Abstract
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 (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.
Conclusion:
An aminopeptidase from Anopheles quadrimaculatus mosquitoes is a specific binding protein for Bacillus thuringiensis Cry11Ba.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Amino Acid Sequence
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Animals
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Anopheles / enzymology*
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Bacillus thuringiensis Toxins
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Bacterial Proteins / metabolism*
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Bacterial Toxins / metabolism*
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Biosensing Techniques
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CD13 Antigens / chemistry
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CD13 Antigens / isolation & purification
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CD13 Antigens / metabolism*
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Cell Membrane / enzymology
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Chromatography, Ion Exchange / methods
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Endotoxins / metabolism*
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Hemolysin Proteins
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Insect Proteins / chemistry
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Insect Proteins / isolation & purification
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Insect Proteins / metabolism
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Microvilli / enzymology
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Molecular Sequence Data
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Protein Binding
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Sequence Analysis, Protein
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Species Specificity
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Surface Plasmon Resonance / methods
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Transport Vesicles / enzymology
Substances
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Bacillus thuringiensis Toxins
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Bacterial Proteins
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Bacterial Toxins
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Endotoxins
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Hemolysin Proteins
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Insect Proteins
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insecticidal crystal protein, Bacillus Thuringiensis
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CD13 Antigens