Language：English   Publishing type：Research paper (scientific journal)   Publisher：MDPI AG  

Ion channel proteins play important roles in various cell functions, making them attractive drug targets. Artificial lipid bilayer recording is a technique used to measure the ion transport activities of channel proteins with high sensitivity and accuracy. However, the measurement efficiency is low. In order to improve the efficiency, we developed a method that allows us to form bilayers on a hydrogel bead and record channel currents promptly. We tested our system by measuring the activities of various types of channels, including gramicidin, alamethicin, α-hemolysin, a voltage-dependent anion channel 1 (VDAC1), a voltage- and calcium-activated large conductance potassium channel (BK channel), and a potassium channel from Streptomyces lividans (KcsA channel). We confirmed the ability for enhanced measurement efficiency and measurement system miniaturizion.

DOI： 10.3390/mi11121070

PubMed

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Authorship：Lead author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

Cry46Ab from Bacillus thuringiensis TK-E6 is a new mosquitocidal toxin with an aerolysin-type architecture, and it is expected to be used as a novel bioinsecticide. Cry46Ab acts as a functional pore-forming toxin, and characteristics of the resulting channel pores, including ion selectivity, have been analyzed. However, the relationship between channel-pore ion selectivity and insecticidal activity remains to be elucidated. To clarify the effects of charged amino acid residues on the ion permeability of channel-pores and the resulting insecticidal activity, in the present study, we constructed Cry46Ab mutants in which a charged amino acid residue within a putative transmembrane β-hairpin region was replaced with an oppositely charged residue. Bioassays using Culex pipiens mosquito larvae revealed that the mosquitocidal activity was altered by the mutation. A K155E Cry46Ab mutant exhibited toxicity apparently higher than that of wild-type Cry46Ab, but the E159K and E163K mutants exhibited decreased toxicity. Ions selectivity measurements demonstrated that the channel pores formed by both wild-type and mutant Cry46Abs were cation selective, and their cation preference was also similar. However, the degree of cation selectivity was apparently higher in channel pores formed by the K155E mutant, and reduced selectivity was observed with the E159K and E163K mutants. Our data suggest that channel-pore cation selectivity is a major determinant of Cry46Ab mosquitocidal activity and that cation selectivity can be controlled via mutagenesis targeting the transmembrane β-hairpin region. KEY POINTS: • Cry46Ab mutants were constructed by targeting the putative transmembrane β-hairpin region. • Charged residues within the β-hairpin control the flux of ions through channel pores. • Channel-pore cation selectivity is correlated with insecticidal activity.

DOI： 10.1007/s00253-020-10893-5

PubMed

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Other Link： https://link.springer.com/article/10.1007/s00253-020-10893-5/fulltext.html

Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

Cry46Ab from Bacillus thuringiensis TK-E6 is a new mosquitocidal toxin with aerolysin-type architecture, and has been shown that co-administration of Cry46Ab with other mosquitocidal Cry toxins results in synergistic toxicity against Culex pipiens Coquillett (Diptera: Culicidae) mosquito larvae. Cry46Ab, therefore, is expected to find use in improving the insecticidal activity of B. thuringiensis-based bioinsecticides. In the present study, the mode of action of Cry46Ab was explored by single-channel measurements of Cry46Ab channel-pores. The single-channel conductances of channel-pores formed in planar lipid bilayers by Cry46Ab were determined to be 31.8 +/- 2.7 pS in 150 mM NaCl and 24.2 +/- 0.7 pS in 150 mM CaCl2. Ion-selectivity measurements revealed that the channel-pores formed by Cry46Ab were cation selective. The permeability ratio of K+ to Cl-was approximately 4, and the preferences for cations were K+ > Na+, K+ > Ca2+, and Ca2+ > Na+. A calcein release assay using liposomes suggested that Cry46Ab influences the integrity of membrane vesicles. Formation of cation-selective channel-pores has been observed with other insecticidal Cry toxins that have structures distinct from those of Cry46Ab; the capability of forming such pores may be a property required of insecticidal toxins.

DOI： 10.1007/s13355-019-00635-z

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Other Link： http://link.springer.com/article/10.1007/s13355-019-00635-z/fulltext.html

Language：English  

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Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

DOI： 10.1007/s13355-017-0529-5

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Other Link： http://link.springer.com/content/pdf/10.1007/s13355-017-0529-5.pdf

Authorship：Lead author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

DOI： 10.1016/j.ibmb.2017.06.015

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Authorship：Lead author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

DOI： 10.1007/s13355-016-0454-z

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Other Link： http://link.springer.com/article/10.1007/s13355-016-0454-z/fulltext.html

Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

DOI： 10.1016/j.jbiosc.2013.12.004

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Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

DOI： 10.1007/s00284-013-0301-1

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Other Link： http://link.springer.com/article/10.1007/s00284-013-0301-1/fulltext.html

Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

DOI： 10.1016/j.pep.2013.01.011

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Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

DOI： 10.1007/s00253-011-3216-4

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Other Link： http://link.springer.com/article/10.1007/s00253-011-3216-4/fulltext.html

Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Wiley  

DOI： 10.1111/j.1742-4658.2010.07704.x

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：American Society for Microbiology  

<title>ABSTRACT</title>

Cry4Aa produced by
<italic>Bacillus thuringiensis</italic>
is a dipteran-specific toxin and is of great interest for developing a bioinsecticide to control mosquitoes. Therefore, it is very important to characterize the functional motif of Cry4Aa that is responsible for its mosquitocidal activity. In this study, to characterize a potential receptor binding site, namely, loops 1, 2, and 3 in domain II, we constructed a series of Cry4Aa mutants in which a residue in these three loops was replaced with alanine. A bioassay using
<italic>Culex pipiens</italic>
larvae revealed that replacement of some residues affected the mosquitocidal activity of Cry4Aa, but the effect was limited. This finding was partially inconsistent with previous results which suggested that replacement of the Cry4Aa loop 2 results in a significant loss of mosquitocidal activity. Therefore, we constructed additional mutants in which multiple (five or six) residues in loop 2 were replaced with alanine. Although the replacement of multiple residues also resulted in some decrease in mosquitocidal activity, the mutants still showed relatively high activity. Since the insecticidal spectrum of Cry4Aa is specific, Cry4Aa must have a specific receptor on the surface of the target tissue, and loss of binding to the receptor should result in a complete loss of mosquitocidal activity. Our results suggested that, unlike the receptor binding site of the well-characterized molecule Cry1, the receptor binding site of Cry4Aa is different from loops 1, 2, and 3 or that there are multiple binding sites that work cooperatively for receptor binding.

DOI： 10.1128/aem.02175-09

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Authorship：Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

DOI： 10.1016/j.jbiosc.2009.03.016

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Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

DOI： 10.1007/s00253-008-1560-9

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Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

DOI： 10.1007/s00284-006-0351-8

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

Plutella xylostella strain resistant (PXR) to Bacillus thuringiensis Cry1Ac toxin was not killed at even more than 1000 microg Cry1Ac/g diet but killed by Cry1Ab at 0.5 microg/g diet. In contrast, susceptible strain (PXS) was killed by Cry1Ac at 1 microg/g diet. Cy3-labeld Cry1A(s) binding to brush border membrane vesicles (BBMV) prepared from both strains were analyzed with direct binding assay. The Kd value of Cry1Aa to both BBMV was almost identical: 213.2 and 205.8 nM, and 263.5 and 265.0 nM for Cry1Ac. The highest Kd values were in Cry1Ab which showed most effective insecticidal activity in PXS and PXR, 2126 and 2463 nM, respectively. These results clearly showed that the BBMV from PXR and PXS could equally bind to Cry1Ac. The binding between BBMV and Cy3-labeled Cry1Ac was inhibited only by anti-175 kDa cadherin-like protein (CadLP) and -252 kDa protein antisera, but not by anti-120 kDa aminopeptidase. This supports that resistance in PXR resulted from the abortion of pore formation after the binding of Cry1Ac to the BBMV. And furthermore, the importance of 175K CadLP and P252 proteins in those bindings was suggested. We briefly discuss possible mechanisms of the resistance.

DOI： 10.1016/j.cbpb.2007.04.013

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

DOI： 10.1263/jbb.103.381

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

DOI： 10.1016/j.pestbp.2006.01.011

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

DOI： 10.1016/j.cbpb.2006.04.013

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Wiley  

DOI： 10.1111/j.1439-0434.2006.01076.x

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Oxford University Press (OUP)  

Proteins in the brush border membrane (BBM) of the midgut binding to the insecticidal Cry1Ac toxin from Bacillus thuringiensis were investigated to examine the lower sensitivity of Bombyx mori to Cry1Ac, and new aminopeptidase N that bound to Cry1Ac was discovered. DEAE chromatography of Triton X-100-soluble BBM proteins from the midgut revealed 96-kDa aminopeptidase that bound to Cry1Ac. The enzyme was purified to homogeneity and estimated to be a 96.4-kDa molecule on a silver-stained SDS-PAGE gel. However, the native protein was eluted as a single peak corresponding to approximately 190-kDa on gel filtration and gave a single band on native PAGE. The enzyme was determined to be an aminopeptidase N (APN96) from its substrate specificity. Antiserum to class 3 B. mori APN (BmAPN3) recognized APN96, but peptide mass fingerprinting revealed that 54% of the amino acids of matched peptides were identical to those of BmAPN3, suggesting that APN96 was a novel isoform of the APN3 family. On ligand blots, APN96 bound to Cry1Ac but not Cry1Aa or Cry1Ab, and the interaction was inhibited by GalNAc. K(D) of the APN96-Cry1Ac interaction was determined to be 1.83 +/- 0.95 microM. The lectin binding assay suggested that APN96 had an N-linked bi-antennal oligosaccharide or an O-linked mucin type one. The role of APN96 was discussed in relation to the insensitivity of B. mori to Cry1Ac.

DOI： 10.1093/jb/mvj024

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

DOI： 10.1016/j.pestbp.2005.02.001

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Japanese Society of Applied Entomology & Zoology  

DOI： 10.1303/aez.2005.125

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Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Wiley  

DOI： 10.1016/j.febslet.2004.09.029

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：American Society for Microbiology  

<title>ABSTRACT</title>

We describe the properties of a novel 252-kDa protein (P252) isolated from brush border membranes of
<italic>Bombyx mori</italic>
. P252 was found in a Triton X-100-soluble brush border membrane vesicle fraction, suggesting that it may be a component of the midgut epithelial cell membrane. P252 was purified to homogeneity, and the amino acid sequence of two internal peptides was determined, but neither of the peptides matched protein sequences in the available databases. The apparent molecular mass of the purified protein was estimated by denaturing gel electrophoresis to be 252 kDa, and it migrated as a single band on native gels. However, gel filtration chromatography indicated an apparent mass of 985 kDa, suggesting that P252 may exist as a homo-oligomer. The associations of P252 with Cry1Aa, Cry1Ab, and Cry1Ac were specific, and
<italic>
K
_d
</italic>
constants were determined to be 28.9, 178.5, and 20.0 nM, respectively. A heterologous competition assay was also done. P252 did not exhibit Leu-pNA hydrolysis activity, and binding to the Cry1A toxins was not inhibited by GalNAc. Binding assays of P252 with various lectins indicated the presence of three antennal N-linked high-mannose-type as well as O-linked mucin-type sugar side chains. While the function of P252 is not yet clear, we propose that it may function with Cry1A toxins during the insecticidal response and/or Cry toxin resistance mechanism.

DOI： 10.1128/aem.70.8.4604-4612.2004

PubMed

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Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Informa UK Limited  

DOI： 10.1080/0958315031000151710

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Japanese Society for Plant Cell and Molecular Biology  

DOI： 10.5511/plantbiotechnology.20.215

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Publisher：The Japanese Society of Sericultural Science  

CHAPS-soluble proteins from BBMV of Plutella xylostella which were highly resistant and susceptible to Cry1Ac of Bacillus thuringiensis were used to determine the capability of binding with Cry1A toxins. Both ligand and western blot analyses with the proteins and Cry1A toxins showed that major three 120, 110 and 100 kDa proteins bound with Cry1Aa and Ac, but not with Cry1Ab. Furthermore, the proteins were positive with anti aminopeptidase N antibody and the intensity and pattern of the binding were almost the same, respectively in the both straihs. Cry1Aa and Ac were shown to bind with the proteins at about 0.7 ng toxin/mm² membrane/10 min in both the strains using plasmon resonance. Their binding curves were almost the same each other. Cry1Ab, however, was not shown to bind with the BBMV proteins in both the strains.

DOI： 10.11416/jsss.jsss72.0.66.0

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Publisher：The Japanese Society of Sericultural Science  

A hundred twenty kDa aminopeptidase N (APN120) from Bombyx mori BBM has been thought to be a candidate for the receptor of Bacillus thuringiensis Cry1Aa and Cry1Ac toxins. Ligand blot analysis showed that Cry1Aa and Cry1Ac bound to not only APN120 but also APN110 and APN100. Along with these APN proteins, we found 90 kDa APN like protein (APN90) having significant APN activity but negative to anti APN120 antibody. The APN was purified with DEAE Sepharose and Sephacryl S300 chromatography and at least seven APN-like proteins were found. In ligand blot analysis, APN90 was shown to specifically bind to Cry1Ac but neither Cry1Aa nor Cry1Ab. Here we present interesting and novel properties of purified APN90 and we also briefly discuss the role of it.

DOI： 10.11416/jsss.jsss72.0.64.0

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

DOI： 10.1007/s007050170101

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Other Link： http://link.springer.com/article/10.1007/s007050170101/fulltext.html

Language：English   Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

DOI： 10.1006/viro.2000.0530

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Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

DOI： 10.1016/s0168-1702(99)00129-x

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Japanese Society of Applied Entomology & Zoology  

DOI： 10.1303/aez.2000.45

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Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Japanese Society of Applied Entomology & Zoology  

DOI： 10.1303/aez.2000.163

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

DOI： 10.1016/s0168-1702(99)00097-0

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Authorship：Lead author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

DOI： 10.1006/viro.1999.9894

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

DOI： 10.1023/a:1007972108026

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Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

DOI： 10.1007/s007050050085

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Other Link： http://link.springer.com/article/10.1007/s007050050085/fulltext.html

Language：Japanese   Publisher：The Japanese Society of Sericultural Science  

The five viruses, Bombyx mori densonucleosis virus type 1 (BmDNV-1), -type 2 (BmDNV-2), Bombyx mori nuclear polyhedrosis virus (BmDPV), Bombyx mori cytoplasmic polyhedrosis virus (BmCPV), and Infectious flacherie virus (IFV), are the agents causing fetal disease of the silkworm. The aim of this study is to establish a simple and highly sensitive PCR system for detection of all the viruses. A combination of the RT-PCR and the nested PCR was found to be effective to amplify DNA and/or RNA virus genome sequences in a reaction maintaining high sensitivity and specificity. In this report, the primer design and the condition of the PCR for the detection of all the viruses are described.

DOI： 10.11416/kontyushigen1930.66.477

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Microbiology Society  

DOI： 10.1099/0022-1317-77-3-555

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Springer Science and Business Media LLC  

DOI： 10.1007/bf01315423

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Japanese Society of Applied Entomology & Zoology  

DOI： 10.1303/aez.29.442

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Authorship：Lead author,　Corresponding author   Language：Japanese   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)   Publisher：社団法人 日本蚕糸学会  

DOI： 10.11416/konchubiotec.77.3_205

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Language：Japanese   Publishing type：Rapid communication, short report, research note, etc. (bulletin of university, research institution)   Publisher：Niigata University  

Aminopeptidase N(APN) localizing on the apical membrane of midgut epithelial cells is one of the plausible candidate of the receptor proteins for Bacillus thuringiensis Cry1Aa toxin which specifically kills lepidopteran insects. However, comprehensive evidences to address above possibility have not been established yet. We tried to express the APN1, BmAPN1, onto plasma membrane of cultured insect cells to investigate the interaction with Cry1Aa. Gene expression system was constructed with High five cultured insect cells and baculovirus expression system. On 48 h after the infection of the cells with gene modified baculovirus, 110 kDa BmAPN1 was expressed on the cell membranes. Aminopeptidase activity was ten times higher than that of non-infected cultured cells. The recombinant BmAPN1 was the same size as native one localizing on the brush border membrane of midgut epithelial cells. The transformed cells expressing BmAPN1 is a good system for the investigation of interaction between APN and Cry1Aa toxin.

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Other Link： http://hdl.handle.net/10191/5041

Language：Japanese   Publishing type：Rapid communication, short report, research note, etc. (bulletin of university, research institution)   Publisher：Niigata University  

Wasted sludge from a bean curd factory was mixed with newspaper chips cut (12 mm ×3 mm) and aerated right after the placement of the mixture into a fermenter. The sludge was mixed with newspaper chips at 15% (w/w) and composted under continuous aeration at 80 L/min/m2 bottom area of the fermenter. Hereafter we called the compost as paper-compost. The resulted paper-compost showed no inhibitory effect in germination of the komatsuna, Brassica nappas seeds and increased thereafter growth of them. On the other hand, the application of chemical fertilizer at the same amount of nitrogen content as that of paper-compost showed almost no growth of the plantlets. Generally, polyaluminum chlorides were added to the wasted water in active sludge sewer system to coagulate the excess amount of sludge, therefore, there is a possibility that the Al to remain after even the completion of composting, then the aluminum contents in the compost was evaluated with an atomic absorption spectrophotometer. The content in the compost was 160 mg/kg compost dried. On the other hand, the aluminum contents in wasted sludge and newspaper which were used to make the compost were 110 and 150 mg/kg, respectively. Thus, the aluminum in the composts was thought to be derived from those newspapers and active sludge. At least, polyaluminum chloride used to coagulate the excess sludge was not seemed to remain in the compost.

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Other Link： http://agriknowledge.affrc.go.jp/RN/2010742738

Language：English   Publishing type：Rapid communication, short report, research note, etc. (bulletin of university, research institution)   Publisher：Niigata University  

Our previous study using liquid organ cultured adventitious roots from turnip (Brassica rapa L.) showed that Ca2+ is required for induction of defense responses in the cultured roots on the treatment with Plasmodiophora brassicae resting spores (Takahashi et al., 2006). To evaluate change in [Ca2+]cyt in cultured root cells on contact with the spores, acetoxymethyl ester derivative of Fura-2 (Fura-2/AM) was loaded into the roots. When ionophore A23187 was treated with Ca2+ simultaneously, the Fura-2 fluorescence ratio that represents relative [Ca2+]cyt increased promptly, showing that the Fura-2/AM system is suitable to evaluate [Ca2+]cyt change in cultured root cells in a second range. Applicability of this method for studies on Ca2+ fluctuation against various extracellular stimuli was supported by observations that treatment with mannitol or NaCl also immediately increased the Fura-2 ratio. When the Fura-2/AM loaded roots were treated with resting spores, no [Ca2+]cyt change was observed during 500 second but when treated with spores pre-incubated with germination-enhancing suspension (GES), a slight but reproducible increase in [Ca2+]cyt was observed. We conclude that although further analysis is needed, the Fura-2/AM system will contribute to revealing the Ca2+ involvement in clubroot-resistance response.

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Other Link： http://agriknowledge.affrc.go.jp/RN/2010742740

Authorship：Lead author   Language：English   Publishing type：Article, review, commentary, editorial, etc. (international conference proceedings)  

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Language：English   Publishing type：Article, review, commentary, editorial, etc. (international conference proceedings)  

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Language：English   Publishing type：Rapid communication, short report, research note, etc. (bulletin of university, research institution)   Publisher：Niigata University  

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Other Link： http://agriknowledge.affrc.go.jp/RN/2010711999

Language：English   Publishing type：Article, review, commentary, editorial, etc. (international conference proceedings)  

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Language：English   Publishing type：Article, review, commentary, editorial, etc. (international conference proceedings)  

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Language：English   Publishing type：Article, review, commentary, editorial, etc. (international conference proceedings)  

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Language：English   Publishing type：Article, review, commentary, editorial, etc. (international conference proceedings)  

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Authorship：Lead author   Language：English   Publishing type：Article, review, commentary, editorial, etc. (international conference proceedings)  

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Language：English   Publishing type：Rapid communication, short report, research note, etc. (bulletin of university, research institution)  

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Language：English   Publishing type：Rapid communication, short report, research note, etc. (bulletin of university, research institution)  

CiNii Article

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Language：Japanese   Publishing type：Rapid communication, short report, research note, etc. (bulletin of university, research institution)   Publisher：Niigata University  

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Authorship：Lead author   Language：English   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)   Publisher：ACADEMIC PRESS INC  

DOI： 10.1006/viro.2000.0668

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Language：English   Publishing type：Article, review, commentary, editorial, etc. (scientific journal)  

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Language：English   Publishing type：Book review, literature introduction, etc.  

Abstract Since the first report of Bacillus sotto by Ishiwata in 1901, thousands of related papers about Bacillus thuringiensis have been documented. In the field of biocontrol of insect pests by this bacterium, after the initial discovery of several B. thuringiensis isolates specific for lepidopteran insects, the isolation of B. thuringiensis israelensis, specific to dipteran larvae by Goldberg and Margalit, and B. thuringiensis tenebrionis, specific to some group of coleopteran insects by Krieg et al. were epoch making advances. In 1992, Ohba et al. isolated B. thuringiensis ja ponensis strain Buibui, which was specific to only scarabaeid larvae. This isolate is the main target of our discussion in this review. These discoveries by which not only B. thuringiensis sciences, but also applied biological control strategies have been enriched, which inspirit us to screen novel isolates. On the other hand, the fields of molecular biology and biochemistry studies on the structural elucidation of toxin proteins and mechanism of action have also tremendously progressed. But the complete mechanism has yet to be solved. For instance, interaction between receptor proteins locating on the plasma membrane of insect midgut epithelial cells and insecticidal proteins has not been fully sketched- In a way, this field is still in chaos. Addressing these exciting and enigmatic subjects will eventually lead to the construction of sustainable agriculture in the 21st century. © 2017 Wiley. All rights reserved.

DOI： 10.1111/j.1744-7917.2000.tb00235.x

Scopus

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Event date： 2019.12.3 - 2019.12.6

Language：Japanese   Presentation type：Poster presentation  

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Event date： 2019.12.3 - 2019.12.6

Language：Japanese   Presentation type：Poster presentation  

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Event date： 2019.3.25 - 2019.3.27

Language：Japanese   Presentation type：Oral presentation (general)  

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