The Bacillus thuringiensis delta-endotoxin is a commercially important pesticide which has specific insecticidal activity on a number of insects. Because it is a biodegradable protein and is not toxic to vertebrates and most non-target insects, it has a low environmental impact. Numerous derivatives are available due to the existence of several genes which encode the delta-endotoxin. As a protein, it has many interesting properties making it ideal for intensive biochemical studies. It is expressed in vivo as a crystal and is developmentally expressed only during sporulation. As a protein toxin, it shares certain properties with other protein toxins, but also has unique features which need to be further clarified. Funds are requested to use genetic engineering and protein engineering techniques to localize the domains of the protein which affect insect specificity, bind to tissue culture cells, and cause cytolytic damage. Changes in the toxin amino acid sequence, which will be performed in this project, are aimed at improving the specificity and activity of the toxin toward certain insect crop pests.

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
1R01AI029092-01
Application #
3143783
Study Section
Tropical Medicine and Parasitology Study Section (TMP)
Project Start
1989-07-01
Project End
1992-06-30
Budget Start
1989-07-01
Budget End
1990-06-30
Support Year
1
Fiscal Year
1989
Total Cost
Indirect Cost
Name
Ohio State University
Department
Type
Schools of Arts and Sciences
DUNS #
098987217
City
Columbus
State
OH
Country
United States
Zip Code
43210
Nair, Manoj S; Dean, Donald H (2015) Composition of the Putative Prepore Complex of Bacillus thuringiensis Cry1Ab Toxin. Adv Biol Chem 5:179-188
Zhang, Qi; Hua, Gang; Bayyareddy, Krishnareddy et al. (2013) Analyses of ?-amylase and ?-glucosidase in the malaria vector mosquito, Anopheles gambiae, as receptors of Cry11Ba toxin of Bacillus thuringiensis subsp. jegathesan. Insect Biochem Mol Biol 43:907-15
Hua, Gang; Zhang, Qi; Zhang, Rui et al. (2013) AgCad2 cadherin in Anopheles gambiae larvae is a putative receptor of Cry11Ba toxin of Bacillus thuringiensis subsp. jegathesan. Insect Biochem Mol Biol 43:153-61
Bayyareddy, Krishnareddy; Zhu, Xiang; Orlando, Ron et al. (2012) Proteome analysis of Cry4Ba toxin-interacting Aedes aegypti lipid rafts using geLC-MS/MS. J Proteome Res 11:5843-55
McNeil, Betina C; Dean, Donald H (2011) Bacillus thuringiensis Cry2Ab is active on Anopheles mosquitoes: single D block exchanges reveal critical residues involved in activity. FEMS Microbiol Lett 325:16-21
Alzate, Oscar; Osorio, Cristina; Florez, Alvaro M et al. (2010) Participation of valine 171 in alpha-Helix 5 of Bacillus thuringiensis Cry1Ab delta-endotoxin in translocation of toxin into Lymantria dispar midgut membranes. Appl Environ Microbiol 76:7878-80
Zhang, Rui; Hua, Gang; Urbauer, Jeffrey L et al. (2010) Synergistic and inhibitory effects of aminopeptidase peptides on Bacillus thuringiensis Cry11Ba toxicity in the mosquito Anopheles gambiae. Biochemistry 49:8512-9
Bayyareddy, Krishnareddy; Andacht, Tracy M; Abdullah, Mohd Amir et al. (2009) Proteomic identification of Bacillus thuringiensis subsp. israelensis toxin Cry4Ba binding proteins in midgut membranes from Aedes (Stegomyia) aegypti Linnaeus (Diptera, Culicidae) larvae. Insect Biochem Mol Biol 39:279-86
Roh, Jong Yul; Nair, Manoj S; Liu, Xinyan Sylvia et al. (2009) Mutagenic analysis of putative domain II and surface residues in mosquitocidal Bacillus thuringiensis Cry19Aa toxin. FEMS Microbiol Lett 295:156-63
Popova-Butler, Alexandra; Dean, Donald H (2009) Proteomic analysis of the mosquito Aedes aegypti midgut brush border membrane vesicles. J Insect Physiol 55:264-72

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