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PubMed1995

Antibiotic production and biocontrol activity by Bacillus subtilis CL27 and Bacillus pumilus CL45.

Bacillus subtilis CL27 and B. pumilus CL45 showed similar activity against Botrytis cinerea in in vitro plate assays. In a seedling bioassay, however, B. subtilis CL27 had activity similar to a commercial fungicide while B. pumilus CL45 failed completely to prevent seedling damping-off caused by Bot. cinerea. Antibiotic production by the two Bacillus strains was found to depend on the growth substrate and highest antibiotic production was found on media based on homogenized cabbage tissue. Antibiotic activity was found to depend on the pH and nutrient concentration in the assay medium. Antifungal antibiotics produced by B. subtilis CL27 and B. pumilus CL45 in different fermentation media were separated by thin layer chromatography. As suspected from the activity spectrum, three antibiotics (one with activity against Alternaria brassicicola, one with activity against Botrytis cinerea and one with activity against both fungi) could be detected in the fermentation broth of CL27, but only one in the fermentation broth of CL45. The two antibiotics produced by strain CL27 with activity against A. brassicicola were identified as peptides since their bands on the TLC plates developed a green to blue/green colour after treatment with 4,4'-tetramethyldiamino-diphenylmethane (TDM) reagent. The third antibiotics produced by strain CL27 and antibiotic produced by CL45 had a similar Rf-value and appeared not to be peptides based on the reaction with TDM. However, they showed a slightly different activity spectrum when tested against a range of different fungi. Antibiotic production was clearly indicated as the mode of action of in vivo biocontrol by strain CL27 against damping off caused by Bot. cinerea of Astilbe micro-plants, because a u.v.-induced antibiotic negative mutant strain CL27b showed no activity in seedling bioassays in vivo. Also the mutant strain CL27a which produced the two peptide antibiotics but had lost the ability to produce the non-peptide antibiotic, showed greatly reduced in vivo activity.

Antibiosis↗
PubMed1988

Homology between endoglucanase Z of Erwinia chrysanthemi and endoglucanases of Bacillus subtilis and alkalophilic Bacillus.

Nucleotide sequencing of the celZ gene encoding the extracellular endoglucanase Z of Erwinia chrysanthemi indicated the presence of an open reading frame encoding 428 amino acids. The mature protein appeared to be extended by a signal peptide of 43 amino acids; this sequence is unusually long and positively charged (+5). It was shown to function as a signal peptide by fusing it to a truncated phoA gene encoding Escherichia coli alkaline phosphatase. Comparison of the encoded sequence with those of the endoglucanases of Bacillus subtilis and alkalophilic Bacillus revealed the existence of a region of extensive homology occurring in all three proteins at about the same distance from the NH2-terminal end. These regions may be involved in substrate binding and/or catalytic sites.

Alkaline Phosphatase↗
PubMed1978

Purification and characterization of the penicillin-binding protein that is the lethal target of penicillin in Bacillus megaterium and Bacillus licheniformis. Protein exchange and complex stability.

The penicillin-binding protein that is thought to be the lethal target of penicillin in Bacillus megaterium (protein 1) has been purified to greater than 95% homogeneity. The membrane-bound penicillin-binding proteins were solubilized with a non-ionic detergent and partially separated from each other by ion-exchange chromatography on DEAE-Sepharose CL-6B. Protein 1 was subsequently purified by covalent affinity chromatography on ampicillin-affinose. Bacillus licheniformis contains an equivalent penicillin-binding protein (protein 1) that can be more readily purified to virtual homogeneity in a one-step procedure. It was separated from the other penicillin-binding proteins by utilizing the observation that in this organism, this particular protein is the only one whose covalent complex with benzylpenicillin subsequently breaks down. Membranes were treated with saturating concentrations of benzylpenicillin followed by the removal of free penicillin and further incubation to allow the complex between benzylpenicillin and protein 1 to break down. The penicillin-binding proteins were then solubilized and applied to a column of ampicillin-affinose to which only protein 1 was bound as the other penicillin-binding proteins still had benzylpenicillin bound to them. Pure protein 1 was eluted from the affinity resin with hydroxylamine. The interaction of benzylpenicillin with purified protein 1 has been studied by separating unbound antibiotic from the benzylpenicillin . protein complex by paper electrophoresis. Benzylpenicillin reacts with the protein rapidly to form a covalent complex and the fully saturated complex has a molar ratio of bound [14C] benzylpenicillin: protein of 0.7:1. The complex breaks down, obeying first-order kinetics, with a half-life of 16 min at 35 degrees C, a value identical to that obtained with the membrane-bound protein. The concentration of benzylpenicillin that results in the formation of 50% of the maximum amount of benzylpenicillin . protein complex is that at which the molar amount of benzylpenicillin present is equal to 50% of the molar amount of penicillin-binding protein, rather than being a measure of any of the kinetic parameters of the binding reaction. This observation may be significant in the interpretation of previous results where the amounts of penicillins needed to kill cells or to inhibit penicillin-sensitive reactions have been expressed as concentrations. The possible importance of the breakdown of beta-lactam . protein complexes in the clinical use of these antibiotics is discussed.

Bacillus↗
PubMed2004

Field evaluation of the efficacy of a probiotic containing Bacillus licheniformis and Bacillus subtilis spores, on the health status and performance of sows and their litters.

The aim of this study was to assess the efficacy of BioPlus 2B, a probiotic containing Bacillus licheniformis and Bacillus subtilis spores, on the health status and productivity of sows and their litters. A total of 109 gilts and sows were allocated into two experimental groups, as follows: untreated controls (UC) and BioPlus 2B (same feeding as the UC group plus BioPlus 2B) at a dose of 400 g/ton of feed (equal to 1.28 x 10(6) viable spores/g of feed). Treatment started from the day of allocation (14 days prior to the expected farrowing) up to the weaning day. Homogeneity of the groups was satisfied with regard to the parity. From the results it was evident that BioPlus 2B supplementation of the feed improved gilt/sow performance as shown by: (i) the increase of sow feed consumption during the first 14 days postpartum and (ii) the decrease of sow weight loss during the suckling period. Certain blood and milk parameters were significantly improved, as shown by higher serum cholesterol and total lipids concentrations and higher milk fat and protein content at mid-suckling period. As a consequence, a positive effect was also noticed as regard litter health and performance characteristics in terms of: (i) decrease in piglet diarrhoea score, (ii) decrease in pre-weaning mortality thus leading to increase in the number of weaned piglets per litter and (iii) increase in piglet body weight at weaning. Moreover, BioPlus 2B tended to improve the health status and fertility of sows demonstrating: (i) tendency to a lower proportion of sows with Mastitis-Metritus-Agalactia (MMA) problems and (ii) lower proportion of sows returning to oestrus.

Animal Feed↗
PubMed2006

Effect of Bacillus licheniformis and Bacillus subtilis supplementation of ewe's feed on sheep milk production and young lamb mortality.

The purpose of this pilot study was to evaluate under field conditions the effect of a probiotic containing Bacillus licheniformis and Bacillus subtilis on young lamb mortality and sheep milk production when administered in the late pregnancy and lactation feed of ewes. In a sheep farm, two groups of milking ewes with identical genetic material, management, nutrition, health status and similar production characteristics were formed. One group (46 ewes) served as control, while the other one (48 ewes) served as a probiotic-treated group. Both groups of ewes received a similar feeding regiment, but the ewes of the second group were additionally offered a probiotic product containing B. licheniformis and B. subtilis (BioPlus 2B, Chr. Hansen, Denmark) at the approximate dose of 2.56 x 10(9) viable spores per ewe per day. Lamb mortality during the 1.5 months suckling period, and milk yield during the 2 months of milk collection for commercial purposes have been recorded. In the non-treated control group, 13.1% mortality was observed versus 7.8% in the probiotic-treated group (P = 0.33), with mortality being mainly due to diarrhoea. Microbiological examination of diarrhoeic faeces from some of the dead lambs in both groups revealed the presence of Escherichia coli. The average daily milk yield per ewe was significantly lower in the control group (0.80 l) than that in the probiotic-treated group (0.93 l) (P < 0.05). Fat and protein content of milk in ewes that received probiotics was significantly (P < 0.05) increased compared with untreated ewes. It was concluded that supplementing ewe's feed with probiotics may have beneficial effect on subsequent milk yields, fat and protein content.

Animal Feed↗
PubMed1995

Bacillus cereus and Bacillus thuringiensis isolated in a gastroenteritis outbreak investigation.

During investigation of a gastroenteritis outbreak in a chronic care institution, Norwalk virus was found in stool specimens from two individuals and bacterial isolates presumptively identified as Bacillus cereus were isolated from four individuals (including one with Norwalk virus) and spice. Phage typing confirmed all Bacillus clinical isolates were phage type 2. All clinical isolates were subsequently identified as B. thuringiensis when tested as a result of a related study (L. Leroux, personal communication). Eight of 10 spice isolates were phage type 4. All B. cereus and B. thuringiensis isolates showed cytotoxic effects characteristic of enterotoxin-producing B. cereus. An additional 20 isolates each of B. cereus and B. thuringiensis from other sources were tested for cytotoxicity. With the exception of one B. cereus, all showed characteristic cytotoxic patterns.

Bacillaceae Infections↗
PubMed1993

Analysis of common antigen of flagella in Bacillus cereus and Bacillus thuringiensis.

Flagellar antigen of Bacillus cereus H.1 was purified and tested for serodiagnostic antigen by ELISA. The antibody against the flagellar antigen of B. cereus H.1 reacted not only with the homologous specific antigen but also reacted with the flagellar antigens of 23 strains of B. cereus. This common flagellar antigen of B. cereus was found to be due to 61-kDa protein by SDS-PAGE and immunoblot assay. Monoclonal antibody H15A5 against common antigenic epitope of B. cereus also reacted with flagellar antigens of 21 strains of Bacillus thuringiensis by ELISA. This monoclonal antibody reacted with the 61-kDa protein of the flagella of B. cereus H.1 and H.2 and B. thuringiensis Kurstaki HD1, Alesti and Aizawai juroi by immunoblot analysis. These results indicated that the common antigenic epitope of the 61-kDa protein existed in the flagella both of B. cereus and B. thuringiensis.

Antibodies, Bacterial↗
PubMed2002

Co-linear scaffold of the Bacillus licheniformis and Bacillus subtilis genomes and its use to compare their competence genes.

We have established the co-linear regions of Bacillus licheniformis, an industrially important bacterium, and Bacillus subtilis, a model bacterium. In the co-linear regions, revealed by PCR, gene content and order are presumed to be conserved. These regions constitute approximately 60% of the compared chromosomes. Sequencing of the competence genes of B. licheniformis allowed us to validate the approach, and to demonstrate how it can be used for the comparative analysis of complex genetic systems. A new insertion sequence, designated IS3Bli1, was discovered in the competence region of the analyzed B. licheniformis strain.

Bacillus↗
PubMed2002

Extremely high frequency of common flagellar antigens between Bacillus thuringiensis and Bacillus cereus.

Bacillus cereus isolates, recovered from natural environments of Japan, were examined for their flagellar (H) antigenicities with the reference H antisera against Bacillus thuringiensis serotypes H1-H55. Of 236 B. cereus isolates tested, 165 (70%) were agglutinated with the reference antisera available. The frequencies of seropositive isolates were: 77% in soils, 68% on phylloplanes, and 60% in animal fecal populations. Among the 45 H serogroups detected, the serovar shandongiensis (H22) was the predominant, followed by the serovars entomocidus (H6), indiana (H16), pakistani (H13), and neoleonensis (H24ab). These five H serovars were commonly distributed in the three populations from different sources.

Antigens, Bacterial↗
PubMed1990

Bacitracin-induced proteins in Bacillus subtilis and Bacillus thuringiensis and their relationship with resistance.

Bacitracin induced one protein (bacitracin-induced protein [BIP]) in Bacillus thuringiensis and two proteins (BIP1 and BIP2) in Bacillus subtilis that were localized in the membrane. Divalent cations acted as cofactors for induction in all three cases. Growth was initially inhibited by the antibiotic, but following induction of proteins growth resumed. B. subtilis cells possessing BIPs were able to duplicate at a normal rate in the presence of bacitracin. The amount of B. subtilis BIPs diminished markedly after a few divisions in the absence of the antibiotic and the organism simultaneously reverted to the susceptible state. Induction of the proteins did not take place after the fourth or fifth hour of the stationary phase. The B. thuringiensis BIP was also induced by vancomycin. Bacitracin did not induce the synthesis of specific proteins in susceptible (Micrococcus lysodeikticus) or outer membrane-possessing resistant bacteria (Escherichia coli).

Bacillus subtilis↗
PubMed1985

Molecular cloning of Bacillus sphaericus penicillin V amidase gene and its expression in Escherichia coli and Bacillus subtilis.

The Bacillus sphaericus gene coding for penicillin V amidase, which catalyzes the hydrolysis of penicillin V to yield 6-aminopenicillanic acid and phenoxyacetic acid, has been isolated by molecular cloning in Escherichia coli. The gene is contained within a 2.2-kilobase HindIII-PstI fragment and is expressed when transferred into E. coli and Bacillus subtilis. The expression in B. subtilis carrying the recombinant plasmid is approximately two times higher than in the original B. sphaericus strain. A comparison of the purified enzyme from B. sphaericus and the expressed gene product in E. coli minicells suggests that the native enzyme consists of four identical subunits, each with a molecular weight of 35,000.

Amidohydrolases↗
PubMed1990

Transfer of the toxin protein genes of Bacillus sphaericus into Bacillus thuringiensis subsp. israelensis and their expression.

The genes encoding the toxic determinants of Bacillus sphaericus have been expressed in a nontoxic and a toxic strain of Bacillus thuringiensis subsp. israelensis. In both cases, the B. sphaericus toxin proteins were produced at a high level during sporulation of B. thuringiensis and accumulated as crystalline structures. B. thuringiensis transformants expressing B. sphaericus and B. thuringiensis subsp. israelensis toxins did not show a significant enhancement of toxicity against Aedes aegypti, Anopheles stephensi, and Culex pipiens larvae.

Aedes↗
PubMed1990

Molecular cloning of the 130-kilodalton mosquitocidal delta-endotoxin gene of Bacillus thuringiensis subsp. israelensis in Bacillus sphaericus.

A 3.7-kilobase (kb) XbaI fragment harboring the cryIVB gene (L. Thorne, F. Garduno, T. Thompson, D. Decker, M. A. Zounes, M. Wild, A. M. Walfield, and T. J. Pollock, J. Bacteriol. 166:801-811, 1986) which encoded a 130-kilodalton (kDa) mosquitocidal toxin from a 110-kb plasmid of Bacillus thuringiensis subsp. israelensis 4Q2-72 was cloned into pUC12 and transformed into Escherichia coli. The clone with a recombinant plasmid (designated pBT8) was toxic to Aedes aegypti larvae. The fragment (3.7 kb) was ligated into pBC16 (tetracycline resistant [Tcr]) and transformed by the method of protoplast transformation into Bacillus sphaericus 1593 and 2362, which were highly toxic to Anopheles and Culex mosquito larvae but less toxic to Aedes larvae. After cell regeneration on regeneration medium, the Tcr plasmids from transformants (pBTC1) of both strains of B. sphaericus were prepared and analyzed. The 3.7-kb XbaI fragment from the B. thuringiensis subsp. israelensis plasmid was shown to be present by agarose gel electrophoresis and Southern blot hybridization. In addition, B. sphaericus transformants produced a 130-kDa mosquitocidal toxin which was detected by Western (immuno-) blot analysis with antibody prepared against B. thuringiensis subsp. israelensis 130-kDa mosquitocidal toxin. The 50% lethal concentrations of the transformants of strains 1593 and 2362 against A. aegypti larvae were 2.7 X 10(2) and 5.7 X 10(2) cells per ml, respectively. This level of toxicity was comparable to the 50% lethal concentration of B. thuringiensis subsp. israelensis but much higher than that of B. sphaericus 1593 and 2362 (4.7 X 10(4) cells per ml) against A. aegypti larvae.(ABSTRACT TRUNCATED AT 250 WORDS)

Aedes↗
PubMed1992

Expression of the mosquitocidal toxins of Bacillus sphaericus and Bacillus thuringiensis subsp. israelensis by recombinant Caulobacter crescentus, a vehicle for biological control of aquatic insect larvae.

In the quest for effective control of mosquitoes, attention has turned increasingly to strains of the bacteria Bacillus sphaericus and Bacillus thuringiensis subsp. israelensis, which produce potent toxins with specific mosquitocidal activities. However, sedimentation of the bacterial spores limits the duration of effective control after field application of these bacilli. We describe here the cloning of genes encoding the 51.4- and 41.9-kDa toxins from B. sphaericus 2297, the 100-kDa toxin from B. sphaericus SSII-1, and the 130-kDa toxin from B. thuringiensis subsp. israelensis into the broad-host-range plasmid pRK248 and the transfer of these genes for expression in Caulobacter crescentus CB15. The recombinant C. crescentus cells were shown to be toxic to mosquito larvae. Caulobacter species are ubiquitous microorganisms residing in the upper regions of aquatic environments and therefore provide the potential for prolonged control by maintaining mosquitocidal toxins in larval feeding zones.

Animals↗
PubMed1997

Cloning of novel enterotoxin genes from Bacillus cereus and Bacillus thuringiensis.

A novel enterotoxin gene was cloned from Bacillus cereus FM1, and its nucleotide sequence was determined. Previously, a 45-kDa protein causing characteristic enterotoxin symptoms in higher animals had been isolated (K. Shinagawa, p. 181-193, in A. E. Pohland et al., ed., Microbial Toxins in Foods and Feeds, 1990) from the same B. cereus strain, but no report of cloning of the enterotoxin gene has been published. In the present study, a specific antibody to the purified enterotoxin was produced and used to screen the genomic library of B. cereus FM1 made with the lambda gt11 vector. An immunologically positive clone was found to contain the full protein-coding region and some 5' and 3' flanking regions. The deduced amino acid sequence of the cloned gene indicated that the protein is rich in beta structures and contains some unusual sequences, such as consecutive Asn residues. In order to clone enterotoxin genes from Bacillus thuringiensis, two PCR primers were synthesized based on the nucleotide sequence of the B. cereus gene. These primers were designed to amplify the full protein-coding region. PCR conducted with DNA preparations from the B. thuringiensis subsp. sotto and B. thuringiensis subsp. israelensis strains successfully amplified a segment of DNA with a size almost identical to that of the protein-coding region of the B. cereus enterotoxin. Nucleotide sequences of the amplified DNA segments showed that these B. thuringiensis strains contain an enterotoxin gene very similar to that of B. cereus. Further PCR screening of additional B. thuringiensis strains with four primer pairs in one reaction revealed that some additional B. thuringiensis strains contain enterotoxin-like genes.

Amino Acid Sequence↗
PubMed1998

Variable cross-resistance to Cry11B from Bacillus thuringiensis subsp. jegathesan in Culex quinquefasciatus (Diptera: Culicidae) resistant to single or multiple toxins of Bacillus thuringiensis subsp. israelensis.

A novel mosquitocidal bacterium, Bacillus thuringiensis subsp. jegathesan, and one of its toxins, Cry11B, in a recombinant B. thuringiensis strain were evaluated for cross-resistance with strains of the mosquito Culex quinquefasciatus that are resistant to single and multiple toxins of Bacillus thuringiensis subsp. israelensis. The levels of cross-resistance (resistance ratios [RR]) at concentrations which caused 95% mortality (LC95) between B. thuringiensis subsp. jegathesan and the different B. thuringiensis subsp. israelensis-resistant mosquito strains were low, ranging from 2.3 to 5.1. However, the levels of cross-resistance to Cry11B were much higher and were directly related to the complexity of the B. thuringiensis subsp. israelensis Cry toxin mixtures used to select the resistant mosquito strains. The LC95 RR obtained with the mosquito strains were as follows: 53.1 against Cq4D, which was resistant to Cry11A; 80.7 against Cq4AB, which was resistant to Cry4A plus Cry4B; and 347 against Cq4ABD, which was resistant to Cry4A plus Cry4B plus Cry11A. Combining Cyt1A with Cry11B at a 1:3 ratio had little effect on suppressing Cry11A resistance in Cq4D but resulted in synergism factors of 4.8 and 11.2 against strains Cq4AB and Cq4ABD, respectively; this procedure eliminated cross-resistance in the former mosquito strain and reduced it markedly in the latter strain. The high levels of activity of B. thuringiensis subsp. jegathesan and B. thuringiensis subsp. israelensis, both of which contain a complex mixture of Cry and Cyt proteins, against Cry4- and Cry11-resistant mosquitoes suggest that novel bacterial strains with multiple Cry and Cyt proteins may be useful in managing resistance to bacterial insecticides in mosquito populations.

Animals↗
PubMed2000

Introduction of raw starch-binding domains into Bacillus subtilis alpha-amylase by fusion with the starch-binding domain of Bacillus cyclomaltodextrin glucanotransferase.

We constructed two types of chimeric enzymes, Ch1 Amy and Ch2 Amy. Ch1 Amy consisted of a catalytic domain of Bacillus subtilis X-23 alpha-amylase (Ba-S) and the raw starch-binding domain (domain E) of Bacillus A2-5a cyclomaltodextrin glucanotransferase (A2-5a CGT). Ch2 Amy consisted of Ba-S and D (function unknown) plus E domains of A2-5a CGT. Ch1 Amy acquired raw starch-binding and -digesting abilities which were not present in the catalytic part (Ba-S). Furthermore, the specific activity of Ch1 Amy was almost identical when enzyme activity was evaluated on a molar basis. Although Ch2 Amy exhibited even higher raw starch-binding and -digesting abilities than Ch1 Amy, the specific activity was lower than that of Ba-S. We did not detect any differences in other enzymatic characteristics (amylolytic pattern, transglycosylation ability, effects of pH, and temperature on stability and activity) among Ba-S, Ch1 Amy, and Ch2 Amy.

Amino Acid Sequence↗