Analyses of alpha-amylase and alpha-glucosidase in the malaria vector mosquito, Anopheles gambiae, as receptors of Cry11Ba toxin of Bacillus thuringiensis subsp jegathesan

作者：Zhang Qi; Hua Gang; Bayyareddy Krishnareddy; Adang Michael J^*

来源：Insect Biochemistry and Molecular Biology, 2013, 43(10): 907-915.

DOI：10.1016/j.ibmb.2013.07.003

• Bacillus thuringiensis
• Bt
• Cry toxin
• Mosquitocidal
• Amylase
• Glucosidase

Bacillus thuringiensis subsp. jegathesan produces Cry11Ba crystal protein with high toxicity to mosquito larvae. The Cry11Ba toxicity is dependent on its receptors on mosquito larval midgut epithelial cells. Previously, a cadherin-like protein (AgCad2), aminopeptidase (AgAPN2) and alkaline phosphatase (AgALP1) were reported to be involved in regulation of Cry11Ba toxicity on Anopheles gambiae larvae. Here, the cDNAs encoding alpha-amylase (AgAmy1) and alpha-glucosidase (Agm3) were cloned from A. gambiae larva midgut. Both are glycophosphatidylinositol (GPI) anchored proteins on brush border membranes (BBMV). Immunohistochemistry revealed their localization on different regions of the larval midgut. AgAmyl and Agm3 bound Cry11Ba with high affinity, 37.6 nM and 21.1 nM respectively. Cry11Ba toxicity against A. gambiae larvae was neutralized by both AgAmy1 and Agm3. The results provide evidence that both AgAmy1 and Agm3 function as receptors of Cry11Ba in A. gambiae.

• 出版日期2013-10