Parasporal Body Formation via Overexpression of the Cry10Aa Toxin of Bacillus thuringiensis subsp. israelensis , and Cry10Aa-Cyt1Aa Synergism

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Parasporal body formation via overexpression of the Cry10Aa toxin of Bacillus thuringiensis subsp. israelensis, and Cry10Aa-Cyt1Aa synergism.

Bacillus thuringiensis subsp. israelensis is the most widely used microbial control agent against mosquitoes and blackflies. Its insecticidal success is based on an arsenal of toxins, such as Cry4A, Cry4B, Cry11A, and Cyt1A, harbored in the parasporal crystal of the bacterium. A fifth toxin, Cry10Aa, is synthesized at very low levels; previous attempts to clone and express Cry10Aa were limited,...

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Antibacterial activity of Cyt1Aa from Bacillus thuringiensis subsp. israelensis.

Cyt1Aa is a delta-endotoxin protein that is produced by Bacillus thuringiensis subsp. israelensis. It is a membrane pore-forming toxin that is lethal to insect larvae and is broadly cytolytic to vertebrate as well as invertebrate cells. Cyt1Aa is produced as a protoxin of 27 kDa. Proteolytic activation results in a reduction of the molecular mass to approximately 23-24 kDa and a threefold incre...

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

Bacillus thuringiensis subsp. israelensis produces crystal proteins, Cry (4Aa, 4Ba, 10Aa, and 11Aa) and Cyt (1Aa and 2Ba) proteins, toxic to mosquito vectors of human diseases. Cyt1Aa overcomes insect resistance to Cry11Aa and Cry4 toxins and synergizes the toxicity of these toxins. However, the molecular mechanism of synergism remains unsolved. Here, we provide evidence that Cyt1Aa functions a...

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Characterization of the parasporal inclusion of Bacillus thuringiensis subsp. kyushuensis.

Electron microscopy of Bacillus thuringiensis subsp. kyushuensis revealed that the parasporal inclusions are composed of a homogeneous center surrounded by a thick, electron-dense coating. Antibodies directed against the 135- and 65-kilodalton B. thuringiensis subsp. israelensis peptides cross-reacted with the 70- and 26-kilodalton peptides, respectively, of B. thuringiensis subsp. kyushuensis.

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Complete sequence and organization of pBtoxis, the toxin-coding plasmid of Bacillus thuringiensis subsp. israelensis.

The entire 127,923-bp sequence of the toxin-encoding plasmid pBtoxis from Bacillus thuringiensis subsp. israelensis is presented and analyzed. In addition to the four known Cry and two known Cyt toxins, a third Cyt-type sequence was found with an additional C-terminal domain previously unseen in such proteins. Many plasmid-encoded genes could be involved in several functions other than toxin pr...

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ژورنال

عنوان ژورنال: Applied and Environmental Microbiology

سال: 2009

ISSN: 0099-2240,1098-5336

DOI: 10.1128/aem.00409-09