Effect of ionic strength on the assembly of simian vacuolating virus capsid protein around poly(styrene sulfonate)

Roi Asor, Surendra W. Singaram, Yael Levi-Kalisman, Michael F. Hagan*, Uri Raviv*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

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. Graphic abstract: [Figure not available: see fulltext.].

Original languageAmerican English
Article number107
JournalEuropean Physical Journal E
Volume46
Issue number11
DOIs
StatePublished - 2 Nov 2023

Bibliographical note

Publisher Copyright:
© 2023, The Author(s), under exclusive licence to EDP Sciences, SIF and Springer-Verlag GmbH Germany, part of Springer Nature.

Fingerprint

Dive into the research topics of 'Effect of ionic strength on the assembly of simian vacuolating virus capsid protein around poly(styrene sulfonate)'. Together they form a unique fingerprint.

Cite this