scholarly journals Bacillus thuringiensis subsp. israelensis Cyt1Aa synergizes Cry11Aa toxin by functioning as a membrane-bound receptor

2005 ◽  
Vol 102 (51) ◽  
pp. 18303-18308 ◽  
Author(s):  
C. Perez ◽  
L. E. Fernandez ◽  
J. Sun ◽  
J. L. Folch ◽  
S. S. Gill ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Bacillus Thuringiensis Subsp ◽  
Membrane Bound

scholarly journals Knockout of Two Cry-Binding Aminopeptidase N Isoforms Does Not Change Susceptibility of Aedes aegypti Larvae to Bacillus thuringiensis subsp. israelensis Cry4Ba and Cry11Aa Toxins

Insects ◽  
2021 ◽  
Vol 12 (3) ◽  
pp. 223
Author(s):  
Junxiang Wang ◽  
Xiaozhen Yang ◽  
Huan He ◽  
Jingru Chen ◽  
Yuanyuan Liu ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Reverse Genetics ◽  
Membrane Vesicles ◽  
Molecular Evidence ◽  
Bacillus Thuringiensis Subsp ◽  
Membrane Bound ◽  
Homozygous Strain ◽  
High Binding Affinity ◽  
Single Knockout

The insecticidal Cry4Ba and Cry11Aa crystal proteins from Bacillus thuringiensis subsp. israelensis (Bti) are highly toxic to Ae. aegypti larvae. The glycosylphosphatidylinositol (GPI)-anchored APN was identified as an important membrane-bound receptor for multiple Cry toxins in numerous Lepidoptera, Coleoptera, and Diptera insects. However, there is no direct molecular evidence to link APN of Ae. aegypti to Bti toxicity in vivo. In this study, two Cry4Ba/Cry11Aa-binding Ae. aegypti GPI-APN isoforms (AeAPN1 and AeAPN2) were individually knocked-out using CRISPR/Cas9 mutagenesis, and the AeAPN1/AeAPN2 double-mutant homozygous strain was generated using the reverse genetics approach. ELISA assays showed that the high binding affinity of Cry4Ba and Cry11Aa protoxins to the midgut brush border membrane vesicles (BBMVs) from these APN knockouts was similar to the background from the wild-type (WT) strain. Likewise, the bioassay results showed that neither the single knockout of AeAPN1 or AeAPN2, nor the simultaneous disruption of AeAPN1 and AeAPN2 resulted in significant changes in susceptibility of Ae. aegypti larvae to Cry4Ba and Cry11Aa toxins. Accordingly, our results suggest that AeAPN1 and AeAPN2 may not mediate Bti Cry4Ba and Cry11Aa toxicity in Ae. aegypti larvae as their binding proteins.

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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