Michael J. Adang, PhD, University of Georgia

Michael J. Adang, PhD
Michael J. Adang, PhD

The Adang laboratory has focused on the target sites (e.g. receptors) in the insect midgut that determine insecticidal specificity and how those receptors differ in insects that are either naturally tolerant or have acquired resistance to Bt. Their group also participates in interdisciplinaryprojects to engineerBt d -endotoxins into soybeansand peanuts. The lab have been using isolated toxin binding proteins, and reconstituted them into membranes to determine toxin function. They are also taking a genetic approach by identifying and cloning genes encoding toxin binding proteins in Manduca sexta and Heliothisvirescens . Genes encoding binding proteins have been expressed in cultured insect cells. Recently, they have used phage technology to genetically modify the insecticidal specificity of d -endotoxins. By combining molecular and biochemical tools the challenge of insect resistance to Bt toxins can be addressed.



  1. Sangadala S, Walters FS, English LH, Adang MJ. A mixture of Manduca sexta aminopeptidase and phosphatase enhances Bacillus thuringiensis insecticidal CryIA(c) toxin binding and 86Rb(+)-K+ efflux in vitro. J Biol Chem. 1994 Apr 1;269(13):10088-92.
  2. Zhang, Q., Hua, G., Bayyareddy, K., and Adang, M.J. 2013. Analyses of a-amylase and a-glucosidase in the malaria vector Anopheles gambiae as receptors of Cry11Ba toxins of Bacillus thuringiensis subsp. jegethesan. Insect Biochem. Mole. Biol. 31:907-915.
  3. Bayyareddy K1, Zhu X, Orlando R, Adang MJ. Proteome analysis of Cry4Ba toxin-interacting Aedes aegypti lipid rafts using geLC-MS/MS. J Proteome Res. 2012 Dec 7;11(12):5843-55.
  4. Bayyareddy K1, Andacht TM, Abdullah MA, Adang MJ. 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. 2009 Apr;39(4):279-86.
  5. Hua G, Zhang R, Bayyareddy K, Adang MJ. Anopheles gambiae alkaline phosphatase is a functional receptor of Bacillus thuringiensis jegathesan Cry11Ba toxin. Biochemistry. 2009 Oct 20;48(41):9785-93.