Baculoviral capsid display of His-tagged ZnO inorganic binding peptide.
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 (His(6)) 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.
Song
Lei
L
College of Life Science and Technology, Beijing University of Chemical Technology, 100029, Beijing, China, slof-songlei@163.com.
Liu
Yingying
Y
Chen
Jinchun
J
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