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

Jiying Ning, Gonca Erdemci-Tandogan, Ernest L. Yufenyuy, Jef Wagner, Benjamin A. Himes, Gongpu Zhao, Christopher Aiken, Roya Zandi () and Peijun Zhang ()
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Jiying Ning: 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
Christopher Aiken: Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine
Roya Zandi: University of California
Peijun Zhang: University of Pittsburgh School of Medicine

Nature Communications, 2016, vol. 7, issue 1, 1-12

Abstract: 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.

Date: 2016
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DOI: 10.1038/ncomms13689

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