HIV-1 nuclear import in macrophages is regulated by CPSF6-capsid interactions at the nuclear pore complex
Nuclear entry of HIV-1 replication complexes through intact nuclear pore complexes is critical for successful infection. The host protein cleavage-and-polyadenylation-specificity-factor-6 (CPSF6) has been implicated in different stages of early HIV-1 replication. Applying quantitative microscopy of...
Gespeichert in:
| Hauptverfasser: | , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
23 January 2019
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| In: |
eLife
Year: 2019, Jahrgang: 8 |
| ISSN: | 2050-084X |
| DOI: | 10.7554/eLife.41800 |
| Online-Zugang: | Verlag, Volltext: https://doi.org/10.7554/eLife.41800
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| Verfasserangaben: | David Alejandro Bejarano, Ke Peng, Vibor Laketa, Kathleen Börner, K. Laurence Jost, Bojana Lucic, Bärbel Glass, Marina Lusic, Barbara Müller, Hans-Georg Kräusslich |
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| 520 | |a Nuclear entry of HIV-1 replication complexes through intact nuclear pore complexes is critical for successful infection. The host protein cleavage-and-polyadenylation-specificity-factor-6 (CPSF6) has been implicated in different stages of early HIV-1 replication. Applying quantitative microscopy of HIV-1 reverse-transcription and pre-integration-complexes (RTC/PIC), we show that CPSF6 is strongly recruited to nuclear replication complexes but absent from cytoplasmic RTC/PIC in primary human macrophages. Depletion of CPSF6 or lack of CPSF6 binding led to accumulation of HIV-1 subviral complexes at the nuclear envelope of macrophages and reduced infectivity. Two-color stimulated-emission-depletion microscopy indicated that under these circumstances HIV-1 complexes are retained inside the nuclear pore and undergo CA-multimer dependent CPSF6 clustering adjacent to the nuclear basket. We propose that nuclear entry of HIV-1 subviral complexes in macrophages is mediated by consecutive binding of Nup153 and CPSF6 to the hexameric CA lattice. | ||
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