Coarse-grained simulation reveals key features of HIV-1 capsid self-assembly

John M. A. Grime, James F. Dama, Barbie K. Ganser-Pornillos, Cora L. Woodward, Grant J. Jensen, Mark Yeager and Gregory A. Voth ()
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John M. A. Grime: Institute for Biophysical Dynamics, James Franck Institute, and Computation Institute, The University of Chicago
James F. Dama: Institute for Biophysical Dynamics, James Franck Institute, and Computation Institute, The University of Chicago
Barbie K. Ganser-Pornillos: University of Virginia School of Medicine
Cora L. Woodward: California Institute of Technology
Grant J. Jensen: California Institute of Technology
Mark Yeager: University of Virginia School of Medicine
Gregory A. Voth: Institute for Biophysical Dynamics, James Franck Institute, and Computation Institute, The University of Chicago

Nature Communications, 2016, vol. 7, issue 1, 1-11

Abstract: Abstract The maturation of HIV-1 viral particles is essential for viral infectivity. During maturation, many copies of the capsid protein (CA) self-assemble into a capsid shell to enclose the viral RNA. The mechanistic details of the initiation and early stages of capsid assembly remain to be delineated. We present coarse-grained simulations of capsid assembly under various conditions, considering not only capsid lattice self-assembly but also the potential disassembly of capsid upon delivery to the cytoplasm of a target cell. The effects of CA concentration, molecular crowding, and the conformational variability of CA are described, with results indicating that capsid nucleation and growth is a multi-stage process requiring well-defined metastable intermediates. Generation of the mature capsid lattice is sensitive to local conditions, with relatively subtle changes in CA concentration and molecular crowding influencing self-assembly and the ensemble of structural morphologies.

Date: 2016
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DOI: 10.1038/ncomms11568

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