Peptides selected from phage display library may change the conformation of S protein of rice stripe virus |
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Authors: | Hongwei Zhang Zhicai Qu Xiaoning Zhang Fengwei Bai Youzhong Wan Minghua Shao Mingming Ye Daleng Shen |
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Affiliation: | (1) Institute of Genetics, School of Life Sciences, Fudan University, Shanghai, 200433, P. R. China |
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Abstract: | Phages with high affinity to the S protein obtained fromrice stripe virus (RSV) were enriched fromphage-displayed random 12-mer peptide library after threerounds of biopanning. 9 different peptides from theenriched library were selected by ELISA. Circulardichroism (CD) spectra of the GST-S fusion protein withbinding phages and non-binding phages showed thatstructure of the S protein was changed after it bound toeach of these 9 selected 12-mer peptides, which suggestedthat these peptides might disrupt the function of Sprotein. Thus, those peptides might be used to developplant resistance and disrupt virus transmission. 3 of the12-mer peptide genes were fused with the GST gene in pGEX3X. The fusion proteins were also obtained using E.coli expression system and purified. |
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Keywords: | circular dichroism phage display peptide rice stripe virus S protein |
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