Abdullah Mohd Amir F, Valaitis Algimantas P, Dean Donald H
Department of Biochemistry and The Protein Research Group, The Ohio State University, Columbus, Ohio 43210, USA.
BMC Biochem. 2006 May 22;7:16. doi: 10.1186/1471-2091-7-16.
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.
从几种鳞翅目昆虫中分离出的氨肽酶N（APN）型蛋白被认为是苏云金芽孢杆菌（Bt）毒素Cry毒素的结合蛋白（受体）。我们检测了四斑按蚊的刷状缘膜囊泡（BBMV）蛋白，以确定该生物体中的APN是否会结合对其有活性的杀蚊Cry毒素。
从四斑按蚊的刷状缘膜中分离出一种具有APN活性的100 kDa蛋白（APNAnq 100）。表面等离子体共振的天然状态结合分析表明，APNAnq 100与杀蚊Bt毒素Cry11Ba形成紧密结合，但与Cry2Aa、Cry4Ba或Cry11Aa不形成紧密结合。
四斑按蚊中的一种氨肽酶是苏云金芽孢杆菌Cry11Ba的特异性结合蛋白。
