TRIM5α self-assembly and compartmentalization of the HIV-1 viral capsid

Alvin Yu; Katarzyna A. Skorupka; Alexander J. Pak; Barbie K. Ganser-Pornillos; Owen Pornillos; Gregory A. Voth

doi:10.1038/s41467-020-15106-1

Nature Communications (Mar 2020)

TRIM5α self-assembly and compartmentalization of the HIV-1 viral capsid

Alvin Yu,
Katarzyna A. Skorupka,
Alexander J. Pak,
Barbie K. Ganser-Pornillos,
Owen Pornillos,
Gregory A. Voth

Affiliations

Alvin Yu: Department of Chemistry, Chicago Center for Theoretical Chemistry, Institute for Biophysical Dynamics, and James Franck Institute, The University of Chicago
Katarzyna A. Skorupka: Department of Molecular Physiology and Biological Physics, University of Virginia
Alexander J. Pak: Department of Chemistry, Chicago Center for Theoretical Chemistry, Institute for Biophysical Dynamics, and James Franck Institute, The University of Chicago
Barbie K. Ganser-Pornillos: Department of Molecular Physiology and Biological Physics, University of Virginia
Owen Pornillos: Department of Molecular Physiology and Biological Physics, University of Virginia
Gregory A. Voth: Department of Chemistry, Chicago Center for Theoretical Chemistry, Institute for Biophysical Dynamics, and James Franck Institute, The University of Chicago

DOI: https://doi.org/10.1038/s41467-020-15106-1
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 10

Abstract

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Tripartite-motif containing (TRIM) proteins modulate cellular responses to viral infection. Here the authors use molecular dynamics simulations to demonstrate that TRIM5α uses a two-dimensional lattice hopping mechanism to aggregate on the HIV capsid surface and initiate lattice growth.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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