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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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“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]
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In the citing paper
“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
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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
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“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
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“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
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“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
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“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
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Citations
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Self-citationHIV-1 uncoats in the nucleus near sites of integration
Burdick, R. C., Li, C., Munshi, M., Rawson, J. M. O., Nagashima, K., Hu, W.-S., & Pathak, V. K. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1920631117 · Cited by 313
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Self-citation
Cited by
Sorted by citations
Items 101–200 of 223
Confined no more: Viral mechanisms of nuclear entry and egress
Molenberghs, F., Bogers, J., & Vos, W. H. D. (2020) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2020.105875 · Cited by 11
Cyclophilin A facilitates HIV-1 integration
Padron, A., Dwivedi, R., Chakraborty, R., Prakash, P., Kim, K., Shi, J., Ahn, J., Pandhare, J., Luban, J., Aiken, C., et al. (2024) · Journal of Virology · doi:10.1128/jvi.00947-24 · Cited by 10
“…suggest that the intact or near-intact HIV-1 capsid is imported through the NPC (94, 120, 121) and RTN could be completed in the nucleus (95, 122, 123), we (99, 100, 110, 118) and others (111, 124–130) have shown that PICs extracted ~5 hpi from the cytoplasm (Cy-PICs) retain viral DNA…”
Role of Transportin-SR2 in HIV-1 Nuclear Import
Tabasi, M., Nombela, I., Janssens, J., Lahousse, A. P., Christ, F., & Debyser, Z. (2021) · Viruses · doi:10.3390/v13050829 · Cited by 10
“by using an inducible nuclear pore complex blockade, namely Nup62 fused to a drug-inducible dimerization domain B (DmrB), found that despite the completion of reverse transcription in the nucleus, some degree of cytoplasmic reverse transcription is required for a productive infection [78].”
MethodSalas-Briceno, K., & Ross, S. R. (2021) · Journal of Virology · doi:10.1128/jvi.01244-21 · Cited by 7
“Recent studies have 227 suggested that HIV reverse transcription largely occurs in the nucleus (40-43).”
BackgroundSpatial resolution of HIV-1 post-entry steps in resting CD4 T cells
Ananth, S., Ambiel, I., Schifferdecker, S., Müller, T. G., Wratil, P. R., Mejías‐Pérez, E., Kräusslich, H., Müller, B., Keppler, O. T., & Fackler, O. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.113941 · Cited by 10
May I Help You with Your Coat? HIV-1 Capsid Uncoating and Reverse Transcription
Arribas, L., Menéndez‐Arias, L., & Betancor, G. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25137167 · Cited by 10
“(vii) is there a single mechanism for capsid uncoating, or are alternative routes possible (as it seems to occur with N74D or P90A CA mutant viruses [102])?”
BackgroundInfluentialEquine Infectious Anemia Virus Cellular Partners Along the Viral Cycle
Schimmich, C., Vabret, A., Zientara, S., & Valle‐Casuso, J. C. (2024) · Viruses · doi:10.3390/v17010005 · Cited by 8
“More recently, it appears that blockage of the nuclear pores impairs reverse transcription and uncoating, implying that both steps happen inside the nucleus [16].”
The nuclear localization signal of CPSF6 governs post-nuclear import steps of HIV-1 infection
Rohlfes, N., Radhakrishnan, R., Singh, P. K., Bedwell, G. J., Engelman, A., Dharan, A., & Campbell, E. M. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1012354 · Cited by 8
Self-citationHikichi, Y., Burdick, R. C., Patro, S. C., Ding, S.-Y., Luke, B. T., Clark, E., Ablan, S. D., Wu, X., Pathak, V. K., & Freed, E. O. (2025) · Science Advances · doi:10.1126/sciadv.adz8980 · Cited by 8
Murine leukemia virus infection of non-dividing dendritic cells is dependent on nucleoporins
Salas-Briceno, K., Zhao, W., & Ross, S. R. (2024) · PLOS Pathogens · doi:10.1371/journal.ppat.1011640 · Cited by 8
Efficient HIV-1 in vitro reverse transcription: optimal capsid stability is required
Burdick, R. C., & Pathak, V. K. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00458-3 · Cited by 8
“The results of these robust cell-free assays, and those from cell-based assays by us and others have gratifyingly converged to show that reverse transcription primarily occurs in the context of an intact viral core.(4,5) It is anticipated that the cell-free ERT assays described by Christensen et al.”
Dynactin 1 negatively regulates HIV-1 infection by sequestering the host cofactor CLIP170
Shanmugapriya, S., da Silva, E. S., Campbell, J. A., Boisjoli, M.-P., & Naghavi, M. H. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2102884118 · Cited by 8
A new class of capsid-targeting inhibitors that specifically block HIV-1 nuclear import
Boulay, A., Quevarec, E., Malet, I., Nicastro, G., Chamontin, C., Perrin, S., Henriquet, C., Pugnière, M., Courgnaud, V., Blaise, M., et al. (2024) · EMBO Molecular Medicine · doi:10.1038/s44321-024-00143-w · Cited by 8
CPSF6 promotes HIV-1 preintegration complex function
Chaudhuri, E., Jang, S., Chakraborty, R., Radhakrishnan, R., Arnarson, B., Prakash, P., Cornish, D., Rohlfes, N., Singh, P. K., Shi, J., et al. (2025) · Journal of Virology · doi:10.1128/jvi.00490-25 · Cited by 7
Self-citationKinetic implications of IP 6 anion binding on the molecular switch of HIV-1 capsid assembly
Gupta, M., Hudait, A., Yeager, M. J., & Voth, G. A. (2025) · Science Advances · doi:10.1126/sciadv.adt7818 · Cited by 9
Extracellular membrane particles en route to the nucleus – exploring the VOR complex
Lorico, A., Santos, M. F., Karbanová, J., & Corbeil, D. (2025) · Biochemical Society Transactions · doi:10.1042/bst20253005 · Cited by 8
“Capsid uncoating at nuclear pores or inside the nucleus were documented [201,202].”
Reverse transcription progression and genome length regulate HIV-1 core elasticity and disassembly
Deshpande, A., Shi, J., Rotem‐Dai, N., Aiken, C., & Rousso, I. Y. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1013269 · Cited by 7
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Taylor, I. A., & Fassati, A. (2023) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjad076 · Cited by 7
“Recent evidence shows that reverse transcription can be completed in the nucleus ( Dharan et al., 2020 ; Li et al., 2021 ; Muller et al., 2021 ; Rensen et al., 2021 ) , which, by delaying core uncoating until shortly before integration, would reduce the risk of DNA sensing in the cytoplasm and…”
BackgroundMeasuring the subcellular compartmentalization of viral infections by protein complementation assay
Fernandez, J., Hassen‐Khodja, C., Georget, V., Rose, T., Jacob, Y., Janin, Y. L., Nisole, S., Vidalain, P., & Arhel, N. J. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2010524118 · Cited by 7
“Recent reports of intact HIV-1 capsids in the nucleus suggest that reverse transcription and uncoating can also occur after nuclear import near sites of integration (12, 13).”
BackgroundHe, Y., Xu, M., Ouyang, J., Zhao, L., Ma, T., Zhang, X., Wang, R., Shang, H., & Liang, G. (2025) · Nature Communications · doi:10.1038/s41467-025-58218-2 · Cited by 6
Hudait, A., Burdick, R. C., Bare, E. K., Pathak, V. K., & Voth, G. A. (2026) · eLife · doi:10.7554/elife.109282.4 · Cited by 6
New Advances in Anti-HIV-1 Strategies Targeting the Assembly and Stability of Capsid Protein
Zhang, C., Li, B., Li, J., Zhang, H., & Wu, Y. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26125819 · Cited by 6
Gien, H., Morse, M., McCauley, M. J., Rouzina, I. F., Gorelick, R. J., & Williams, M. C. (2024) · Viruses · doi:10.3390/v16060872 · Cited by 6
“Further studies have confirmed that an endogenous reverse transcription (ERT) process can complete within intact cores in vitro and in the nucleus [21,24,25].”
BackgroundThe innate immune factor RPRD2/REAF and its role in the Lv2 restriction of HIV
Jackson-Jones, K. A., McKnight, Á., & Sloan, R. D. (2023) · mBio · doi:10.1128/mbio.02572-21 · Cited by 6
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Cell Type-Dependent Escape of Capsid Inhibitors by Simian Immunodeficiency Virus SIVcpz
Twizerimana, A. P., Scheck, R., Becker, D., Zhang, Z., Wammers, M., Avelar, L. A. A., Pflieger, M., Häussinger, D., Kurz, T., Gohlke, H., et al. (2020) · Journal of Virology · doi:10.1128/jvi.01338-20 · Cited by 6
“These data, together with our findings, lead us to postulate that SIVcpz viruses, in particular SIVcpzPts, infect at least some cell types via a pathway that is independent of NUP153, NUP358, and CPSF6, consistent with recent findings describing a heterogeneity of nuclear pore complexes influencing HIV-1 infection (6,…”
ResultPreclinical virology profiles of the HIV-1 capsid inhibitors VH4004280 and VH4011499
Wang, C., Huang, H., Valera, L., Parcella, K. E., Iwuagwu, C. I., McAuliffe, B., Falk, P. J., O’Boyle, D. R., Rose, R. E., Padilla, R., et al. (2025) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00309-25 · Cited by 5
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Nuclear restriction of HIV-1 infection by SUN1
Persaud, M., Selyutina, A., Buffone, C., Opp, S., Donahue, D. A., Schwartz, O., & Diaz‐Griffero, F. (2021) · Scientific Reports · doi:10.1038/s41598-021-98541-4 · Cited by 5
Técher, H. (2024) · BioEssays · doi:10.1002/bies.202400066 · Cited by 5
“60] Altogether these results suggest that in addition to nuclear DNA sensing, part of TREX1 role in HIV-1 blockade may depend on its nuclear localization.”
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Masuda, T., Kotani, O., Yokoyama, M., Abe, Y., Kawai, G., & Sato, H. (2022) · Viruses · doi:10.3390/v15010031 · Cited by 6
A DNA-origami nuclear pore mimic reveals nuclear entry mechanisms of HIV-1 capsidPreprint
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“Within the NPC and inside the nucleus, cooperation and competition between CPSF6 and other proteins such as CypA (Schaller et al., 2011) and NUP153 (Di Nunzio et al., 2012; Koh et al., 2013) may occur to enable the delivery of the capsid to sites of integration.”
BackgroundBeyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication
Jehad, M. A., Ali, L. M., Pillai, V. N., Prabhu, S. G., Mustafa, F., & Rizvi, T. A. (2026) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaf066 · Cited by 5
“…of host factors like the cleavage and polyadenylation specificity factor 6 (CPSF6) and nuclear pore complex (NPC) proteins, NUP153 and NUP358 (Matreyek et al. 2013 , Buffone et al. 2018 , Bejarano et al. 2019 , Burdick et al. 2020 , Dharan et al. 2020 , Selyutina et al. 2020 , Zila et al. 2021 ).”
InfluentialLenacapavir-induced capsid damage uncovers HIV-1 genomes emanating from nuclear speckles
Müller, T. G., Klaus, S., Žíla, V., Lucic, B., Penzo, C., Nopper, S. L., Golani, G., Anders‐Össwein, M., Sonntag-Buck, V., Heuser, A., et al. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00652-5 · Cited by 4
“This process starts following entry of the capsid into the cytoplasm (Hu and Hughes, 2012), but is only completed inside the nucleus (Dharan et al, 2020; Selyutina et al, 2020; Burdick et al, 2020; Francis et al, 2020; Rensen et al, 2021; Müller et al, 2021).”
InfluentialEssential functions of inositol hexakisphosphate (IP6) in murine leukemia virus replication
Biswas, B., Lai, K. K., Bracey, H., Datta, S. A. K., Harvin, D., Sowd, G. A., Aiken, C., & Rein, A. R. (2024) · mBio · doi:10.1128/mbio.01158-24 · Cited by 4
Early HIV replication revisited
Arhel, N. J. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0784-z · Cited by 4
Park, K., Lee, D., Jeong, J., Lee, S., Kim, S., & Ahn, K. (2024) · eLife · doi:10.7554/elife.97348 · Cited by 4
“…post-infection hours, when the HIV-1 genome is imported into the nucleus and integration may initiate ( Brussel and Sonigo, 2003 ; Albanese et al., 2008 ; Dharan et al., 2020 ), we hypothesized that host genomic R-loops play a role in HIV-1 integration and possibly in integration site selection.”
Epigenetic mechanisms of retroviral regulation: a comparative review
Shin, S. Y., Tahmida, M., Beliakova‐Bethell, N., & LaMere, S. A. (2026) · Epigenetics & Chromatin · doi:10.1186/s13072-025-00659-6 · Cited by 3
“The location where reverse transcription takes place is also different in these two viruses: MLV is reverse transcribed solely in the cytoplasm, whereas in HIV-1, it begins in the cytoplasm but ends near or in the nucleus (although the precise site of completion remains controversial) [9, 153, 154].”
Xiu, C., Chen, R., Wen, L., Qin, T., Liao, Y., Tao, X., Yuan, Z., Wei, W., Li, J., Huang, Y., et al. (2024) · Journal of Medical Virology · doi:10.1002/jmv.70116 · Cited by 3
“Besides, this new discovery supports emerging perspectives indicating that crucial steps in HIV ‐ 1 infection, such as reverse transcription and uncoating, occur within the nucleus [30, 31] rather than the previously believed cytoplasm.”
Nup358 and Nup153 Facilitate nuclear import of BmNPV nucleocapsids in Bombyx mori cells
Yin, K., Zhang, T., Huang, J., & Hao, B. (2025) · Journal of Invertebrate Pathology · doi:10.1016/j.jip.2025.108318 · Cited by 3
Single-molecule measurements of double-stranded DNA condensation
Gien, H., Rouzina, I. F., Morse, M., McCauley, M. J., & Williams, M. C. (2025) · Biophysical Journal · doi:10.1016/j.bpj.2025.03.033 · Cited by 3
Moloney Murine Leukemia Virus p12 Is Required for Histone Loading onto Retroviral DNAs
Wang, G. Z., & Goff, S. P. (2021) · Journal of Virology · doi:10.1128/jvi.00495-21 · Cited by 3
Lentiviral Nef Proteins Differentially Govern the Establishment of Viral Latency
Carlin, E., Greer, B. D., Lowman, K. E., Dalecki, A. G., Duverger, A. E., Wagner, F., & Kutsch, O. (2022) · Journal of Virology · doi:10.1128/jvi.02206-21 · Cited by 3
HIV capsids: orchestrators of innate immune evasion, pathogenesis and pandemicity
Morling, K. L., ElGhazaly, M., Milne, R. S. B., & Towers, G. J. (2025) · Journal of General Virology · doi:10.1099/jgv.0.002057 · Cited by 7
“Whilst it was initially thought that viral DNA synthesis completes in the cytoplasm, recent work suggests that it can complete in the nucleus, consistent with the completion of RT driving nuclear uncoating [63, 65, 68, 107].”
Bao, Q., & Zhou, J. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115188 · Cited by 4
Decoding the biogenesis of HIV-induced CPSF6 puncta and their fusion with nuclear specklesPreprint
Tomasini, C., Cuche, C., Ay, S., Collard, M., Cui, B., Rashid, M., Bhattacharjee, S., Tello-Rubio, B., Buchrieser, J., Luchsinger, C., et al. (2024) · eLife · doi:10.7554/elife.103725 · Cited by 3
“They unveil that crucial stages of early viral infection occur within the host nucleus ( Burdick et al., 2020 ; Dharan et al., 2020 ; Francis et al., 2020 ; Scoca et al., 2023 ; Selyutina et al., 2020 ).”
HIV-1 signalling remodels nuclear pores to licence infection
Mesner, D., Whelan, M. V. X., Shivkumar, M., Reuschl, A., Chiozzi, R. Z., Thalassinos, K., de Bruin, R. A. M., & Jolly, C. L. (2026) · Nature · doi:10.1038/s41586-026-10453-3 · Cited by 2
“This includes CA-binding Nups that act as co-factors for HIV-1 infection (Nup358, Nup98, Nup153, Nup62) 22,30–32 as well as TPR and Nup62, which regulate NPC structure and assembly 33 .”
Maternal embryonic leucine zipper kinase (MELK) optimally regulates the HIV-1 uncoating process
Nishiyama, T., Takada, T., Takeuchi, H., & Iwami, S. (2022) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2022.111152 · Cited by 2
Detection of CPSF6 in Biomolecular Condensates as a Reporter of HIV-1 Nuclear Import
Luchsinger, C., & Diaz‐Griffero, F. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3862-0_9 · Cited by 2
Decoding the biogenesis of HIV-induced CPSF6 puncta and their fusion with nuclear speckles
Tomasini, C., Cuche, C., Ay, S., Collard, M., Cui, B., Rashid, M., Bhattacharjee, S., Tello-Rubio, B., Buchrieser, J., Luchsinger, C., et al. (2026) · eLife · doi:10.7554/elife.103725.3 · Cited by 2
Blockade of de novo dNTP biosynthesis pathway delays HIV-1 early life cycle kinetics and dynamics
Siddique, M. A., McRaven, M. D., Arif, M. S., Allen, E. J., McKee, C., Honne, S., Sultana, T., Kim, B., Carias, A. M., Mamede, J. I., et al. (2025) · mBio · doi:10.1128/mbio.01047-25 · Cited by 2
“However, other research groups have put forth the nuclear pore (5, 41, 42) or nucleus (4, 7, 43, 44) as the site of initiation and completion of HIV-1 capsid uncoating.”
The human cellular protein NoL12 is a specific partner of the HIV-1 nucleocapsid protein NCp7
Zgheib, S., Taha, N., Zeiger, M., Glushonkov, O., Lequeu, T., Anton, H., Didier, P., Boutant, E., Mély, Y., & Réal, É. (2023) · Journal of Virology · doi:10.1128/jvi.00040-23 · Cited by 3
Sousa, A. (2021) · Biomedical Journal of Scientific & Technical Research · doi:10.26717/bjstr.2021.34.005501 · Cited by 2
Chemical Stabilization of the HIV-1 Capsid Results in Efficient HIV-1 Reverse Transcription in vitroPreprint
Jennings, J., Shi, J., Varadarajan, J., Jamieson, P. J., & Aiken, C. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.17.302315 · Cited by 2
Gifford, L. B., & Melikyan, G. B. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.22.553958 · Cited by 2
Decoding the biogenesis of HIV-induced CPSF6 puncta and their fusion with the nuclear specklePreprint
Tomasini, C., Cuche, C., Ay, S., Collard, M., Cui, B., Rashid, M., Bhattacharjee, S., Buchrieser, J., Luchsinger, C., Bertelli, C., et al. (2024) · eLife · doi:10.7554/elife.103725.1 · Cited by 2
Hudait, A., Burdick, R. C., Bare, E. K., Pathak, V. K., & Voth, G. A. (2025) · eLife · doi:10.7554/elife.109282 · Cited by 2
“…mechanistic models had proposed that viral cores uncoat in the cytoplasm or at the NPC central channel since the size of the capsid either exceeds or is comparable to the diameter of the NPC central channel ( Hulme et al., 2011 ; Mamede et al., 2017 ; Burdick et al., 2017 ; Dharan et al., 2020 ).”
Research progress on HIV-1 structural proteins and antiviral therapies
Wang, H., Yuan, J., & Wang, H. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1805597 · Cited by 2
“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).”
Regulation of expression of unintegrated and integrated HIV-1 DNA: keeping the wolves at bay
Goff, S. P. (2024) · Frontiers in Virology · doi:10.3389/fviro.2024.1481451 · Cited by 1
Effects of GS-CA1 on nuclear envelope-associated early HIV-1 infection steps
Singh, A., Fourcassié, V., dos Santos, K. C. G., Chelbi, H., Mérindol, N., Droit, A., Germain, H., & Berthoux, L. (2025) · Frontiers in Virology · doi:10.3389/fviro.2025.1547176 · Cited by 1
“Interestingly, HIV-1 was also found to modulate the levels of Nup358 at NPCs (12, 13), which opens the possibility that HIV-1 cores affect NPCs integrity instead of simply using them to achieve passage to the nucleus.”
Preece, B., Peppel, W., Gallegos, R., Ysassi, G., Clinger, G., Bohn, N., Adhikary, B., Mendonça, L., Belnap, D. M., Vershinin, M. D., et al. (2025) · Viruses · doi:10.3390/v17030364 · Cited by 1
“After fusion of the viral membrane with the next host, the integrity of the mature core is essential for delivery of the HIV RNP to the nucleus of the next host [29,30], allowing for integration of the viral DNA into the genome of the target cell.”
How HIV-1 Uses the Metabolite Inositol Hexakisphosphate to Build Its Capsid
James, L. C. (2025) · Viruses · doi:10.3390/v17050689 · Cited by 1
“The exact spatiotemporal nature of uncoating and the manner in which it is triggered are subjects of current intense research by multiple groups [8,11–14].”
Biswas, U., Bernal, C., Wang, R., & DeStefano, J. J. (2025) · Journal of Virology · doi:10.1128/jvi.00564-25 · Cited by 1
Luchsinger, C., Dai, A. Z., Yalamanchili, H. K., Balakrishnan, A., Huang, K.-L., Bertelli, C., Cui, B., Lorenzo-Redondo, R., Wagner, E. J., & Diaz‐Griffero, F. (2025) · mBio · doi:10.1128/mbio.02865-25 · Cited by 1
HIV-1 uncoating location dictates sites of integration
Burdick, R. C., Patro, S. C., Bare, E. K., Siddiqui, R., Delviks‐Frankenberry, K. A., Nikolaitchik, O. A., Hughes, S. H., Wu, X., Hu, W.-S., & Pathak, V. K. (2026) · Nature Communications · doi:10.1038/s41467-026-71679-3 · Cited by 1
“Consistent with our observations, it was demonstrated that reverse transcription is completed after nuclear entry 10 – 12 and multiple recent studies have reported the presence of intact or largely intact HIV-1 capsids within the nucleus 13 – 17 .”
Monitoring HIV-1 Nuclear Import Kinetics Using a Chemically Induced Nuclear Pore Blockade Assay
Dharan, A., & Campbell, E. M. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3862-0_10 · Cited by 1
Self-citationBiochemical Detection of Capsid in the Nucleus During HIV-1 Infection
Diaz‐Griffero, F. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3862-0_11 · Cited by 1
Ding, D., Shi, D., Xu, S., Zhou, Y., Jiang, X., Liu, X., Dick, A., & Zhan, P. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-23932-8.00018-2 · Cited by 1
Clicking viruses—with chemistry toward mechanisms in infection
Greber, U. F. (2025) · Journal of Virology · doi:10.1128/jvi.00471-25 · Cited by 1
La capside du virus de l’immunodéficience humaine au centre d’un engouement sans précédent
Arhel, N. J. (2021) · médecine/sciences · doi:10.1051/medsci/2021050 · Cited by 1
Overlap Intensity: An ImageJ Macro for Analyzing the HIV-1 In Situ Uncoating Assay
Ingram, Z., Matheney, H., Wise, E., Weatherford, C., & Hulme, A. E. (2021) · Viruses · doi:10.3390/v13081604 · Cited by 1
“In recent years, quantification of these subtle changes has become increasingly important given studies showing evidence of biphasic uncoating, uncoating at the nuclear pore, and nuclear uncoating [6,16,20,23,25,44].”
BackgroundPost-transcriptional regulation of HIV-1 gene expression
Tripathi, A., Mitra, A., Dasgupta, A., & Mitra, D. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91305-8.00004-1 · Cited by 1
Human immunodeficiency virus-1 induces and targets host genomic R-loops for viral genome integrationPreprint
Park, K., Lee, D., Jeong, J., Lee, S., Kim, S., & Ahn, K. (2024) · eLife · doi:10.7554/elife.97348.1 · Cited by 1
Park, K., Lee, D., Jeong, J., Lee, S., Kim, S., & Ahn, K. (2024) · eLife · doi:10.7554/elife.97348.2 · Cited by 1
The Discovery and Development of Islatravir (4′‐Ethynyl‐2‐fluoro‐2′‐deoxyadenosine [EFdA], MK‐8591)
Snyder, A. A., Wen, X., Michailidis, E., Kirby, K. A., Mitsuya, H., & Sarafianos, S. G. (2025) · Wiley eBooks · doi:10.1002/9783527845088.ch04 · Cited by 2
Kirby, K. A., McFadden, W. M., Wang, L., Du, H., Zhang, H., Castaner, A. E., Lorson, Z. C., Nafisi, A., Selyutina, A., Luchsinger, C., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.30.696960 · Cited by 1
“PF74 and GS-CA1 have been reported to prevent the formation of CPSF6 accumulation in nuclear speckles during infection (7, 40, 64).”
The right place at the right time
Toit, A. D. (2020) · Nature Reviews Microbiology · doi:10.1038/s41579-020-0396-x
Travis, C., Nakamura, T., Amano, M., Takamune, N., Matsuoka, M., & Nakata, H. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.18.444758
Bedwell, G. J., & Engelman, A. (2021) · eLife · doi:10.7554/elife.69887
Informatically-informed biochemical characterization of aptamer-protein complexes
Gruenke, P. R. (2022) · MOspace Institutional Repository (University of Missouri) · doi:10.32469/10355/91663
Induction of membraneless organelles as a strategy for HIV-1 post-nuclear entry steps
Zhou, S. M., & Deng, H. (2023) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjad013
“This dogma has recently been broken by studies showing that the cone-shaped HIV-1 capsids along with vRNA genomes can be transported through the nuclear pore complex, and nuclear import proceeds the completion of reverse transcription (Dharan et al., 2020; Zila et al., 2021).”
BackgroundMurine leukemia virus can infect non-dividing cellsPreprint
Salas-Briceno, K., Zhao, W., & Ross, S. R. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.30.555458
Advanced Therapy Medicinal Products: Clinical, Non-clinical, and Quality Considerations
Mastrobattista, E., Doevendans, E., van Til, N. P., Kemp, V., de Vrij, J., & Hoogendoorn, K. H. (2024) · Springer eBooks · doi:10.1007/978-3-031-30023-3_14
Central nervous system complications of human immunodeficiency virus infection
Zhou, W., Bhattarai, S., Sapkota, R., Santamaria, A. M., & Gendelman, H. E. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-99744-7.00015-8
Characterization of Nuclear HIV-Induced Membraneless Organelles Through Fluorescence Microscopy
Scoca, V., & Nunzio, F. D. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3862-0_8 · Cited by 1
Landolfo, S., Raviola, S., & Andrea, M. D. (2024) · Elsevier eBooks · doi:10.1016/b978-0-128-24465-4.00049-1
Kinetic Implications of IP 6 Anion Binding on the Molecular Switch of the HIV-1 Capsid AssemblyPreprint
Gupta, M., Hudait, A., Yeager, M. J., & Voth, G. A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.05.627050
Preece, B., Peppel, W., Gallegos, R., Yassasi, G., Clinger, G., Bohn, N., Adhikary, B., Mendonça, L., Belnap, D. M., Vershinin, M. D., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.12.628087
HIV-1 capsid found guilty of breaking and entering
Dharan, A., & Campbell, E. M. (2025) · Nature Microbiology · doi:10.1038/s41564-025-02071-y
Self-citationThe intersection of viral mimicry and nuclear entry
Dickson, C. F., Phalora, P. K., & Jacques, D. A. (2025) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2025.07.002
Luchsinger, C., Dai, A. Z., Yalamanchili, H. K., Balakrishnan, A., Huang, K.-L., Bertelli, C., Cui, B., Lorenzo-Redondo, R., Wagner, E. J., & Diaz‐Griffero, F. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.07.669137
Decoding the biogenesis of HIV-induced CPSF6 puncta and their fusion with the nuclear specklePreprint
Tomasini, C., Cuche, C., Ay, S., Collard, M., Cui, B., Rashid, M., Bhattacharjee, S., Tello-Rubio, B., Buchrieser, J., Luchsinger, C., et al. (2025) · eLife · doi:10.7554/elife.103725.2
Hudait, A., Burdick, R. C., Bare, E. K., Pathak, V. K., & Voth, G. A. (2025) · eLife · doi:10.7554/elife.109282.1
Stoichiometric Binding of Cyclophilin‐A to The HIV‐1 Capsid Modulates Its Mechanoelastic Properties
Rey, J. S., Bryer, A. J., & Perilla, J. R. (2026) · Small · doi:10.1002/smll.75453
Hudait, A., Burdick, R. C., Bare, E. K., Pathak, V. K., & Voth, G. A. (2026) · eLife · doi:10.7554/elife.109282.2
Caractérisation des activités antivirales des anticorps anti-VIH-1 et anti-SARS-CoV-2
Dufloo, J. (2021) · theses.fr (ABES) · doi:10.70675/215798eaz7f82z4e57za8eazf4453d37b8c8
Bonaventure, B. (2020) · theses.fr (ABES) · doi:10.70675/768c3190z3177z4b25z88b9z9a029e425462
Identification of specific phylogenetic properties of HIV-1 M and O integrases
Toccafondi, E. (2022) · theses.fr (ABES) · doi:10.70675/2facab6ezc20az472dz8350z9fb6e718e1d4 · Cited by 1
Metadata
- 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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