Title |
Bacillus thuringiensis subsp. kurstaki HD1 as a factory to synthesize alkali-labile ChiA74∆sp chitinase inclusions, Cry crystals and spores for applied use
|
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Published in |
Microbial Cell Factories, January 2014
|
DOI | 10.1186/1475-2859-13-15 |
Pubmed ID | |
Authors |
José Eleazar Barboza-Corona, Jorge Luis Delgadillo-Ángeles, José Cristóbal Castañeda-Ramírez, Uriel Eleazar Barboza-Pérez, Luz Edith Casados-Vázquez, Dennis K Bideshi, Ma Cristina del Rincón-Castro |
Abstract |
The endochitinase ChiA74 is a soluble secreted enzyme produced by Bacillus thuringiensis that synergizes the entomotoxigenecity of Cry proteins that accumulate as intracellular crystalline inclusion during sporulation. The purpose of this study was to produce alkaline-soluble ChiA74∆sp inclusions in B. thuringiensis, and to determine its effect on Cry crystal production, sporulation and toxicity to an important agronomical insect, Manduca sexta. To this end we deleted the secretion signal peptide-coding sequence of chiA74 (i.e. chiA74∆sp) and expressed it under its native promoter (pEHchiA74∆sp) or strong chimeric sporulation-dependent cytA-p/STAB-SD promoter (pEBchiA74∆sp) in Escherichia coli, acrystalliferous B. thuringiensis (4Q7) and B. thuringiensis HD1. |
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Student > Bachelor | 3 | 7% |
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Unknown | 6 | 13% |
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