Issue:ISSN 2095-1353
CN 11-6020/Q
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2012年49 No.5
Using phage display to map the binding epitope of the Bacillus thuringiensis Cry2Ab toxin
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Key Words:phage display,epitope mapping,Cry2Ab
Abstract:The insecticidal Cry toxins produced by Bacillus thuringiensisare highly specific to different insects. Various proteins,such as cadherin,aminopeptidase-N (APN ) and alkaline phosphatase (ALP ) are characterized as potential Cry-receptors. However,little is known about the mode of Cry2Ab action,such as its receptors and binding sites. We used phage display to characterize the binding epitope of the Cry2Ab toxinin vitro. A two peptide sequence was identified after four-rounds of screening. ELISA analysis showed that activated Cry2Ab toxin could bind these two peptides with highaffinity. The results indicate that employing this method can efficiently screen out target peptides with high affinity andspecificity.The method also provides a valuable platform to discover the mode of other Bt toxins.