Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 134, Issue 21, Pages 8823-8830Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja2110703
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Funding
- Safra Foundation
- Wolfson Foundation
- Rudin Foundation
- James Franck Center
- Fritz Haber Minerva Center
- Hebrew University Nanocenter
- US Israel Binational Science Foundation [2005050]
- NIH [R01-A1077688]
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Remarkably, uniform virus-like particles self-assemble in a process that appears to follow a rapid kinetic mechanism. The mechanisms by which spherical viruses assemble from hundreds of capsid proteins around nucleic acid, however, are yet unresolved. Using time-resolved small-angle X-ray scattering (TR-SAXS), we have been able to directly visualize SV40 VP1 pentamers encapsidating short RNA molecules (500mers). This assembly process yields T = 1 icosahedral particles comprised of 12 pentarners and one RNA molecule. The reaction is nearly one-third complete within 35 ms, following a two-state kinetic process with no detectable intermediates. Theoretical analysis of kinetics, using a master equation, shows that the assembly process nucleates at the RNA and continues by a cascade of elongation reactions in which one VP1 pentamer is added at a time, with a rate of approximately 10(9) M-1 s(-1). The reaction is highly robust and faster than the predicted diffusion limit. The emerging molecular mechanism, which appears to be general to viruses that assemble around nucleic acids, implicates long-ranged electrostatic interactions. The model proposes that the growing nucleoprotein complex acts as an electrostatic antenna that attracts other capsid subunits for the encapsidation process.
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