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In vitro protease cleavage and computer simulations reveal the HIV-1 capsid maturation pathway

Author

Listed:
  • Jiying Ning

    (University of Pittsburgh School of Medicine
    Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine)

  • Gonca Erdemci-Tandogan

    (University of California)

  • Ernest L. Yufenyuy

    (Microbiology and Immunology, Vanderbilt University Medical Center)

  • Jef Wagner

    (University of California)

  • Benjamin A. Himes

    (University of Pittsburgh School of Medicine)

  • Gongpu Zhao

    (University of Pittsburgh School of Medicine
    Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine)

  • Christopher Aiken

    (Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine
    Microbiology and Immunology, Vanderbilt University Medical Center)

  • Roya Zandi

    (University of California)

  • Peijun Zhang

    (University of Pittsburgh School of Medicine
    Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine
    University of Oxford, The Henry Wellcome Building for Genomic Medicine
    Electron Bio-Imaging Centre, Diamond Light Sources, Harwell Science and Innovation Campus)

Abstract

HIV-1 virions assemble as immature particles containing Gag polyproteins that are processed by the viral protease into individual components, resulting in the formation of mature infectious particles. There are two competing models for the process of forming the mature HIV-1 core: the disassembly and de novo reassembly model and the non-diffusional displacive model. To study the maturation pathway, we simulate HIV-1 maturation in vitro by digesting immature particles and assembled virus-like particles with recombinant HIV-1 protease and monitor the process with biochemical assays and cryoEM structural analysis in parallel. Processing of Gag in vitro is accurate and efficient and results in both soluble capsid protein and conical or tubular capsid assemblies, seemingly converted from immature Gag particles. Computer simulations further reveal probable assembly pathways of HIV-1 capsid formation. Combining the experimental data and computer simulations, our results suggest a sequential combination of both displacive and disassembly/reassembly processes for HIV-1 maturation.

Suggested Citation

  • Jiying Ning & Gonca Erdemci-Tandogan & Ernest L. Yufenyuy & Jef Wagner & Benjamin A. Himes & Gongpu Zhao & Christopher Aiken & Roya Zandi & Peijun Zhang, 2016. "In vitro protease cleavage and computer simulations reveal the HIV-1 capsid maturation pathway," Nature Communications, Nature, vol. 7(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13689
    DOI: 10.1038/ncomms13689
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    Cited by:

    1. Anna-Sophia Krebs & Hsuan-Fu Liu & Ye Zhou & Juan S. Rey & Lev Levintov & Juan Shen & Andrew Howe & Juan R. Perilla & Alberto Bartesaghi & Peijun Zhang, 2023. "Molecular architecture and conservation of an immature human endogenous retrovirus," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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