Abstract
Virus-templated fabrication of compound structures can be made through incorporating the specifically inorganic-binding peptide into the viral scaffold, widely used is phage display system. Compared to prokaryotic phages, insect cell-based baculovirus has some strengths such as the adaptability to the proteins’ posttranslational modification and non-replication in mammalian cells. As an attempt to explore the baculovirus-mediated bioconjugates, we show in this study that a genetically engineered baculovirus, with a hexahistidine (His6) tagged ZnO binding peptide fused to the N-terminus of the viral capsid protein vp39 of AcNPV, was constructed. It maintains both the viral infectivity and the fusion protein’s activity. The presence of the fusion protein on the baculovirus particle was demonstrated by western blot analysis of purified budded virus. Its display on the virus capsid was revealed by virus fractionation analysis. The binding of nanosized ZnO powders to the virus capsid was visualized by transmission electron microscopy (TEM). This is the first report of the display of the inorganic-binding peptide on the capsid of eukaryotic baculovirus. Aimed at the nanomaterials’ application in the biological field, this research could find useful in the biotracking of the baculovirus transduction process and the preparation of novel functional nanodevices.
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Acknowledgments
The authors gratefully appreciate the enormous support of the research team of Professor Jianguo Chen from Peking University. We also thank unselfish assistance of Researcher Qi Lian Qin, Dr. Huan Zhang from Chinese Academy of Sciences. We are truly grateful to Dr. Peng Hu from Institute of Process Engineering for the generous presents of nanomateirals.
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Song, L., Liu, Y. & Chen, J. Baculoviral capsid display of His-tagged ZnO inorganic binding peptide. Cytotechnology 62, 133–141 (2010). https://doi.org/10.1007/s10616-010-9269-x
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DOI: https://doi.org/10.1007/s10616-010-9269-x