Identification of a Bacillus thuringiensis Cry11Ba toxin-binding aminopeptidase from the mosquito, Anopheles quadrimaculatus
1 Department of Biochemistry and The Protein Research Group, The Ohio State University, Columbus, Ohio 43210, USA
2 Department of Science, Faculty of Engineering, International Islamic University Malaysia, Kuala Lumpur, Malaysia
3 Department of Entomology, University of Georgia, Athens, GA 30602, USA
4 USDA Forest Service, Delaware, Ohio, USA
BMC Biochemistry 2006, 7:16 doi:10.1186/1471-2091-7-16Published: 22 May 2006
Aminopeptidase N (APN) type proteins isolated from several species of lepidopteran insects have been implicated as Bacillus thuringiensis (Bt) toxin-binding proteins (receptors) for Cry toxins. We examined brush border membrane vesicle (BBMV) proteins from the mosquito Anopheles quadrimaculatus to determine if APNs from this organism would bind mosquitocidal Cry toxins that are active to it.
A 100-kDa protein with APN activity (APNAnq 100) was isolated from the brush border membrane of Anopheles quadrimaculatus. Native state binding analysis by surface plasmon resonance shows that APNAnq 100 forms tight binding to a mosquitocidal Bt toxin, Cry11Ba, but not to Cry2Aa, Cry4Ba or Cry11Aa.
An aminopeptidase from Anopheles quadrimaculatus mosquitoes is a specific binding protein for Bacillus thuringiensis Cry11Ba.