Molecular Mechanism for the Insecticidal Activity of Bacillus Thuringiensis

Award Information
Agency:
Department of Agriculture
Branch
n/a
Amount:
$50,000.00
Award Year:
1996
Program:
SBIR
Phase:
Phase I
Contract:
n/a
Award Id:
34396
Agency Tracking Number:
34396
Solicitation Year:
n/a
Solicitation Topic Code:
n/a
Solicitation Number:
n/a
Small Business Information
2005 Cabot Blvd., West, Langhorne, PA, 19047
Hubzone Owned:
N
Minority Owned:
N
Woman Owned:
N
Duns:
n/a
Principal Investigator:
Dr. William P. Donovan
Principal Investigator
() -
Business Contact:
() -
Research Institute:
n/a
Abstract
Bacillus thuringiensis crystal proteins are highly toxic to certain species of lepidopteran insects but are much less toxic to other lepidoteran species and usually have significantly lower toxicity to non-lepidopteran species. In addition, some lepidopteran species that initially were susceptible to Bacillus thuringiensis have developed resistance. Understanding the molecular mechanism for the insecticidal activity of Bacillus thuringiensis crystal proteins represents a significant area of research accomplishment. One rationale for this research is that such understanding will assist efforts to improve the toxicity of crystal proteins through protein engineering. Protein engineering efforts have been aided by two important findings on the mechanism of toxicity of crystal proteins. Briefly stated these findings are 1) Bacillus thuringiensis crystal proteins bind to cells lining the insect midgut; 2) Bound proteins form pores causing colloid osmotic lysis of the insect gut cells. It is presumed that lysis of gut cells results in insect death. This proposal will explore promising avenues of research which will add to the understanding of the mechanism of toxicity of Bacillus thuringiensis crystal proteins.

* information listed above is at the time of submission.

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