Peptides selected from phage display library may change the conformation of S protein of rice stripe virus |
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Authors: | Zhang Hongwei Qu Zhicai Zhang Xiaoning Bai Fengwei Wan Youzhong Shao Minghua Ye Mingming Shen Daleng |
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Affiliation: | (1) Institute of Genetics, School of Life Sciences, Fudan University, 200433 Shanghai, P. R. China |
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Abstract: | Summary Phages with high affinity to the S protein obtained from rice stripe virus (RSV) were enriched from phage-displayed random 12-mer peptide library after three rounds of biopanning. 9 different peptides from the enriched library were selected by ELISA. Circular dichroism (CD) spectra of the GST-S fusion protein with binding phages and non-binding phages showed that structure of the S protein was changed after it bound to each of these 9 selected 12-mer peptides, which suggested that these peptides might disrupt the function of S protein. Thus, those peptides might be used to develop plant resistance and disrupt virus transmission. 3 of the 12-mer peptide genes were fused with the GST gene in pGEX 3X. The fusion proteins were also obtained usingE. coli expression system and purified. |
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Keywords: | circular dichroism phage display peptide rice stripe virus S protein |
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