thuringiensis were isolated from soils in southwest and northwest of China. The morphology of cells, spores and parasporal crystals of these strains was investigated under transmission and scanning electro-microscope. Proteins of delta-endotoxins from all strains were analysed by rapid SDS-PAGE. 9 species of insects in Lepidoptera, Coleoptera and Diptera were tested for assay of delta-endotoxins. Some kinds of parasporal crystals were quite different in form and in composition of protein from those reported before. Most of strains were nontoxic to all of 9 species used in bio-assay. Some strains were very effective in species of Coleoptera or Noctuidae.

Animals↗
PubMed1993

Characterization of a Bacillus thuringiensis strain which is toxic to the housefly Musca domestica.

A Bacillus thuringiensis isolate has been discovered which is toxic to the common housefly (Musca domestica) as well as other Diptera and Lepidoptera. Crystal delta-endotoxins purified from this isolate killed 50% of Musca larvae at a concentration of 10.2 micrograms/ml, and beta-exotoxin was not detected. Sodium dodecyl polyacrylamide gel electrophoresis of the purified crystals revealed three protein species which were related to CryIA(b), CryIB and CryIIA toxins on the basis of immunoreactivity and amino-terminal sequence determination. Southern blot and DNA restriction analyses suggested that the strain has sequences related to one cryIA(b), one cryIIA, and two cryIIB genes.

Amino Acid Sequence↗
PubMed1995

Crystallization of a membrane pore-forming protein with mosquitocidal activity from Bacillus thuringiensis subspecies kyushuensis.

CytB, a membrane pore-forming toxin from Bacillus thuringiensis subspecies kyushuensis, is specifically toxic to dipteran insect larvae but broadly cytolytic in vitro. It has been purified in the protoxin form from a recombinant Escherichia coli source and crystals have been obtained which diffract X-rays to at least 2.6 A resolution. The tendency for CytB to aggregate in solution was overcome by including 50 mM of urea or 8 mM of ethanolamine during crystallization. Mutants designed to add or subtract single cysteine residues for the purpose of heavy atom derivative preparation were similarly purified and crystallized. The crystals are hexagonal bipyramids. They belong to space group P6(1)22 (or P6(5)22) with lattice constants a = b = 67.34 A, c = 170.96 A, and contain one molecule of the CytB protoxin (MW 29235) per asymmetric unit and 27% solvent by volume.

Bacillus thuringiensis↗