IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v418y2002i6898d10.1038_nature00939.html
   My bibliography  Save this article

Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein

Author

Listed:
  • Ann M. Sheehy

    (University of Pennsylvania School of Medicine)

  • Nathan C. Gaddis

    (University of Pennsylvania School of Medicine)

  • Jonathan D. Choi

    (The Children's Hospital of Philadelphia)

  • Michael H. Malim

    (University of Pennsylvania School of Medicine
    Guy's, King's and St Thomas' School of Medicine, King's College London)

Abstract

Viruses have developed diverse non-immune strategies to counteract host-mediated mechanisms that confer resistance to infection. The Vif (virion infectivity factor) proteins are encoded by primate immunodeficiency viruses, most notably human immunodeficiency virus-1 (HIV-1). These proteins are potent regulators of virus infection and replication and are consequently essential for pathogenic infections in vivo1,2,3,4,5,6. HIV-1 Vif seems to be required during the late stages of virus production3,6 for the suppression of an innate antiviral phenotype that resides in human T lymphocytes7,8. Thus, in the absence of Vif, expression of this phenotype renders progeny virions non-infectious. Here, we describe a unique cellular gene, CEM15, whose transient or stable expression in cells that do not normally express CEM15 recreates this phenotype, but whose antiviral action is overcome by the presence of Vif. Because the Vif:CEM15 regulatory circuit is critical for HIV-1 replication, perturbing the circuit may be a promising target for future HIV/AIDS therapies.

Suggested Citation

  • Ann M. Sheehy & Nathan C. Gaddis & Jonathan D. Choi & Michael H. Malim, 2002. "Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein," Nature, Nature, vol. 418(6898), pages 646-650, August.
  • Handle: RePEc:nat:nature:v:418:y:2002:i:6898:d:10.1038_nature00939
    DOI: 10.1038/nature00939
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature00939
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.

    File URL: https://libkey.io/10.1038/nature00939?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Diako Ebrahimi & Hamid Alinejad-Rokny & Miles P Davenport, 2014. "Insights into the Motif Preference of APOBEC3 Enzymes," PLOS ONE, Public Library of Science, vol. 9(1), pages 1-9, January.
    2. Hannah O. Ajoge & Tyler M. Renner & Kasandra Bélanger & Matthew Greig & Samar Dankar & Hinissan P. Kohio & Macon D. Coleman & Emmanuel Ndashimye & Eric J. Arts & Marc-André Langlois & Stephen D. Barr, 2023. "Antiretroviral APOBEC3 cytidine deaminases alter HIV-1 provirus integration site profiles," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    3. Atanu Maiti & Adam K. Hedger & Wazo Myint & Vanivilasini Balachandran & Jonathan K. Watts & Celia A. Schiffer & Hiroshi Matsuo, 2022. "Structure of the catalytically active APOBEC3G bound to a DNA oligonucleotide inhibitor reveals tetrahedral geometry of the transition state," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    4. Fumiaki Ito & Ana L. Alvarez-Cabrera & Kyumin Kim & Z. Hong Zhou & Xiaojiang S. Chen, 2023. "Structural basis of HIV-1 Vif-mediated E3 ligase targeting of host APOBEC3H," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    5. Hanjing Yang & Kyumin Kim & Shuxing Li & Josue Pacheco & Xiaojiang S. Chen, 2022. "Structural basis of sequence-specific RNA recognition by the antiviral factor APOBEC3G," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    6. Joseph Hiatt & Judd F. Hultquist & Michael J. McGregor & Mehdi Bouhaddou & Ryan T. Leenay & Lacy M. Simons & Janet M. Young & Paige Haas & Theodore L. Roth & Victoria Tobin & Jason A. Wojcechowskyj & , 2022. "A functional map of HIV-host interactions in primary human T cells," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    7. Vanessa B Soros & Wes Yonemoto & Warner C Greene, 2007. "Newly Synthesized APOBEC3G Is Incorporated into HIV Virions, Inhibited by HIV RNA, and Subsequently Activated by RNase H," PLOS Pathogens, Public Library of Science, vol. 3(2), pages 1-16, February.
    8. Takahide Kouno & Satoshi Shibata & Megumi Shigematsu & Jaekyung Hyun & Tae Gyun Kim & Hiroshi Matsuo & Matthias Wolf, 2023. "Structural insights into RNA bridging between HIV-1 Vif and antiviral factor APOBEC3G," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    9. Jing Ma & Xiaoyu Li & Jian Xu & Quan Zhang & Zhenlong Liu & Pingping Jia & Jinming Zhou & Fei Guo & Xuefu You & Liyan Yu & Lixun Zhao & Jiandong Jiang & Shan Cen, 2013. "The Roles of APOBEC3G Complexes in the Incorporation of APOBEC3G into HIV-1," PLOS ONE, Public Library of Science, vol. 8(10), pages 1-9, October.
    10. Iraj Hosseini & Feilim Mac Gabhann, 2012. "Multi-Scale Modeling of HIV Infection in vitro and APOBEC3G-Based Anti-Retroviral Therapy," PLOS Computational Biology, Public Library of Science, vol. 8(2), pages 1-17, February.
    11. Weijing Yang & Hong Wang & Zhaolong Li & Lihua Zhang & Jianhui Liu & Frank Kirchhoff & Chen Huan & Wenyan Zhang, 2024. "RPLP1 restricts HIV-1 transcription by disrupting C/EBPβ binding to the LTR," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    12. Hanjing Yang & Josue Pacheco & Kyumin Kim & Ayub Bokani & Fumiaki Ito & Diako Ebrahimi & Xiaojiang S. Chen, 2024. "Molecular mechanism for regulating APOBEC3G DNA editing function by the non-catalytic domain," Nature Communications, Nature, vol. 15(1), pages 1-19, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:418:y:2002:i:6898:d:10.1038_nature00939. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.