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Nat Commun. 2018 May 10;9(1):1861. doi: 10.1038/s41467-018-04220-w.

Single molecule fate of HIV-1 envelope reveals late-stage viral lattice incorporation.

Author information

1
Molecular and Cellular Biophysics Program, Department of Biological Sciences, University of Denver, Denver, CO, 80210, USA.
2
HIV Dynamics and Replication Program, Center for Cancer Research, National Cancer Institute, Frederick, MD, 21702, USA.
3
Advanced Imaging Center, Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA, 20147, USA.
4
Molecular and Cellular Biophysics Program, Department of Biological Sciences, University of Denver, Denver, CO, 80210, USA. schuyler.vanengelenburg@du.edu.

Abstract

Human immunodeficiency virus type 1 (HIV-1) assembly occurs on the inner leaflet of the host cell plasma membrane, incorporating the essential viral envelope glycoprotein (Env) within a budding lattice of HIV-1 Gag structural proteins. The mechanism by which Env incorporates into viral particles remains poorly understood. To determine the mechanism of recruitment of Env to assembly sites, we interrogate the subviral angular distribution of Env on cell-associated virus using multicolor, three-dimensional (3D) superresolution microscopy. We demonstrate that, in a manner dependent on cell type and on the long cytoplasmic tail of Env, the distribution of Env is biased toward the necks of cell-associated particles. We postulate that this neck-biased distribution is regulated by vesicular retention and steric complementarity of Env during independent Gag lattice formation.

PMID:
29748537
PMCID:
PMC5945595
DOI:
10.1038/s41467-018-04220-w
[Indexed for MEDLINE]
Free PMC Article

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