This is the peer reviewed version of the following article:Devkota, B., Petrov, A., Lemieux, S., Boz, M. B., Tang, L., Schneemann, A., … Harvey, S. C. (2009). Structural and Electrostatic Characterization of Pariacoto Virus: Implications for Viral Asembly. Biopolymers, 91(7), 530–538. http://doi.org/10.1002/bip.21168, which has been published in final form at doi.org/10.1002/bip.21168. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-ArchivingWe present the first all-atom model for the structure of a T=3 virus, pariacoto virus (PaV), which is a non-enveloped, icosahedral RNA virus and a member of the Nodaviridae family. The model is an extension of the crystal structure, which reveals about 88% of the protein structure but only about 35% of the RNA structure. Evaluation of alternative models confirms our earlier observation that the polycationic protein tails must penetrate deeply into the core of the virus, where they stabilize the structure by neutralizing a substantial fraction of the RNA charge. This leads us to propose a model for the assembly of small icosahedral RNA viruses: nonspecific binding of the protein tails to the RNA leads to a collapse of the complex, in a fashion reminiscent of DNA condensation. The globular protein domains are excluded from the condensed phase but are tethered to it, so they accumulate in a shell around the condensed phase, where their concentration is high enough to trigger oligomerization and formation of the mature virus
