Nuclear pore blockade reveals that HIV-1 completes reverse transcription and uncoating in the nucleus
Open accessAbstract
Retroviral infection involves the reverse transcription of the viral RNA genome into DNA, which is subsequently integrated into the host cell genome. Human immunodeficiency virus type 1 (HIV-1) and other lentiviruses mediate the infection of non-dividing cells through the ability of the capsid protein 1 to engage the cellular nuclear import pathways of the target cell and mediate their nuclear translocation through components of the nuclear pore complex 2-4. Although recent studies have observed the presence of the capsid protein in the nucleus during infection 5-8, reverse transcription and disassembly of the viral core have conventionally been considered to be cytoplasmic events. Here, we use an inducible nuclear pore complex blockade to monitor the kinetics of HIV-1 nuclear import and define the biochemical staging of these steps of infection. Surprisingly, we observe that nuclear import occurs with relatively rapid kinetics (<5 h) and precedes the completion of reverse transcription in target cells, demonstrating that reverse transcription is completed in the nucleus. We also observe that HIV-1 remains susceptible to the capsid-destabilizing compound PF74 following nuclear import, revealing that uncoating is completed in the nucleus. Additionally, we observe that certain capsid mutants are insensitive to a Nup62-mediated nuclear pore complex blockade in cells that potently block infection by wild-type capsid, demonstrating that HIV-1 can use distinct nuclear import pathways during infection. These studies collectively define the spatio-temporal staging of critical steps of HIV-1 infection and provide an experimental system to separate and thereby define the cytoplasmic and nuclear stages of infection by other viruses.
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CA participates in multiple stages of the HIV-1 replication cycle, including reverse transcription, cytoplasmic transport via microtubules, uncoating, nuclear import, integration, and viral assembly.
“Beyond its structural role, CA participates in multiple stages of the viral replication cycle, including reverse transcription (RT), cytoplasmic transport via microtubules, uncoating of the viral pre-integration complex, nuclear import, integration, and viral assembly (12, 13).”
From Research progress on HIV-1 structural proteins and antiviral therapies (2026) · cites this paper as [12]
The Abstract (page not provided) describes CA-mediated nuclear import, capsid uncoating, and a functional role for assembled CA after nuclear entry; it also says CA influences integration-site selection. It discusses reverse transcription in relation to the capsid core, but does not establish every role in the list. Our copy does not substantiate CA-mediated cytoplasmic transport via microtubules or viral assembly. (LLM, conf=0.86)
Experimental — accuracy not yet measuredIn HIV-1, reverse transcription begins in the cytoplasm and is completed within the intact CA in the nucleus.
“However, using HIV-1 as a model, it has now been established that reverse transcription begins in the cytoplasm and is completed within the intact CA in the nucleus (Fig. 5).”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Dharan et al. 2020
The paper’s indexed text (labelled Abstract; no page given) says some cytoplasmic reverse transcription is necessary for productive nuclear import and that reverse transcription can complete in the nucleus. It also reports a functional role for assembled CA after nuclear import, but does not establish that reverse transcription finishes within an intact capsid. (LLM, conf=0.86)
Experimental — accuracy not yet measuredIn HIV-1, the intact CA containing the reverse transcription complex-including dimerized RNA, RT, CA, NC, IN, Vpr, and host factors such as APOBEC3G-gains access to the nucleus.
“Recent studies have shown that in HIV-1, the intact CA containing the reverse transcription complex, which includes dimerized RNA, RT, CA, NC, IN, Vpr, and host factors such as APOBEC3G gains access to the nucleus (Fig. 5) (Burdick et al. 2020, Dharan et al. 2020, Selyutina et al. 2020, Li et al. 2021, Müller et al. 2021).”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Dharan et al. 2020
The paper’s abstract reports that the viral ribonucleoprotein complex enters the nucleus before reverse transcription is complete, and that assembled CA remains functionally relevant after import (Fig. 4). It does not establish that an intact capsid enters the nucleus or document the claimed cargo list, particularly Vpr and APOBEC3G. (LLM, conf=0.86)
Experimental — accuracy not yet measuredIntact CA and CA-like structures are present inside the nucleus.
“some recent studies report the presence of intact CA and CA-like structures inside the nucleus, challenging the prevailing notions about retroviral CA uncoating”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Dharan et al. 2020
In the paper’s discussion (section labelled Abstract in our copy; page unavailable), continued PF74 sensitivity after nuclear import is interpreted as evidence that assembled CA functions in the nucleus. The paper also notes reports of nuclear capsid, but it does not establish that intact capsids or CA-like structures were observed inside the nucleus. (LLM, conf=0.84)
Experimental — accuracy not yet measuredUncoating near the integration site is due to the mounting physical pressure exerted by the newly reverse transcribed DNA.
“uncoating occurs near the integration site ~1.5 hours before integration due to the mounting physical pressure exerted by the newly reverse transcribed DNA”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Dharan et al. 2020
The paper’s main text (indexed under Abstract; page unavailable) reports that reverse transcription and uncoating complete in the nucleus, and says reverse transcription can induce uncoating. It does not establish that uncoating occurs near the integration site, about 1.5 hours before integration, or because newly transcribed DNA exerts physical pressure. Its References list a separate study on uncoating near integration sites, but that does not support the claimed mechanism. (LLM, conf=0.85)
Experimental — accuracy not yet measured
HIV-1 PICs contain CA molecules.
“In contrast to this, HIV-1 PICs have been found to contain CA molecules; furthermore, some recent studies report the presence of intact CA and CA-like structures inside the nucleus, challenging the prevailing notions about retroviral CA uncoating (Burdick et al. 2020, Dharan et al. 2020, Selyutina et al. 2020, Müller et al. 2021).”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Dharan et al. 2020
The passage labeled Abstract (page unavailable) says CA remains associated with nuclear viral ribonucleoprotein complexes and reports evidence that assembled CA remains functional after nuclear import. It does not specifically identify those complexes as preintegration complexes (PICs) or establish CA content in PICs as such. (LLM, conf=0.77)
Experimental — accuracy not yet measuredFor at least HIV-1, once the CA is inside the nucleus, reverse transcription and PIC formation are completed, and uncoating occurs near the integration site approximately 1.5 hours before integration.
“Thus, for at least HIV-1, once the CA is inside the nucleus, reverse transcription and PIC formation are completed, and uncoating occurs near the integration site ~1.5 hours before integration due to the mounting physical pressure exerted by the newly reverse transcribed DNA (Fig. 5) (Rankovic et al. 2017, Burdick et al. 2020, Dharan et al. 2020, Li et al. 2021, Müller et al. 2021, Yu et al. 2022)”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Dharan et al. 2020
The paper’s Abstract (page unavailable) says HIV-1 enters the nucleus before reverse transcription is complete and remains susceptible to a capsid-destabilizing compound after nuclear import, supporting nuclear completion of reverse transcription and uncoating. Our copy does not establish PIC formation, uncoating near the integration site approximately 1.5 hours before integration, or the citing sentence’s proposed physical-pressure mechanism. (LLM, conf=0.87)
Experimental — accuracy not yet measured
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- Authors
- Dharan, A., Bachmann, N., Talley, S., Zwikelmaier, V., & Campbell, E. M.
- Affiliations
- Loyola University Chicago (US)
- Corresponding author
- Campbell, Edward M.
- Venue
- Nature Microbiology
- Published
- 2020-06-01
- Volume
- 5
- Issue
- 9
- Pages
- 1088-1095
- ISSN
- 2058-5276 (ISSN-L)
- PMC
- PMC9286700
- OpenAlex
- W3031494023
- Cited by
- 223
- References
- 30
- Citations by year
- 2026: 21 · 2025: 36 · 2024: 40 · 2023: 26 · 2022: 26 · 2021: 53 · 2020: 21
- FWCI
- 16.59
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- Nature Microbiology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Division of Intramural Research, National Institute of Allergy and Infectious Diseases (R21 AI139009)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
- Keywords
- HIV-1, reverse transcription, viral uncoating, nuclear import, nuclear pore complex, capsid protein, Nup62, capsid mutants, lentiviral infection
- MeSH terms
- Capsid, Cell Nucleus, Cytoplasm, HeLa Cells, Humans, Indoles, Macrophages, Phenylalanine, Virus Replication, CD4-Positive T-Lymphocytes, HIV-1, HIV Infections, Active Transport, Cell Nucleus, Nuclear Pore, Capsid Proteins, Reverse Transcription, Host-Pathogen Interactions, HEK293 Cells
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