@article {27113,
	title = {Effect of ionic strength on the assembly of simian vacuolating virus capsid protein around poly(styrene sulfonate)},
	volume = {46},
	number = {11},
	year = {2023},
	month = {2023},
	pages = {107},
	abstract = {Virus-like particles (VLPs) are noninfectious nanocapsules that can be used for drug delivery or vaccine applications. VLPs can be assembled from virus capsid proteins around a condensing agent, such as RNA, DNA, or a charged polymer. Electrostatic interactions play an important role in the assembly reaction. VLPs assemble from many copies of capsid protein, with a combinatorial number of intermediates. Hence, the mechanism of the reaction is poorly understood. In this paper, we combined solution small-angle X-ray scattering (SAXS), cryo-transmission electron microscopy (TEM), and computational modeling to determine the effect of ionic strength on the assembly of Simian Vacuolating Virus 40 (SV40)-like particles. We mixed poly(styrene sulfonate) with SV40 capsid protein pentamers at different ionic strengths. We then characterized the assembly product by SAXS and cryo-TEM. To analyze the data, we performed Langevin dynamics simulations using a coarse-grained model that revealed incomplete, asymmetric VLP structures consistent with the experimental data. We found that close to physiological ionic strength, $$T=1$$VLPs coexisted with VP1 pentamers. At lower or higher ionic strengths, incomplete particles coexisted with pentamers and $$T=1$$particles. Including the simulated structures was essential to explain the SAXS data in a manner that is consistent with the cryo-TEM images.},
	isbn = {1292-895X},
	url = {https://doi.org/10.1140/epje/s10189-023-00363-x},
	author = {Asor, Roi and Singaram, Surendra W. and Levi-Kalisman, Yael and Hagan, Michael F. and Raviv, Uri}
}
