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The HIV-1 capsid core is an opportunistic nuclear import receptor

Author

Listed:
  • Guangai Xue

    (Model Development Section, Cancer Innovation Laboratory, National Cancer Institute)

  • Hyun Jae Yu

    (Basic Science Program, Leidos Biomedical Research, Frederick National Laboratory)

  • Cindy Buffone

    (Albert Einstein College of Medicine)

  • Szu-Wei Huang

    (Model Development Section, Cancer Innovation Laboratory, National Cancer Institute)

  • KyeongEun Lee

    (Model Development Section, Cancer Innovation Laboratory, National Cancer Institute)

  • Shih Lin Goh

    (University of Massachusetts Medical School)

  • Anna T. Gres

    (University of Missouri)

  • Mehmet Hakan Guney

    (University of Massachusetts Medical School)

  • Stefan G. Sarafianos

    (University of Missouri
    University of Missouri
    Emory University School of Medicine)

  • Jeremy Luban

    (University of Massachusetts Medical School)

  • Felipe Diaz-Griffero

    (Albert Einstein College of Medicine)

  • Vineet N. KewalRamani

    (Model Development Section, Cancer Innovation Laboratory, National Cancer Institute)

Abstract

The movement of viruses and other large macromolecular cargo through nuclear pore complexes (NPCs) is poorly understood. The human immunodeficiency virus type 1 (HIV-1) provides an attractive model to interrogate this process. HIV-1 capsid (CA), the chief structural component of the viral core, is a critical determinant in nuclear transport of the virus. HIV-1 interactions with NPCs are dependent on CA, which makes direct contact with nucleoporins (Nups). Here we identify Nup35, Nup153, and POM121 to coordinately support HIV-1 nuclear entry. For Nup35 and POM121, this dependence was dependent cyclophilin A (CypA) interaction with CA. Mutation of CA or removal of soluble host factors changed the interaction with the NPC. Nup35 and POM121 make direct interactions with HIV-1 CA via regions containing phenylalanine glycine motifs (FG-motifs). Collectively, these findings provide additional evidence that the HIV-1 CA core functions as a macromolecular nuclear transport receptor (NTR) that exploits soluble host factors to modulate NPC requirements during nuclear invasion.

Suggested Citation

  • Guangai Xue & Hyun Jae Yu & Cindy Buffone & Szu-Wei Huang & KyeongEun Lee & Shih Lin Goh & Anna T. Gres & Mehmet Hakan Guney & Stefan G. Sarafianos & Jeremy Luban & Felipe Diaz-Griffero & Vineet N. Ke, 2023. "The HIV-1 capsid core is an opportunistic nuclear import receptor," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-39146-5
    DOI: 10.1038/s41467-023-39146-5
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    References listed on IDEAS

    as
    1. Ashwanth C. Francis & Mariana Marin & Parmit K. Singh & Vasudevan Achuthan & Mathew J. Prellberg & Kristina Palermino-Rowland & Shuiyun Lan & Philip R. Tedbury & Stefan G. Sarafianos & Alan N. Engelma, 2020. "Publisher Correction: HIV-1 replication complexes accumulate in nuclear speckles and integrate into speckle-associated genomic domains," Nature Communications, Nature, vol. 11(1), pages 1-1, December.
    2. Guochao Wei & Naseer Iqbal & Valentine V. Courouble & Ashwanth C. Francis & Parmit K. Singh & Arpa Hudait & Arun S. Annamalai & Stephanie Bester & Szu-Wei Huang & Nikoloz Shkriabai & Lorenzo Briganti , 2022. "Prion-like low complexity regions enable avid virus-host interactions during HIV-1 infection," Nature Communications, Nature, vol. 13(1), pages 1-19, December.
    3. Ashwanth C. Francis & Mariana Marin & Parmit K. Singh & Vasudevan Achuthan & Mathew J. Prellberg & Kristina Palermino-Rowland & Shuiyun Lan & Philip R. Tedbury & Stefan G. Sarafianos & Alan N. Engelma, 2020. "HIV-1 replication complexes accumulate in nuclear speckles and integrate into speckle-associated genomic domains," Nature Communications, Nature, vol. 11(1), pages 1-17, December.
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    Cited by:

    1. Alex Kleinpeter & Donna L. Mallery & Nadine Renner & Anna Albecka & J. Ole Klarhof & Eric O. Freed & Leo C. James, 2024. "HIV-1 adapts to lost IP6 coordination through second-site mutations that restore conical capsid assembly," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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