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Background  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.    Results  A 100-kDa protein with APN activity (APN Anq  100) was isolated from the brush border membrane of  Anopheles quadrimaculatus . Native state binding analysis by surface plasmon resonance shows that APN Anq  100 forms tight binding to a mosquitocidal Bt toxin, Cry11Ba, but not to Cry2Aa, Cry4Ba or Cry11Aa.    Conclusion  An aminopeptidase from  Anopheles quadrimaculatus  mosquitoes is a specific binding protein for  Bacillus thuringiensis  Cry11Ba.

Identification of a Bacillus thuringiensis Cry11Ba toxin-binding aminopeptidase from the mosquito, Anopheles quadrimaculatus