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HIV-1 Nef promotes infection by excluding SERINC5 from virion incorporation

Author

Listed:
  • Annachiara Rosa

    (University of Trento, Centre for Integrative Biology)

  • Ajit Chande

    (University of Trento, Centre for Integrative Biology)

  • Serena Ziglio

    (University of Trento, Centre for Integrative Biology)

  • Veronica De Sanctis

    (University of Trento, Laboratory of Biomolecular Sequence and Structure Analysis for Health, NGS facility)

  • Roberto Bertorelli

    (University of Trento, Laboratory of Biomolecular Sequence and Structure Analysis for Health, NGS facility)

  • Shih Lin Goh

    (University of Massachusetts Medical School, Program in Molecular Medicine)

  • Sean M. McCauley

    (University of Massachusetts Medical School, Program in Molecular Medicine)

  • Anetta Nowosielska

    (University of Massachusetts Medical School, Program in Molecular Medicine)

  • Stylianos E. Antonarakis

    (University of Geneva
    iGE3 Institute of Genetics and Genomics of Geneva)

  • Jeremy Luban

    (University of Massachusetts Medical School, Program in Molecular Medicine)

  • Federico Andrea Santoni

    (University of Geneva)

  • Massimo Pizzato

    (University of Trento, Centre for Integrative Biology)

Abstract

HIV-1 Nef, a protein important for the development of AIDS, has well-characterized effects on host membrane trafficking and receptor downregulation. By an unidentified mechanism, Nef increases the intrinsic infectivity of HIV-1 virions in a host-cell-dependent manner. Here we identify the host transmembrane protein SERINC5, and to a lesser extent SERINC3, as a potent inhibitor of HIV-1 particle infectivity that is counteracted by Nef. SERINC5 localizes to the plasma membrane, where it is efficiently incorporated into budding HIV-1 virions and impairs subsequent virion penetration of susceptible target cells. Nef redirects SERINC5 to a Rab7-positive endosomal compartment and thereby excludes it from HIV-1 particles. The ability to counteract SERINC5 was conserved in Nef encoded by diverse primate immunodeficiency viruses, as well as in the structurally unrelated glycosylated Gag from murine leukaemia virus. These examples of functional conservation and convergent evolution emphasize the fundamental importance of SERINC5 as a potent anti-retroviral factor.

Suggested Citation

  • Annachiara Rosa & Ajit Chande & Serena Ziglio & Veronica De Sanctis & Roberto Bertorelli & Shih Lin Goh & Sean M. McCauley & Anetta Nowosielska & Stylianos E. Antonarakis & Jeremy Luban & Federico And, 2015. "HIV-1 Nef promotes infection by excluding SERINC5 from virion incorporation," Nature, Nature, vol. 526(7572), pages 212-217, October.
    • Handle: RePEc:nat:nature:v:526:y:2015:i:7572:d:10.1038_nature15399
    DOI: 10.1038/nature15399
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    Cited by:

    1. Sunan Li & Rongrong Li & Iqbal Ahmad & Xiaomeng Liu & Silas F. Johnson & Liangliang Sun & Yong-Hui Zheng, 2022. "Cul3-KLHL20 E3 ubiquitin ligase plays a key role in the arms race between HIV-1 Nef and host SERINC5 restriction," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    2. Caterina Prelli Bozzo & Alexandre Laliberté & Aurora De Luna & Chiara Pastorio & Kerstin Regensburger & Stefan Krebs & Alexander Graf & Helmut Blum & Meta Volcic & Konstantin M. J. Sparrer & Frank Kir, 2024. "Replication competent HIV-guided CRISPR screen identifies antiviral factors including targets of the accessory protein Nef," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    3. Susan A. Leonhardt & Michael D. Purdy & Jonathan R. Grover & Ziwei Yang & Sandra Poulos & William E. McIntire & Elizabeth A. Tatham & Satchal K. Erramilli & Kamil Nosol & Kin Kui Lai & Shilei Ding & M, 2023. "Antiviral HIV-1 SERINC restriction factors disrupt virus membrane asymmetry," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    4. Uddhav Timilsina & Supawadee Umthong & Emily B. Ivey & Brandon Waxman & Spyridon Stavrou, 2022. "SARS-CoV-2 ORF7a potently inhibits the antiviral effect of the host factor SERINC5," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

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