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Scaffolding viral protein NC nucleates phase separation of the HIV-1 biomolecular condensate

  1. Author:
    Monette, Anne
    Niu, Meijuan
    Nijhoff Asser, Maya
    Gorelick,Robert
    Mouland, Andrew J

  2. Author Address

    HIV-1 RNA Trafficking Lab, Lady Davis Institute at the Jewish General Hospital, Montreal, Quebec H3T 1E2, Canada. Electronic address: anne.monette@mail.mcgill.ca., HIV-1 RNA Trafficking Lab, Lady Davis Institute at the Jewish General Hospital, Montreal, Quebec H3T 1E2, Canada; Department of Microbiology and Immunology, McGill University, Montreal, Quebec H3A 2B4, Canada., AIDS and Cancer Virus Program, Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research, Frederick, MD 21701, USA., HIV-1 RNA Trafficking Lab, Lady Davis Institute at the Jewish General Hospital, Montreal, Quebec H3T 1E2, Canada; Department of Microbiology and Immunology, McGill University, Montreal, Quebec H3A 2B4, Canada; Department of Medicine, McGill University, Montreal, Quebec H4A 3J1, Canada. Electronic address: andrew.mouland@mcgill.ca.,
    1. Year: 2022
    2. Date: Aug 23
  2. Journal: Cell Reports
    1. 40
    2. 8
    3. Pages: 111251
  4. Type of Article: Article
  5. Article Number: 111251
  1. Abstract:

    Membraneless biomolecular condensates (BMCs) contribute to the replication of a growing number of viruses but remain to be functionally characterized. Previously, we demonstrated that pan-retroviral nucleocapsid (NC) proteins phase separated into condensates regulating virus assembly. Here we discover that intrinsically disordered human immunodeficiency virus-type 1 (HIV-1) core proteins condense with the viral genomic RNA (vRNA) to assemble as BMCs attaining a geometry characteristic of viral reverse transcription complexes. We explore the predisposition, mechanisms, and pharmacologic sensitivity of HIV-1 core BMCs in living cells. HIV-1 vRNA-interacting NC condensates were found to be scaffolds onto which client capsid, reverse transcriptase, and integrase condensates assemble. HIV-1 core BMCs exhibit fundamental characteristics of BMCs and are drug-sensitive. Lastly, protease-mediated maturation of Gag and Gag-Pol precursor proteins yield abundant and visible BMCs in cells. This study redefines HIV-1 core components as fluid BMCs and advances our understanding of the nature of viral cores during ingress. Copyright © 2022 The Author(s). Published by Elsevier Inc. All rights reserved.

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External Sources

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  2. DOI: 10.1016/j.celrep.2022.111251
  3. PMID: 36001979
  4. PII : S2211-1247(22)01069-5

Library Notes

  1. Fiscal Year: FY2021-2022
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