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Cone-shaped HIV-1 capsids are transported through intact nuclear pores

By Vojtech Zila, Erica Margiotta, Beata Turoňová, Thorsten G. Müller, Christian E. Zimmerli, Simone Mattei, Matteo Allegretti, Kathleen Börner, Jona Rada, Barbara Müller, Marina Lusic, Hans-Georg Kräusslich, Martin Beck

Posted 30 Jul 2020
bioRxiv DOI: 10.1101/2020.07.30.193524

Human immunodeficiency virus (HIV-1) remains a major health threat. Viral capsid uncoating and nuclear import of the viral genome are critical for productive infection. The size of the HIV-1 capsid is generally believed to exceed the diameter of the nuclear pore complex (NPC), indicating that capsid uncoating has to occur prior to nuclear import. Here, we combined correlative light and electron microscopy with subtomogram averaging to capture the structural status of reverse transcription-competent HIV-1 complexes in infected T cells. We demonstrate that the diameter of the NPC in cellulo is sufficient for the import of apparently intact, cone-shaped capsids. Subsequent to nuclear import, we detected disrupted and empty capsid fragments, indicating that uncoating of the replication complex occurs by breaking the capsid open, and not by disassembly into individual subunits. Our data directly visualize a key step in HIV-1 replication and enhance our mechanistic understanding of the viral life cycle. ### Competing Interest Statement The authors have declared no competing interest.

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