Photoresponsive, reversible immobilization of virus particles on supramolecular platforms

2017 ◽  
Vol 53 (11) ◽  
pp. 1896-1899 ◽  
Author(s):  
N. L. Weineisen ◽  
C. A. Hommersom ◽  
J. Voskuhl ◽  
S. Sankaran ◽  
A. M. A. Depauw ◽  
...  

Covalently attached azobenzene moieties to cowpea chlorotic mottle virus (CCMV) allow for photoresponsive immobilization on cucurbit[8]uril bearing surfaces.


Author(s):  
Timothy S. Baker

Cowpea chlorotic mottle virus (CCMV) is a T=3 icosahedral RNA plant virus of diameter 25-26 nm. The negative staining-carbon film technique provides a useful method for inducing crystallization of the virus into hexagonal or square packed monolayers. This investigation reports an optical and digital analysis of electron micrographs, which shows that the virus packing in square arrays is not the most obvious one.Figure (a) shows a typical, negatively stained array, obtained by the published procedure. Close inspection reveals that all virus particles are oriented with a two-fold rotation axis normal to the plane of the array. Horne et al. have shown that adjacent particles are aligned at right angles to each other. Thus there are two particles in each unit cell with dimension~37.5 nm (outlined in (a)). The low resolution, apparent primitive lattice is a pseudo-lattice. This is confirmed in the optical diffraction pattern (Fig. b) where the strong, low resolution (<6 nm) spots appear at the pseudo-lattice positions.



2018 ◽  
Vol 13 (22) ◽  
pp. 3518-3525 ◽  
Author(s):  
Suzanne B. P. E. Timmermans ◽  
Daan F. M. Vervoort ◽  
Lise Schoonen ◽  
Roeland J. M. Nolte ◽  
Jan C. M. van Hest




1972 ◽  
Vol 15 (3) ◽  
pp. 247-251 ◽  
Author(s):  
J. B. Bancroft ◽  
I. H. Flack






2011 ◽  
Vol 1317 ◽  
Author(s):  
Yuanzheng Wu ◽  
Hetong Yang ◽  
Hyun-Jae Shin

Abstract:Cowpea chlorotic mottle virus (CCMV) has been a model system for virus studies for over 40 years and now is considered to be a perfect candidate as nanoplatform for applications in materials science and medicine. The ability of CCMV to self assemblein vitrointo virus-like particles (VLPs) or capsids makes an ideal reaction vessel for nanomaterial synthesis and entrapment. Here we report expression of codon optimized CCMV coat protein inPichia pastorisand production of self assembled CCMV VLPs by large-scale fermentation. CCMV coat protein gene (573 bp) was synthesized according to codon preference ofP. pastorisand cloned into pPICZA vector. The recombinant plasmid pPICZA-CP was transformed intoP. pastorisGS115 by electroporation. The resulting yeast colonies were screened by PCR and analyzed for protein expression by SDS-PAGE. After large-scale fermentation CCMV coat protein yields reached 4.8 g L−1. The CCMV VLPs were purified by modified PEG precipitation followed by cesium chloride density gradient ultracentrifugation, and then analyzed by size exclusion fast performance liquid chromatography (FPLC), UV spectrometry and transmission electron microscopy. Myoglobin was used as a model protein to be encapsulated in CCMV VLPs. The fluorescence spectroscopy showed that inclusion of myoglobin had occurred. The results indicated the production of CCMV capsids byP. pastorisfermentation now available for utilization in pharmacology or nanotechnology fields.



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