scholarly journals Effect of midgut proteolytic activity on susceptibility of lepidopteran larvae to Bacillus thuringiensis subsp. Kurstaki

2014 ◽  
Vol 4 ◽  
Author(s):  
Reza Talaei-Hassanloui ◽  
Raziyeh Bakhshaei ◽  
Vahid Hosseininaveh ◽  
Ayda Khorramnezhad
Keyword(s):  
Bacillus Thuringiensis ◽  
Proteolytic Activity ◽  
Bacillus Thuringiensis Subsp ◽  
Lepidopteran Larvae

scholarly journals Comparative analysis of the individual protoxin components in P1 crystals of Bacillus thuringiensis subsp. kurstaki isolates NRD-12 and HD-1

1990 ◽  
Vol 269 (2) ◽  
pp. 507-512 ◽  
Author(s):  
L Masson ◽  
G Préfontaine ◽  
L Péloquin ◽  
P C K Lau ◽  
R Brousseau
Keyword(s):  
Bacillus Thuringiensis ◽  
Choristoneura Fumiferana ◽  
Insect Cell Line ◽  
Gene Products ◽  
Bacillus Thuringiensis Subsp ◽  
Independent Verification ◽  
Lepidopteran Larvae ◽  
Bacterium Bacillus ◽  
The Individual

Two commercially important strains (NRD-12 and HD-1) of the entomopathogenic bacterium Bacillus thuringiensis subsp. kurstaki each contain three genes of partially identical sequence coding for three classes of 130-135 kDa protoxins (termed the 4.5, 5.3 and 6.6 protoxins) that display toxicity towards various lepidopteran larvae. These gene products combine to form the intracellular bipyramidal P1 crystal. Each of the genes from both strains was cloned and expressed in Escherichia coli. Analysis of the cloned genes at the restriction-endonuclease level revealed no detectable differences among genes within a particular gene class. The composition of the P1 crystal from both strains was quantitatively analysed by CNBr cleavage of the purified P1 crystal, with the purified recombinant gene products as reference proteins. Independent verification of the presence of high 6.6-protoxin gene product in the P1 crystal was provided by a rapid in vitro lawn cell toxicity assay directed against a Choristoneura fumiferana (CF-1) insect cell line. The results indicate that, although all three gene products are represented within the P1 crystal of either NRD-12 or HD-1, only the contents of the 4.5 and 5.3 protoxins vary between the two crystals, whereas the 6.6 protoxin contents are similar and represent approximately one-third of the P1 crystal in either strain.

Self-transfer and mobilisation capabilities of the pXO2-like plasmid pBT9727 from Bacillus thuringiensis subsp. konkukian 97-27

Plasmid ◽  
2008 ◽  
Vol 59 (2) ◽  
pp. 134-138 ◽  
Author(s):  
Géraldine A. Van der Auwera ◽  
Sophie Timmery ◽  
Jacques Mahillon
Keyword(s):  
Bacillus Thuringiensis ◽  
Bacillus Thuringiensis Subsp

Cytolytic Peptide Fragments of Cyt1Aa from Bacillus thuringiensis subsp. israelensis

2012 ◽  
Vol 65 (2) ◽  
pp. 121-127
Author(s):  
Marina Nisnevitch ◽  
Svetlana Nikonov ◽  
Yeshayahu Nitzan
Keyword(s):  
Bacillus Thuringiensis ◽  
Peptide Fragments ◽  
Bacillus Thuringiensis Subsp

scholarly journals Amino sugars in the glycoprotein toxin from Bacillus thuringiensis subsp. israelensis.

1987 ◽  
Vol 169 (2) ◽  
pp. 796-801 ◽  
Author(s):  
M A Pfannenstiel ◽  
G Muthukumar ◽  
G A Couche ◽  
K W Nickerson
Keyword(s):  
Bacillus Thuringiensis ◽  
Amino Sugars ◽  
Bacillus Thuringiensis Subsp

Cloning of Two New cry Genes from Bacillus thuringiensis subsp. wuhanensis Strain

2000 ◽  
Vol 40 (4) ◽  
pp. 227-232 ◽  
Author(s):  
White-Shang Kuo ◽  
Jong-Huon Lin ◽  
Ching-Chou Tzeng ◽  
Shui-Shang Kao ◽  
Kin-Fu Chak
Keyword(s):  
Bacillus Thuringiensis ◽  
Cry Genes ◽  
Bacillus Thuringiensis Subsp

Purification and characterization of an exochitinase from Bacillus thuringiensis subsp. aizawai and its action against phytopathogenic fungi

2006 ◽  
Vol 52 (7) ◽  
pp. 651-657 ◽  
Author(s):  
Luis Morales de la Vega ◽  
J Eleazar Barboza-Corona ◽  
Maria G Aguilar-Uscanga ◽  
Mario Ramírez-Lepe
Keyword(s):  
Bacillus Thuringiensis ◽  
Sodium Dodecyl ◽  
Sclerotium Rolfsii ◽  
Phytopathogenic Fungi ◽  
Purification And Characterization ◽  
Chitinolytic Enzyme ◽  
Bacillus Thuringiensis Subsp ◽  
Sds Page ◽  
Fusarium Sp

A chitinolytic enzyme from Bacillus thuringiensis subsp. aizawai has been purified and its molecular mass was estimated ca. 66 kDa by sodium dodecyl sulfate – polyacryamide gel electrophoresis (SDS–PAGE). The enzyme was able to hydrolyze chitin to chitobiosides but not carboxymethylcellulose, cellulose, pullulan, and laminarin. Optimal pH and temperature were detected at 6 and 50 °C, respectively. Stability, in the absence of substrate, was observed at temperatures less than 60 °C and pH between 5 and 8. Enzyme activity was significantly inhibited by K+ and EDTA and completely inhibited by Hg2+. Purified chitinase showed lytic activity against cell walls from six phytopathogenic fungi and inhibited the mycelial growth of both Fusarium sp. and Sclerotium rolfsii. The biocontrol efficacy of the enzyme was tested in the protection of bean seeds infested with six phytopathogenic fungi.Key words: chitinase, Bacillus thuringiensis, purification, phytopathogenic fungi.

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