Capsid-CPSF6 Interaction Licenses Nuclear HIV-1 Trafficking to Sites of Viral DNA Integration
Open accessAbstract
HIV-1 integration into the host genome favors actively transcribed genes. Prior work indicated that the nuclear periphery provides the architectural basis for integration site selection, with viral capsid-binding host cofactor CPSF6 and viral integrase-binding cofactor LEDGF/p75 contributing to selection of individual sites. Here, by investigating the early phase of infection, we determine that HIV-1 traffics throughout the nucleus for integration. CPSF6-capsid interactions allow the virus to bypass peripheral heterochromatin and penetrate the nuclear structure for integration. Loss of interaction with CPSF6 dramatically alters virus localization toward the nuclear periphery and integration into transcriptionally repressed lamina-associated heterochromatin, while loss of LEDGF/p75 does not significantly affect intranuclear HIV-1 localization. Thus, CPSF6 serves as a master regulator of HIV-1 intranuclear localization by trafficking viral preintegration complexes away from heterochromatin at the periphery toward gene-dense chromosomal regions within the nuclear interior.
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In CPSF6 knockout cells, pre-integration complexes congregate at the nuclear periphery and target LADs for integration while losing the preference for SPADs.
“In CPSF6 knockout cells, PICs congregated at the nuclear periphery and uncharacteristically targeted LADs for integration while losing the preference for SPADs84,85.”
From Structure and function of retroviral integrase (2022) · cites this paper as [85]
The Results sections on intranuclear localization and LAD integration report that PIC-associated signals were enriched at the nuclear periphery in CPSF6-knockout cells and that LADs became preferred integration targets. Our copy does not report SPAD integration targeting or establish a loss of SPAD preference; its Discussion mentions trafficking to speckles but not that specific result. Page numbers are unavailable in the indexed copy. (LLM, conf=0.88)
Experimental — accuracy not yet measuredCPSF6 facilitates targeting of HIV-1 PICs to transcriptionally active regions of the genome found deep within the center of the nucleus.
“Another important host factor identified in retroviral integration is CPSF6 that facilitates targeting of the HIV-1 PICs to transcriptionally active regions of the genome found deep within the center of the nucleus (Rasheedi et al. 2016, Achuthan et al. 2018, Singh et al. 2022a).”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Achuthan et al. 2018
The Introduction and Discussion say CPSF6 helps HIV-1 PICs bypass peripheral heterochromatin and reach transcriptionally active, gene-dense regions in the nuclear interior. But the claim’s placement of those regions deep in the nuclear center is too specific: the Results report avoidance of the central nuclear zone under one set of experimental conditions (page unavailable in our copy). (LLM, conf=0.88)
Experimental — accuracy not yet measuredCPSF6 plays a critical role in regulating nuclear pre-integration complex incursion.
“In addition to its role in nuclear import, CPSF6 plays a critical role in regulating nuclear PIC incursion.”
From Structure and function of retroviral integrase (2022) · cites this paper as [85]
CA facilitates HIV-1 integration into transcriptionally active, gene-rich regions via interacting with CPSF, which helps connect the PIC to intranuclear trafficking pathways to facilitate entry into the inner regions of the nucleus.
“Further evidence shows that CA facilitates HIV-1 integration into transcriptionally active, gene-rich regions via interacting with CPSF that in fact helps connect the PIC to intranuclear trafficking pathways to facilitate entry into the inner regions of the nucleus (Chin et al. 2015, Achuthan et al. 2018).”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Achuthan et al. 2018
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Distinct viral reservoirs in individuals with spontaneous control of HIV-1
Jiang, C., Lian, X., Gao, C., Sun, X., Einkauf, K. B., Chevalier, J. M., Chen, S. M. Y., Hua, S., Rhee, B. S., Chang, K., et al. (2020) · Nature · doi:10.1038/s41586-020-2651-8 · Cited by 387 · see citing works
Self-citationCone-shaped HIV-1 capsids are transported through intact nuclear pores
Žíla, V., Margiotta, E., Turoňová, B., Müller, T. G., Zimmerli, C. E., Mattei, S., Allegretti, M., Börner, K., Rada, J., Müller, B., et al. (2021) · Cell · doi:10.1016/j.cell.2021.01.025 · Cited by 333 · see citing works
HIV-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 · see citing works
“Some previous studies have suggested that low levels of CA are associated with nuclear complexes (14, 15, 17, 19, 20, 22) and are thought to influence integration site selection (23, 24); in these studies, the nuclear CA amounts may have been underestimated because of reduced CA epitope accessibility (25).”
BackgroundInfluentialParallel analysis of transcription, integration, and sequence of single HIV-1 proviruses
Einkauf, K. B., Osborn, M. R., Gao, C., Sun, W., Sun, X., Lian, X., Parsons, E. M., Gladkov, G. T., Seiger, K. W., Blackmer, J. E., et al. (2022) · Cell · doi:10.1016/j.cell.2021.12.011 · Cited by 260 · see citing works
Structural and mechanistic bases for a potent HIV-1 capsid inhibitor
Bester, S. M., Wei, G., Zhao, H., Adu‐Ampratwum, D., Iqbal, N., Courouble, V. V., Francis, A. C., Annamalai, A. S., Singh, P. K., Shkriabai, N., et al. (2020) · Science · doi:10.1126/science.abb4808 · Cited by 244 · see citing works
Self-citationDharan, A., Bachmann, N., Talley, S., Zwikelmaier, V., & Campbell, E. M. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0735-8 · Cited by 223 · see citing works
Bejarano, D. A., Peng, K., Laketa, V., Börner, K., Jost, K. L., Lucic, B., Glass, B., Lusic, M., Müller, B., & Kräusslich, H.-G. (2019) · eLife · doi:10.7554/elife.41800 · Cited by 197 · see citing works
Block-And-Lock Strategies to Cure HIV Infection
Vansant, G., Bruggemans, A., Janssens, J., & Debyser, Z. (2020) · Viruses · doi:10.3390/v12010084 · Cited by 169 · see citing works
HIV-1 cores retain their integrity until minutes before uncoating in the nucleus
Li, C., Burdick, R. C., Nagashima, K., Hu, W.-S., & Pathak, V. K. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2019467118 · Cited by 157 · see citing works
Francis, A. C., Marin, M., Singh, P. K., Achuthan, V., Prellberg, M. J., Palermino-Rowland, K., Lan, S., Tedbury, P. R., Sarafianos, S. G., Engelman, A. N., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17256-8 · Cited by 159 · see citing works
Self-citationStructure and function of retroviral integrase
Maertens, G. N., Engelman, A. N., & Cherepanov, P. (2022) · Nature Reviews Microbiology · doi:10.1038/s41579-021-00586-9 · Cited by 124 · see citing works
Self-citationMüller, T. G., Žíla, V., Peters, K., Schifferdecker, S., Stanić, M., Lucic, B., Laketa, V., Lušić, M., Müller, B., & Kräusslich, H. (2021) · eLife · doi:10.7554/elife.64776 · Cited by 117 · see citing works
Spatially clustered loci with multiple enhancers are frequent targets of HIV-1 integration
Lucic, B., Chen, H., Kuzman, M., Zorita, E. V., Wegner, J., Minneker, V., Wang, W., Fronza, R., Laufs, S., Schmidt, M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12046-3 · Cited by 106 · see citing works
Multiple Roles of HIV-1 Capsid during the Virus Replication Cycle
Novikova, M., Zhang, Y., Freed, E. O., & Peng, K. (2019) · Virologica Sinica · doi:10.1007/s12250-019-00095-3 · Cited by 95 · see citing works
HIV-1 Maturation: Lessons Learned from Inhibitors
Kleinpeter, A. B., & Freed, E. O. (2020) · Viruses · doi:10.3390/v12090940 · Cited by 95 · see citing works
Nuclear Capsid Uncoating and Reverse Transcription of HIV-1
Müller, T. G., Žíla, V., Müller, B., & Kräusslich, H. (2022) · Annual Review of Virology · doi:10.1146/annurev-virology-020922-110929 · Cited by 94 · see citing works
Clustering and reverse transcription of HIV‐1 genomes in nuclear niches of macrophages
Rensen, E., Mueller, F., Scoca, V., Parmar, J. J., Souque, P., Zimmer, C., & Nunzio, F. D. (2020) · The EMBO Journal · doi:10.15252/embj.2020105247 · Cited by 91 · see citing works
Remodeling of the Core Leads HIV-1 Preintegration Complex into the Nucleus of Human Lymphocytes
Blanco-Rodriguez, G., Gazi, A. D., Monel, B., Frabetti, S., Scoca, V., Mueller, F., Schwartz, O., Krijnse‐Locker, J., Charneau, P., & Nunzio, F. D. (2020) · Journal of Virology · doi:10.1128/jvi.00135-20 · Cited by 89 · see citing works
Structure, Function, and Interactions of the HIV-1 Capsid Protein
Rossi, E., Meuser, M. E., Cunanan, C. J., & Cocklin, S. (2021) · Life · doi:10.3390/life11020100 · Cited by 87 · see citing works
HIV-1 capsids enter the FG phase of nuclear pores like a transport receptor
Fu, L., Weiskopf, E. N., Akkermans, O., Swanson, N. A., Cheng, S., Schwartz, T., & Görlich, D. (2024) · Nature · doi:10.1038/s41586-023-06966-w · Cited by 81 · see citing works
The HIV capsid mimics karyopherin engagement of FG-nucleoporins
Dickson, C. F., Hertel, S., Tuckwell, A., Li, N., Ruan, J., Al-Izzi, S. C., Ariotti, N., Sierecki, E., Gambin, Y., Morris, R. G., et al. (2024) · Nature · doi:10.1038/s41586-023-06969-7 · Cited by 85 · see citing works
Tang, L., Sheraz, M. A., McGrane, M., Chang, J., & Guo, J. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1007742 · Cited by 84 · see citing works
The chromatin landscape at the HIV-1 provirus integration site determines viral expression
Vansant, G., Chen, H., Zorita, E. V., Trejbalová, K., Miklík, D., Filion, G. J. P., & Debyser, Z. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa536 · Cited by 73 · see citing works
Multifaceted HIV integrase functionalities and therapeutic strategies for their inhibition
Engelman, A. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.006901 · Cited by 78 · see citing works
Self-citationRotten to the core: antivirals targeting the HIV-1 capsid core
McFadden, W. M., Snyder, A. A., Kirby, K. A., Tedbury, P. R., Raj, M., Wang, Z., & Sarafianos, S. G. (2021) · Retrovirology · doi:10.1186/s12977-021-00583-z · Cited by 65 · see citing works
Self-citationLi, W., Singh, P. K., Sowd, G. A., Bedwell, G. J., Jang, S., Achuthan, V., Oleru, A. V., Wong, D., Fadel, H. J., Lee, K., et al. (2020) · mBio · doi:10.1128/mbio.02254-20 · Cited by 64 · see citing works
Self-citationZhong, Z., Ning, J., Boggs, E. A., Jang, S., Wallace, C. T., Telmer, C. A., Bruchez, M. P., Ahn, J., Engelman, A., Zhang, P., et al. (2021) · mBio · doi:10.1128/mbio.03142-20 · Cited by 59 · see citing works
Self-citationTRIM34 restricts HIV-1 and SIV capsids in a TRIM5α-dependent manner
OhAinle, M., Kim, K., Keceli, S. K., Felton, A., Campbell, E., Luban, J., & Emerman, M. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008507 · Cited by 58 · see citing works
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Self-citationHIV capsid and integration targeting
Engelman, A. N. (2021) · Viruses · doi:10.3390/v13010125 · Cited by 57 · see citing works
Self-citationBalasubramaniam, M., Pandhare, J., & Dash, C. (2019) · JoLS Journal of Life Sciences · doi:10.36069/jols/20190603 · Cited by 53 · see citing works
Francis, A. C., Marin, M., Prellberg, M., Palermino-Rowland, K., & Melikyan, G. B. (2020) · Viruses · doi:10.3390/v12111234 · Cited by 51 · see citing works
Zhuang, S., & Torbett, B. E. (2021) · Viruses · doi:10.3390/v13030417 · Cited by 51 · see citing works
Prion-like low complexity regions enable avid virus-host interactions during HIV-1 infection
Wei, G., Iqbal, N., Courouble, V. V., Francis, A. C., Singh, P. K., Hudait, A., Annamalai, A. S., Bester, S. M., Huang, S., Shkriabai, N., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33662-6 · Cited by 55 · see citing works
Self-citationShen, Q., Wu, C., Freniere, C., Tripler, T. N., & Xiong, Y. (2021) · Viruses · doi:10.3390/v13112242 · Cited by 50 · see citing works
The cell biology of HIV-1 latency and rebound
Mbonye, U. R., & Karn, J. (2024) · Retrovirology · doi:10.1186/s12977-024-00639-w · Cited by 51 · see citing works
HIV-1 requires capsid remodelling at the nuclear pore for nuclear entry and integration
Guedán, A., Donaldson, C. D., Caroe, E. R., Cosnefroy, O., Taylor, I., & Bishop, K. N. (2021) · bioRxiv · doi:10.1371/journal.ppat.1009484 · Cited by 47 · see citing works
Machida, S., Depierre, D., Chen, H., Thenin-Houssier, S., Petitjean, G., Doyen, C. M., Takaku, M., Cuvier, O., & Benkirane, M. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1913754117 · Cited by 46 · see citing works
HIV-induced membraneless organelles orchestrate post-nuclear entry steps
Scoca, V., Morin, R., Collard, M., Tinévez, J.-Y., & Nunzio, F. D. (2022) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjac060 · Cited by 48 · see citing works
Wells, D., Guo, S., Shao, W., Bale, M. J., Coffin, J. M., Hughes, S. H., & Wu, X. (2020) · BMC Genomics · doi:10.1186/s12864-020-6647-4 · Cited by 45 · see citing works
Self-citationCapsid-Labelled HIV To Investigate the Role of Capsid during Nuclear Import and Integration
Zurnic, I., Dirix, L., Lemmens, V., Borrenberghs, D., Wit, F. D., Vernaillen, F., Rocha, S., Christ, F., Hendrix, J., Hofkens, J., et al. (2020) · Journal of Virology · doi:10.1128/jvi.01024-19 · Cited by 44 · see citing works
Lau, C., Adan, M. A., & Maldarelli, F. M. (2021) · Viruses · doi:10.3390/v13122512 · Cited by 44 · see citing works
Rodríguez-Mora, S., Wit, F. D., García‐Pérez, J., Bermejo, M., López‐Huertas, M. R., Mateos, E., Martí, P., Rocha, S., Vigón, L., Christ, F., et al. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1007958 · Cited by 42 · see citing works
Lenacapavir: A novel injectable HIV-1 capsid inhibitor
Hitchcock, A. M., Kufel, W. D., Dwyer, K. A. M., & Sidman, E. F. (2024) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2023.107009 · Cited by 43 · see citing works
Factors that mold the nuclear landscape of HIV-1 integration
Bedwell, G. J., & Engelman, A. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1207 · Cited by 40 · see citing works
Self-citationA snapshot of HIV-1 capsid–host interactions
Temple, J. E., Tripler, T. N., Shen, Q., & Xiong, Y. (2020) · Current Research in Structural Biology · doi:10.1016/j.crstbi.2020.10.002 · Cited by 41 · see citing works
HIV-1 uncoating requires long double-stranded reverse transcription products
Burdick, R. C., Morse, M., Rouzina, I. F., Williams, M. C., Hu, W.-S., & Pathak, V. K. (2024) · Science Advances · doi:10.1126/sciadv.adn7033 · Cited by 41 · see citing works
Analysis of CA Content and CPSF6 Dependence of Early HIV-1 Replication Complexes in SupT1-R5 Cells
Žíla, V., Müller, T. G., Laketa, V., Müller, B., & Kräusslich, H. (2019) · mBio · doi:10.1128/mbio.02501-19 · Cited by 41 · see citing works
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HIV-1 capsid variability: viral exploitation and evasion of capsid-binding molecules
Saito, A., & Yamashita, M. (2021) · Retrovirology · doi:10.1186/s12977-021-00577-x · Cited by 39 · see citing works
Capsid–host interactions for HIV-1 ingress
Jang, S., & Engelman, A. (2023) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00048-22 · Cited by 37 · see citing works
Self-citationElasticity of the HIV-1 core facilitates nuclear entry and infection
Deshpande, A., Bryer, A. J., Andino-Moncada, J. R., Shi, J., Hong, J., Torres, C. M., Harel, S., Francis, A. C., Perilla, J. R., Aiken, C., et al. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1012537 · Cited by 38 · see citing works
The HIV-1 Viral Protease Is Activated during Assembly and Budding Prior to Particle Release
Tabler, C. O., Wegman, S. J., Chen, J., Shroff, H., Alhusaini, N., & Tilton, J. C. (2022) · Journal of Virology · doi:10.1128/jvi.02198-21 · Cited by 38 · see citing works
Hou, Z., Shen, Y., Fronik, S., Shen, J., Shi, J., Xu, J., Chen, L., Hardenbrook, N. J., Thompson, C., Neumann, S., et al. (2025) · Nature Microbiology · doi:10.1038/s41564-025-02054-z · Cited by 35 · see citing works
Self-citationWang, L., Casey, M. C., Vernekar, S. K. V., Sahani, R. L., Kirby, K. A., Du, H., Zhang, H., Tedbury, P. R., Xie, J., Sarafianos, S. G., et al. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.07.016 · Cited by 34 · see citing works
Self-citationStrategies for Targeting Retroviral Integration for Safer Gene Therapy: Advances and Challenges
Yoder, K. E., Rabe, A. J., Fishel, R. A., & Larue, R. C. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.662331 · Cited by 34 · see citing works
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Impact of LEDGIN treatment during virus production on residual HIV-1 transcription
Vansant, G., Vranckx, L. S., Zurnic, I., Looveren, D. V., de Velde, P. V., Nobles, C. L., Gijsbers, R., Christ, F., & Debyser, Z. (2019) · Retrovirology · doi:10.1186/s12977-019-0472-3 · Cited by 33 · see citing works
How HIV-1 Gag Manipulates Its Host Cell Proteins: A Focus on Interactors of the Nucleocapsid Domain
Klingler, J., Anton, H., Réal, É., Zeiger, M., Moog, C., Mély, Y., & Boutant, E. (2020) · Viruses · doi:10.3390/v12080888 · Cited by 34 · see citing works
HIV-1 Capsid Core: A Bullet to the Heart of the Target Cell
Toccafondi, E., Lener, D., & Negroni, M. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.652486 · Cited by 33 · see citing works
Toward Structurally Novel and Metabolically Stable HIV-1 Capsid-Targeting Small Molecules
Vernekar, S. K. V., Sahani, R. L., Casey, M. C., Kankanala, J., Wang, L., Kirby, K. A., Du, H., Zhang, H., Tedbury, P. R., Xie, J., et al. (2020) · Viruses · doi:10.3390/v12040452 · Cited by 32 · see citing works
Self-citationSpatial and Genomic Correlates of HIV-1 Integration Site Targeting
Singh, P. K., Bedwell, G. J., & Engelman, A. (2022) · Cells · doi:10.3390/cells11040655 · Cited by 34 · see citing works
Self-citationJanssens, J., De Wit, F., Parveen, N., & Debyser, Z. (2022) · mBio · doi:10.1128/mbio.00007-22 · Cited by 28 · see citing works
Bedwell, G. J., Jang, S., Li, W., Singh, P. K., & Engelman, A. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab514 · Cited by 28 · see citing works
Self-citationThe Role of Capsid in HIV-1 Nuclear Entry
Guedán, A., Caroe, E. R., Barr, G., & Bishop, K. N. (2021) · Viruses · doi:10.3390/v13081425 · Cited by 26 · see citing works
HIV-1 capsid and viral DNA integration
Dwivedi, R., Prakash, P., Kumbhar, B. V., Balasubramaniam, M., & Dash, C. (2023) · mBio · doi:10.1128/mbio.00212-22 · Cited by 30 · see citing works
Sim, D. Y., Lee, H., Ahn, C., Park, J.-E., Park, S., Kil, B. J., Shim, B., Kim, B., & Kim, S.-H. (2024) · International Journal of Biological Sciences · doi:10.7150/ijbs.93462 · Cited by 29 · see citing works
Gifford, L. B., & Melikyan, G. B. (2024) · ACS Nano · doi:10.1021/acsnano.3c07678 · Cited by 28 · see citing works
Novel HIV-1 capsid-targeting small molecules of the PF74 binding site
Wang, L., Casey, M. C., Vernekar, S. K. V., Sahani, R. L., Kankanala, J., Kirby, K. A., Du, H., Hachiya, A., Zhang, H., Tedbury, P. R., et al. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112626 · Cited by 27 · see citing works
Self-citationJang, S., Bedwell, G. J., SINGH, S. P., Yu, H. J., Arnarson, B., Singh, P. K., Radhakrishnan, R., Douglas, A. W., Ingram, Z., Freniere, C., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae769 · Cited by 24 · see citing works
Self-citationChintala, K., Mohareer, K., & Banerjee, S. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.716927 · Cited by 23 · see citing works
Clonal Expansion of Infected CD4+ T Cells in People Living with HIV
Coffin, J. M., & Hughes, S. H. (2021) · Viruses · doi:10.3390/v13102078 · Cited by 24 · see citing works
Self-citationCryo-electron Microscopy Reveals the Structure of the Nuclear Pore Complex
Tai, L., Yin, G., Sun, F., & Zhu, Y. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168051 · Cited by 24 · see citing works
Localization and functions of native and eGFP-tagged capsid proteins in HIV-1 particles
Francis, A. C., Cereseto, A., Singh, P. K., Shi, J., Poeschla, E. M., Engelman, A., Aiken, C., & Melikyan, G. B. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010754 · Cited by 24 · see citing works
Self-citationAnderson-Daniels, J., Singh, P. K., Sowd, G. A., Li, W., Engelman, A., & Aiken, C. (2019) · Journal of Virology · doi:10.1128/jvi.01118-19 · Cited by 23 · see citing works
Self-citationStructural and mechanistic bases for resistance of the M66I capsid variant to lenacapavir
Briganti, L., Annamalai, A. S., Bester, S. M., Wei, G., Andino-Moncada, J. R., Singh, S. P., Kleinpeter, A. B., Tripathi, M., Nguyen, B., Radhakrishnan, R., et al. (2025) · mBio · doi:10.1128/mbio.03613-24 · Cited by 23 · see citing works
Self-citationHIV Capsid Inhibitors Beyond PF74
McArthur, C. P., Gallazzi, F., Quinn, T. P., & Singh, K. (2019) · Diseases · doi:10.3390/diseases7040056 · Cited by 23 · see citing works
Bonnet, A., & Lesage, P. (2021) · Current Genetics · doi:10.1007/s00294-021-01154-7 · Cited by 21 · see citing works
The Role of Capsid in the Early Steps of HIV-1 Infection: New Insights into the Core of the Matter
AlBurtamani, N., Paul, A., & Fassati, A. (2021) · Viruses · doi:10.3390/v13061161 · Cited by 20 · see citing works
Capsid-CPSF6 interaction: Master regulator of nuclear HIV-1 positioning and integration
Achuthan, V., Perreira, J. M., Ahn, J. J., Brass, A. L., & Engelman, A. (2019) · JoLS Journal of Life Sciences · doi:10.36069/jols/20190604 · Cited by 22 · see citing works
Self-citationAy, S., & Nunzio, F. D. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168094 · Cited by 20 · see citing works
Fluorescence Biosensor for Real-Time Interaction Dynamics of Host Proteins with HIV-1 Capsid Tubes
Lau, D., Walsh, J. C., Peng, W., Shah, V. B., Turville, S. G., Jacques, D. A., & Böcking, T. (2019) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.9b08521 · Cited by 20 · see citing works
Sahani, R. L., Diana‐Rivero, R., Vernekar, S. K. V., Wang, L., Du, H., Zhang, H., Castaner, A. E., Casey, M. C., Kirby, K. A., Tedbury, P. R., et al. (2021) · Viruses · doi:10.3390/v13030479 · Cited by 20 · see citing works
Self-citationComplex Relationships between HIV-1 Integrase and Its Cellular Partners
Rozina, A., Anisenko, A., Kikhai, T., Silkina, M., & Gottikh, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012341 · Cited by 18 · see citing works
MxB sensitivity of HIV-1 is determined by a highly variable and dynamic capsid surface
Miles, R. J., Kerridge, C., Hilditch, L., Monit, C., Jacques, D. A., & Towers, G. J. (2020) · eLife · doi:10.7554/elife.56910 · Cited by 19 · see citing works
The HIV-1 Capsid: From Structural Component to Key Factor for Host Nuclear Invasion
Scoca, V., & Nunzio, F. D. (2021) · Viruses · doi:10.3390/v13020273 · Cited by 19 · see citing works
Visualizing HIV-1 Capsid and Its Interactions with Antivirals and Host Factors
Wilbourne, M., & Zhang, P. (2021) · Viruses · doi:10.3390/v13020246 · Cited by 20 · see citing works
HIV-1 CA Inhibitors Are Antagonized by Inositol Phosphate Stabilization of the Viral Capsid in Cells
Sowd, G. A., Shi, J., & Aiken, C. (2021) · Journal of Virology · doi:10.1128/jvi.01445-21 · Cited by 19 · see citing works
Self-citationTeaching old dogmas new tricks: recent insights into the nuclear import of HIV-1
Dharan, A., & Campbell, E. M. (2022) · Current Opinion in Virology · doi:10.1016/j.coviro.2022.101203 · Cited by 18 · see citing works
Antiretroviral APOBEC3 cytidine deaminases alter HIV-1 provirus integration site profiles
Ajoge, H. O., Renner, T. M., Bélanger, K., Greig, M., Dankar, S. K., Kohio, H. P., Coleman, M. D., Ndashimye, E., Arts, E. J., Langlois, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-022-35379-y · Cited by 18 · see citing works
Ingram, Z., Kline, C. E., Hughson, A. K., Singh, P. K., Fischer, H. L., Radhakrishnan, R., Sowd, G. A., dos Santos, N. F. B., Ganser‐Pornillos, B. K., Watkins, S. C., et al. (2025) · mBio · doi:10.1128/mbio.00169-25 · Cited by 16 · see citing works
Self-citationChaudhuri, E., Dash, S., Balasubramaniam, M., Padron, A., Holland, J., Sowd, G. A., Villalta, F., Engelman, A., Pandhare, J., & Dash, C. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010534 · Cited by 18 · see citing works
Self-citationDebyser, Z., Bruggemans, A., Belle, S. V., Janssens, J., & Christ, F. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-981-16-0267-2_4 · Cited by 17 · see citing works
Entry of hepatitis B virus: going beyond NTCP to the nucleus
Tian, J., Li, C., & Li, W. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.08.001 · Cited by 17 · see citing works
Exploring HIV-1 Maturation: A New Frontier in Antiviral Development
McGraw, A., Hillmer, G., Mehedincu, S. M., Hikichi, Y., Gagliardi, S., Narayan, K., Tibebe, H., Marquez, D., Bose, L. M., Keating, A., et al. (2024) · Viruses · doi:10.3390/v16091423 · Cited by 17 · see citing works
Towards a Functional Cure of HIV-1: Insight Into the Chromatin Landscape of the Provirus
Janssens, J., Bruggemans, A., Christ, F., & Debyser, Z. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.636642 · Cited by 17 · see citing works
Retroviral integrase: Structure, mechanism, and inhibition
Passos, D. O., Li, M., Craigie, R., & Lyumkis, D. (2021) · The Enzymes · doi:10.1016/bs.enz.2021.06.007 · Cited by 18 · see citing works
Cell-free assays reveal that the HIV-1 capsid protects reverse transcripts from cGAS immune sensing
Scott, T. M., Arnold, L. M., Powers, J. A., McCann, D., Rowe, A. B., Christensen, D. E., Pereira, M. J. B., Zhou, W., Torrez, R. M., Iwasa, J., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1012206 · Cited by 16 · see citing works
Sowd, G. A., Shi, J., Fulmer, A. N., & Aiken, C. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011423 · Cited by 16 · see citing works
Self-citationEmerging role of cyclophilin A in HIV-1 infection: from producer cell to the target cell nucleus
Padron, A., Prakash, P., Pandhare, J., Luban, J., Aiken, C., Balasubramaniam, M., & Dash, C. (2023) · Journal of Virology · doi:10.1128/jvi.00732-23 · Cited by 15 · see citing works
- Authors
- Achuthan, V., Perreira, J. M., Sowd, G. A., Puray-Chavez, M., McDougall, W. M., Paulucci-Holthauzen, A., Wu, X., Fadel, H. J., Poeschla, E. M., Multani, A. S., Hughes, S. H., Sarafianos, S. G., Brass, A. L., & Engelman, A. N.
- Affiliations
- Harvard University (US)
- University of Massachusetts Chan Medical School (US)
- The University of Texas MD Anderson Cancer Center (US)
- Leidos Biomedical Research Inc. (United States) (US)
- Mayo Clinic (US)
- University of Colorado Anschutz (US)
- National Cancer Institute (US)
- University of Missouri (US)
- Corresponding author
- Brass, Abraham L.
- Engelman, Alan N.
- ORCID
- Venue
- Cell Host & Microbe
- Publisher
- Elsevier BV
- Published
- 2018-09
- Volume
- 24
- Issue
- 3
- Pages
- 392-404.e8
- ISSN
- 1931-3128 (ISSN-L)
- PMC
- PMC6368089
- OpenAlex
- W2889370079
- Cited by
- 205
- References
- 78
- Citations by year
- 2026: 17 · 2025: 26 · 2024: 33 · 2023: 20 · 2022: 22 · 2021: 34 · 2020: 29 · 2019: 22 · 2018: 2
- FWCI
- 11.39
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Host & Microbe (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- NIH (R01 AI052014, R01 AI077344, P30 AI060354, T32 AI007245)
- NCI
- Bill and Melinda Gates Foundation (OPP1097381)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Virus-based gene therapy research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- HIV-1, capsid, CPSF6, LEDGF/p75, preintegration complex, nuclear trafficking, heterochromatin, nuclear periphery, viral DNA integration, host cofactors
- MeSH terms
- Capsid, Cell Nucleus, DNA, Viral, Humans, Protein Binding, Virus Replication, HIV-1, HIV Infections, Virus Integration, Intercellular Signaling Peptides and Proteins, mRNA Cleavage and Polyadenylation Factors, Host-Pathogen Interactions
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