• Title/Summary/Keyword: Mosquitocidal

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Expression of Mosquitocidal Bacillus sphaericus Binary Toxin and B. thuringiensis cry11B Genes in B. thuringiensis 407

  • Park, Hyun-Woo
    • International Journal of Industrial Entomology and Biomaterials
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    • v.2 no.2
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    • pp.185-189
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    • 2001
  • Wild type Bacilus thuringiensis subsp. israelensis and B. sphaericus toxins have been used separately as active in ingredients for bacterial insecticides to control mosquito larvae due to their comparable toxicity to chemical insecticides. Cry11B, recently cloned from B. thuringiensis subsp. jegathesan, shows higher toxicity against three major species of mosquito larvae than Cry11A, one of the major component of B. thuringiensis subsp. israelensis inclusion body. To determine whether the combination of cry11B and B. sphaericus binary toxins is as toxic as B. thuringiensis subsp. israelensis parental strain, cry11B and B. sphaericus binary toxins genes were co-expressed as an operon using cytlA promoters/STAB-SD hybrid expression system in B. thuringiensis subsp. israelensis acrystalliferous strain 4Q7. However, unexpectedly, B. sphaericus binary toxins were barely produced, whereas relatively large amount of Cry11B was produced. When this strain was grown in four different media, NB+G and Peptonized Milk produced more toxin proteins and spores per unit of media than GYS and G-Tris. Toxicity of this strain against fourth instar Culex quinquefasciatus was ranged from of 8.3 to 45.7 ng/ml, with NB+G culture being the highest, and GYS culture was the lowest.

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Stability on Chemical Treatment of Niosquitocidal delta-endotoxin from Bacillus thuringiensis subsp. darmstadiensis 73E10-2 (모기유충에 살충력이 있는 Bacillus thuringiensis subsp. darmstadiensis 73E10-2의 delta-endotoxin의 화학적 처치에 따른 안정성)

  • 김광현;조경순;이광배
    • Microbiology and Biotechnology Letters
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    • v.19 no.3
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    • pp.308-312
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    • 1991
  • The delta-endotoxin from B. thuringiensis subsp. damstadienszs 73E10-2 was resistant to high concentration of salt (4M NaBr), organic solvents (50% acetone), denaturants (4 M urea), and neutral detergents (10% triton X-100). In contrast, the toxin was inactivated by treating with charged detergents as well as guanidine hydrochloride or carbon tetra-chloride. The delta-endotoxin is not a sulfhydryl activated toxin, but modification of the lysine side chains eliminated toxicity against mosquito larvae.

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Construction of shuttle vectors expressing the cry11Aa gene and their mosquitocidal activity (모기살충성 cry11Aa 유전자를 발현하는 벡터의 구축과 모기살충효과)

  • Lee, Dae-Weon;Kim, Ho-San;Je, Yeon-Ho;Kim, Joo-Up;Yu, Hyo-Sok;Kang, Seok-Kwon
    • The Korean Journal of Pesticide Science
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    • v.2 no.1
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    • pp.91-96
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    • 1998
  • For the expression of the cry11Aa gene highly toxic to dipteran insects, we constructed two cyanobacteria-Escherichia coli(E. coli) shuttle vectors, pCYASK5-l and pCYASK5-2. These vectors were transformed into E. coli and selected with kanamycin. The expression of the cry11Aa gene in E. coli was characterized by SDS-polyacrylamide gel electrophoresis and Western blot analysis. Two E. coli transformants harboring pCYASK5-1 and pCYASK5-2 expressed the cry11Aa gene in size of 72 kDa and 64 kDa, respectively and showed over 89% mortality against Culex pipiens larvae.

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Characterization of Bacillus thuringiensis subsp. tohokuensis CAB167 Isolate against Mosquito Larva (모기유충에 활성 있는 Bacillus thuringiensis subsp. tohokuensis CAB167 균주의 특성)

  • Kil, Mi-Ra;Kim, Da-A;Paek, Seung-Kyoung;Kim, Jin-Su;Choi, Su-Yeon;Jin, Da-Yong;Youn, Young-Nam;Hwang, In-Chon;Ohba, Michio;Yu, Yong-Man
    • Korean journal of applied entomology
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    • v.47 no.4
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    • pp.457-465
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    • 2008
  • Eight Bacillus thuringiensis strains activated against mosquito larva were compared their characterization. Spherical-shaped parasporal inclusion of B. thuringiensis subsp. tohokuensis CAB167 was observed by phase-contrast microscopy and scanning electron microscopy. $LC_{50}$ values of B. thuringiensis subsp. tohokuensis CAB167 against Culex pipiens molestus, Culex pipiens pallens, and Aedes aegyti were 173, 190 and 580 ng/ml, respectively. B. thuringiensis subsp. tohokuensis CAB167 had a parasporal inclusion containing 4 major protein components, for example, 135, 80, 49 and 28-kDa by SDS-PAGE. Otherwise, after trypsin digestion of parasporal inclusion, SDS-PAGE was showed new protease-resistant peptides at 72 and 63-kDa. Activated toxins of isolated CAB167 were different from other reference strains on a serological by immuno-diffusion test.