Viruses are well known pathogens that cause a wide variety of diseases. To develop better treatments it is vital to understand the infection and replication pathways of viruses. Significant work has already been done towards resolving virus structures, their replication pathway, and transmission. But the physiochemical pathways of the assembly of the virus shell and the packaging of the genetic cargo inside is still not fully understood. Various studies have been conducted to gain insight into virus assembly processes, commonly involving model viruses. One of these model viruses is the cowpea chlorotic mottle virus (CCMV). CCMV is often studied because of its safety, simplicity, and its controllable disassembly and reassembly behaviour. The native CCMV is a positive sense RNA virus that consists of 90 identical capsid protein (CP) dimers and has a diameter of 28 nm and a T=3 icosahedral symmetry.In vitro studies show that CCMV can easily be disassembled into its RNA and free coat protein (CP) dimers upon raising the pH and increasing the ionic strength. Isolated CP can be reassembled into empty capsids at pH 5 and high ionic strength. Furthermore, the CP can assemble around non-native polyanionic species, for example polymers, nanoparticles or genomic material, forming virus-like particles (VLPs) with T = 1, T = 2, or T = 3 icosahedral symmetry, having a diameter of 18 nm, 23 nm, and 28 nm respectively, depending on the cargo size. Besides the VLP formation at pH 5, CCMV capsid protein can also form defined virus like particles at neutral pH, where CP-cargo interactions dominate, when a sufficiently negative template is present. However, the required strength of this interaction and the exact mechanism of assembly at these conditions are currently not yet fully understood. Therefore, this work seeks to determine the minimal number of charges, and thus number of nucleotides, needed to induce the virus assembly around oligonucleotides.

Minimal DNA length needed for the assembly of virus coat proteins

253rd National Meeting (2017)

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