TY - JOUR
T1 - Effect of Calcium Ions and Disulfide Bonds on Swelling of Virus Particles
AU - Asor, Roi
AU - Khaykelson, Daniel
AU - Ben-Nun-Shaul, Orly
AU - Oppenheim, Ariella
AU - Raviv, Uri
N1 - Publisher Copyright:
© 2019 American Chemical Society.
PY - 2019/1/2
Y1 - 2019/1/2
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85059636125&partnerID=8YFLogxK
U2 - 10.1021/acsomega.8b02753
DO - 10.1021/acsomega.8b02753
M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???
AN - SCOPUS:85059636125
SN - 2470-1343
VL - 4
SP - 58
EP - 64
JO - ACS Omega
JF - ACS Omega
IS - 1
ER -