Abstract
Multivalent ions affect the structure and organization of virus nanoparticles. Wild-type simian virus 40 (wt SV40) is a nonenveloped virus belonging to the polyomavirus family, whose external diameter is 48.4 nm. Calcium ions and disulfide bonds are involved in the stabilization of its capsid and are playing a role in its assembly and disassembly pathways. Using solution small-angle X-ray scattering (SAXS), we found that the volume of wt SV40 swelled by about 17% when both of its calcium ions were chelated by ethylene glycol-bis(2-aminoethylether)-N,N,N′,N′-tetraacetic acid and its disulfide bonds were reduced by dithiothreitol. By applying osmotic stress, the swelling could be reversed. DNA-containing virus-like particles behaved in a similar way. The results provide insight into the structural role of calcium ions and disulfide bonds in holding the capsid proteins in compact conformation.
| Original language | American English |
|---|---|
| Pages (from-to) | 58-64 |
| Number of pages | 7 |
| Journal | ACS Omega |
| Volume | 4 |
| Issue number | 1 |
| DOIs | |
| State | Published - 2 Jan 2019 |
Bibliographical note
Funding Information:We thank Daniel Harries for helpful discussion. We thank Desy synchrotron at Hamburg, beamline P12 (D. Svergun and his team), Soleil synchrotron, Swing beamline (J. Perez and his team), and the ESRF synchrotron, ID02 beamline (T. Narayanan and his team) for provision of synchrotron radiation facilities and for assistance in using the beamlines. This project was supported by the Israel Science Foundation (656/17), the United States-Israel Binational Science Foundation (2016311), and the NIH (Award number 1R01AI118933). R.A. acknowledges support from the Kaye-Einstein fellowship foundation.
Publisher Copyright:
© 2019 American Chemical Society.